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Information on EC 3.4.24.35 - gelatinase B
for references in articles please use BRENDA:EC3.4.24.35
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EC Tree 3 Hydrolases
3.4 Acting on peptide bonds (peptidases)
3.4.24 Metalloendopeptidases
3.4.24.35 gelatinase B
IUBMB Comments
Similar to gelatinase A, but possesses a further domain . In peptidase family M10 (interstitial collagenase family)
The enzyme appears in viruses and cellular organisms
- 3.4.24.35
- mmp-2
- metalloproteinases
-
zymography
- metastasis
- timp-1
- endothelial
- necrosis
- angiogenesis
- tnf
- artery
- fibrosis
- neutrophil
- chemokine
- infarct
- plaque
- monocyte
- vessel
- pulmonary
- myocardial
- cerebral
- mapks
- stroke
- erk
-
transwell
-
basement
- aortic
-
invasiveness
- plasminogen
-
blood-brain
- matrigel
- bcl-2
- nf-kappab
- airway
- upa
- osteoclast
- cox-2
- fibronectin
- aneurysm
-
c-reactive
- mt1-mmp
- e-cadherin
- coronary
- tnf-alpha
-
angiogenic
- atherosclerotic
-
anti-metastatic
-
tartrate-resistant
-
urokinase-type
- drug development
- diagnostics
- elastin
- rankl
- medicine
showSynonyms
mmp-9, matrix metalloproteinase-9, matrix metalloproteinase 9, gelatinase b, matrix metallopeptidase 9, matrix metalloprotease-9, mmp 9, 92-kda gelatinase, 92 kda gelatinase, 92-kda type iv collagenase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
92 kDa gelatinase
92-kDa Gelatinase
-
-
-
-
92-kDa gelatinase B
92-kDa Type IV collagenase
95 kDa type IV collagenase/gelatinase
-
-
-
-
Collagenase IV
-
-
-
-
Collagenase type IV
-
-
-
-
gelatinase
gelatinase B
Gelatinase MMP 9
-
-
-
-
GELB
-
-
-
-
Macrophage gelatinase
-
-
-
-
matrix metallopeptidase 9
Matrix metalloproteinase 9
matrix metalloproteinase-9
MMP 9
MMP-9
MMP9
Type IV collagen metalloproteinase
Type IV collagenase
Type IV collagenase/gelatinase
Type V collagenase
-
-
-
-
92 kDa gelatinase
-
-
-
-
92-kDa Type IV collagenase
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-
-
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gelatinase B
-
-
matrix metallopeptidase 9
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Matrix metalloproteinase 9
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-
-
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Matrix metalloproteinase 9
-
-
Matrix metalloproteinase 9
-
-
matrix metalloproteinase-9
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-
683114, 683233, 683429, 683458, 683485, 683512, 683518, 683579, 683749, 683844, 683881, 684069, 695655, 695947, 696967, 696980, 697075, 697548, 697747, 697751, 698149, 698261, 698353, 698359, 699092, 699222, 699345, 699642, 699656, 699932, 699939, 699946, 700527, 700536, 700539, 700581, 701178, 701192, 701274, 701316, 702513, 707146, 707366, 707452, 707631, 707654, 707953, 707964, 708020, 708070, 708086, 708088, 708089, 708144, 708170, 708171, 708198, 708232, 708245, 708409, 708548, 708773, 708775, 708784, 708810, 708814, 708820, 708828, 709051, 709277, 709288, 709301, 709302, 709336, 709413, 709574, 709613, 709619, 709700, 709811, 709819, 709880, 709919, 710077, 710091, 710174, 710177, 710225, 710245, 710452, 710531, 710542, 710557, 710584, 710587, 717349, 717503, 717522, 717898
matrix metalloproteinase-9
-
matrix metalloproteinase-9
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-
652132, 683450, 683480, 683523, 683555, 683816, 684007, 695459, 695847, 696037, 696751, 697149, 697726, 697810, 698338, 699126, 699477, 699716, 701421, 707062, 707302, 707451, 707928, 708024, 708188, 708547, 708548, 708653, 708690, 708695, 708724, 708740, 708746, 709239, 709249, 709303, 709382, 709650, 709680, 709734, 709787, 709791, 709950, 710065, 710067, 710102, 717577, 717960, 718355
matrix metalloproteinase-9
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MMP 9
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-
-
-
MMP-9
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652050, 652384, 683037, 683114, 683170, 683230, 683233, 683376, 683429, 683458, 683485, 683518, 683579, 683710, 683749, 683844, 683881, 684069, 695655, 695947, 696967, 696980, 697075, 697548, 697747, 697751, 698149, 698261, 698353, 698359, 699032, 699092, 699186, 699222, 699345, 699642, 699932, 699939, 699946, 700406, 700527, 700530, 700536, 700539, 700540, 700581, 701178, 701192, 701274, 701316, 702513, 707123, 707146, 707366, 707452, 707631, 707654, 707953, 707964, 707978, 708020, 708070, 708086, 708088, 708089, 708144, 708170, 708171, 708198, 708232, 708245, 708409, 708542, 708548, 708773, 708775, 708784, 708810, 708814, 708820, 708828, 709051, 709277, 709288, 709301, 709302, 709336, 709413, 709574, 709613, 709619, 709620, 709700, 709811, 709819, 709880, 709919, 710077, 710091, 710174, 710177, 710225, 710245, 710452, 710531, 710542, 710557, 710584, 710587, 710650, 717299, 717503, 717522, 717980, 718069, 718385
MMP-9
-
MMP-9
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652132, 683055, 683111, 683450, 683480, 683523, 683525, 683555, 683733, 683816, 684007, 695459, 695847, 696037, 696751, 697149, 697726, 697810, 698338, 699126, 699477, 699716, 701421, 707043, 707062, 707298, 707302, 707451, 707928, 708024, 708188, 708547, 708548, 708653, 708690, 708695, 708703, 708724, 708740, 708746, 709239, 709249, 709303, 709382, 709650, 709680, 709734, 709787, 709791, 709950, 710065, 710067, 710102, 717960, 718355
MMP-9
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Type IV collagen metalloproteinase
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Type IV collagenase
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Type IV collagenase/gelatinase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cleavage of gelatin types I and V and collagen types IV and V
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
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-
-
-
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CAS REGISTRY NUMBER
COMMENTARY
146480-36-6
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(7-methoxy-coumarin-4-yl)acetyl-PLGL-beta-(2,4-dinitrophenylamino)-AAR-NH2 + H2O
(7-methoxy-coumarin-4-yl)acetyl-PL + GL-beta-(2,4-dinitrophenylamino)-AAR-NH2
-
Substrates: -
Products: -
Products: -
?
(7-methoxycoumarin-4-yl)-acetyl-Pro-Leu-Gly-Leu-(3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-Ala-Arg-NH2 + H2O
?
-
Substrates: -
Products: -
Products: -
?
(7-methoxycoumarin-4-yl)acetyl-Pro-Leu-Gly-Leu-beta-(2,4-dinitrophenylamino)Ala-Ala-Arg-NH2 + H2O
?
(7-methoxycoumaryl-4yl)acetylPLGLA2pr(2,4-dinitrophenol)-AR-NH2 + H2O
?
Substrates: -
Products: -
Products: -
?
2,4-dinitrophenyl-Pro-beta-cyclohexylalanyl-Gly-Cys(Me)-His-Ala-Lys(N-Me-2-aminobenzoyl)-NH2 + H2O
?
-
Substrates: a quenched fluorogenic substrate
Products: -
Products: -
?
2,4-Dinitrophenyl-Pro-Leu-Gly-Leu-Trp-Ala-D-Arg-NH2 + H2O
2,4-Dinitrophenyl-Pro-Leu-Gly + Leu-Trp-Ala-D-Arg-NH2
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Substrates: and peptide substrates derived from, utility of substrate mapping form examining the subsite specificities and the optimization of proteinase substrates
Products: -
Products: -
?
Ac-L-Pro-L-Pro(OH)-Gly-L-Gln-Gly-L-Ala-L-Thr-Gly-L-Glu-L-Pro(OH)-Gly-NH2 + H2O
?
-
Substrates: -
Products: -
Products: -
?
ADAM 2 + H2O
?
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Substrates: putative protein substrate with potential cleavage site
Products: -
Products: -
?
betaB1 crystallin + H2O
?
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Substrates: main enzyme substrate in lens extract
Products: -
Products: -
?
CD25 + H2O
?
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Substrates: CD25 is proteolytic cleaved to its soluble form by MMP-9
Products: -
Products: -
?
dentin sialoprotein + H2O
?
Substrates: the enzyme highly efficiently cleaves dentin sialoprotein into distinct fragments in vitro, and the deletion of Mmp9 causes improper processing of dentin sialoprotein in natural teeth
Products: -
Products: -
?
desmoglein 3 + H2O
?
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Substrates: putative protein substrate with potential cleavage site
Products: -
Products: -
?
DNP-Pro-cyclohexyl-Ala-Gly-Cys(Me)-His-Ala-Lys(N-Me-Abz)-NH2 + H2O
DNP-Pro-cyclohexyl-Ala-Gly + Cys(Me)-His-Ala-Lys(N-Me-Abz)-NH2
Substrates: -
Products: -
Products: -
?
endoglin + H2O
?
-
Substrates: putative protein substrate with potential cleavage site
Products: -
Products: -
?
endothilin receptor + H2O
?
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Substrates: putative protein substrate with potential cleavage site
Products: -
Products: -
?
epididymis-specific alpha-mannosidase precursor + H2O
?
-
Substrates: -
Products: -
Products: -
?
fragments of human collagen type II + H2O
?
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Substrates: fragments obtained by cleavage with collagenases MMP-1, MMP-8, or MMP-13. Enzyme produces small remnant peptides with still intact immunodominant epitopes
Products: -
Products: -
?
integrin beta5 + H2O
?
-
Substrates: putative protein substrate with potential cleavage site
Products: -
Products: -
?
kallikrein + H2O
?
-
Substrates: putative protein substrate with potential cleavage site
Products: -
Products: -
?
L-Pro-L-Pro(OH)-Gly-L-Gln-Gly-L-Ala-L-Thr-Gly-L-Glu-L-Pro(OH)-Gly-NH2 + H2O
?
-
Substrates: -
Products: -
Products: -
?
ladinin 1 + H2O
?
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Substrates: putative protein substrate with potential cleavage site
Products: -
Products: -
?
laminin alpha3 chain + H2O
?
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Substrates: putative protein substrate with potential cleavage site
Products: -
Products: -
?
LS276-THP + H2O
?
-
Substrates: development and evaluation of an activatable NIR fluorescent probe LS276-THP for in vivo detection of cancer-related matrix metalloproteinase activity based on a triplehelical peptide substrate with high specificity for MMP-2 and MMP-9 relative to other members of the MMP family, overview. Triple-helical peptides are suitable for highly specific in vivo detection of tumor-related MMP-2 and MMP-9 activity
Products: -
Products: -
?
N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl-7-methoxycoumarin-4-yl acetyl + H2O
?
-
Substrates: -
Products: -
Products: -
?
N-alpha-benzoyl-arginine p-nitroanilide + H2O
N-alpha-benzoyl-Arg + 4-nitroaniline
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Substrates: i.e. BAPNA
Products: -
Products: -
?
Neonatal human proteoglycan + H2O
?
-
Substrates: poor substrate, cleavage of the His16-Ile17 bond
Products: -
Products: -
?
peptide m1A11 + H2O
?
-
Substrates: non-selective peptide substrate
Products: -
Products: -
?
phosphate regulating neutral endopeptidase + H2O
?
-
Substrates: putative protein substrate with potential cleavage site
Products: -
Products: -
?
retinoic acid early inducible protein 1 alpha-precursor + H2O
?
-
Substrates: -
Products: -
Products: -
?
retinoid-inducible serine carboxypeptidase precursor + H2O
?
-
Substrates: -
Products: -
Products: -
?
transforming growth factor-beta + H2O
?
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Substrates: MMP9 mediates activation of latent transforming growth factor-beta
Products: -
Products: -
?
Vitronectin + H2O
?
-
Substrates: 65000 MW and 75000 MW form of vitronectin
Products: -
Products: -
?
(7-methoxycoumarin-4-yl)acetyl-Pro-Leu-Gly-Leu-beta-(2,4-dinitrophenylamino)Ala-Ala-Arg-NH2 + H2O
?
-
Substrates: -
Products: -
Products: -
?
(7-methoxycoumarin-4-yl)acetyl-Pro-Leu-Gly-Leu-beta-(2,4-dinitrophenylamino)Ala-Ala-Arg-NH2 + H2O
?
-
Substrates: -
Products: -
Products: -
?
actin + H2O
?
Substrates: the substrate is incorporated into immune complexes
Products: -
Products: -
?
alphaB-crystallin + H2O
?
Substrates: the substrate is incorporated into immune complexes
Products: -
Products: -
?
apolipoprotein-B 100 + H2O
?
Substrates: the substrate is incorporated into immune complexes
Products: -
Products: -
?
Collagen + H2O
?
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Substrates: cleavage of the carboxyl-terminal triple helix-containing region
Products: -
Products: -
?
Collagen + H2O
?
-
Substrates: MMP-9 inhibits collagen-induced platelet aggregation
Products: -
Products: -
?
Collagen + H2O
?
-
Substrates: cleaves between residues Gly439-Val in both alpha1(V) and alpha(XI) and between residues Gly445-Leu in the alpha2(V) chain
Products: -
Products: -
?
Collagen type I + H2O
?
-
Substrates: soluble, native collagen type I, zymography
Products: -
Products: -
?
Collagen type III + H2O
?
-
Substrates: MMP-9 cleaves native, triple helical type III collagen to generate a 3/4 fragment, zymography
Products: -
Products: -
?
Elastin + H2O
?
-
Substrates: MMP-9 activity leads to elastin breakdown in an animal model of Kawasaki disease, a multisystem vasculitis leading to damage in the coronary circulationand aneurysm formation, overview
Products: -
Products: -
?
epidermal growth factor + H2O
?
-
Substrates: MMP-9 induces TGF-beta1 production in the airway epithelium through the cleavage of epidermal growth factor, EGF, and membrane-bound EGF-like ligands and activating epidermal growth factor receptor
Products: -
Products: -
?
fibrillar collagen + H2O
?
-
Substrates: degradation, MMP-9 is involved in development of osteoarthritis, overview
Products: -
Products: -
?
fibrillar collagen + H2O
?
-
Substrates: degradation, cleavage within the triple helix
Products: -
Products: -
?
Galectin-3 + H2O
?
-
Substrates: a galactoside-binding protein, major cleavage site is the Ala62-Tyr63 bond
Products: -
Products: -
?
Gelatin + H2O
?
-
Substrates: gelatin zymography, mass spectrometrical analysis, overview
Products: -
Products: -
?
Gelatin + H2O
?
-
Substrates: MMP-9 is involved in the degradation of the extracellular matrix, and is implicated in a variety of pathological conditions including cardiovascular and neoplastic diseases
Products: -
Products: -
?
Gelatin + H2O
?
-
Substrates: -
Products: -
Products: -
?
Gelatin + H2O
?
-
Substrates: gelatin zymography using gelatin and fluorescence-conjugated gelatin peptides
Products: -
Products: -
?
Gelatin + H2O
?
-
Substrates: gelatin zymography, from porcine skin
Products: -
Products: -
?
Gelatin + H2O
?
-
Substrates: gelatin zymography
Products: -
Products: -
?
Gelatin + H2O
?
-
696980, 697383, 699222, 699345, 699642, 699656, 699946, 700530, 695947, 708245, 710174, 710225, 710245, 710452, 710531, 710587, 707452, 707631, 702513, 707654, 707953, 707964, 707978, 708020, 708070, 708088, 708089, 708086, 708171, 708409, 708548, 708773, 707123, 708775, 708810, 708828, 709051, 709277, 709288, 709301, 709302, 709413, 709700, 709811, 710077, 707366, 717898, 717980, 718385
Substrates: -
Products: -
Products: -
?
Gelatin + H2O
?
-
Substrates: -
Products: -
Products: -
?
Gelatin + H2O
?
-
Substrates: gelatin zymography
Products: -
Products: -
?
Gelatin + H2O
?
-
Substrates: gelatin zymography, gelatin from porcine skin
Products: -
Products: -
?
Gelatin + H2O
?
-
699477, 696037, 696751, 707062, 708703, 707451, 707928, 708024, 708188, 708548, 708547, 708690, 708695, 708740, 708746, 709178, 709239, 709249, 709382, 707298, 709650, 709680, 709734, 709787, 709791, 707302, 709904, 710067, 710065, 710102, 717577, 718355
Substrates: -
Products: -
Products: -
?
Gelatin + H2O
?
-
Substrates: gelatin zymography, gelatin from porcine skin
Products: -
Products: -
?
Gelatin + H2O
?
-
Substrates: gelatin zymography
Products: -
Products: -
?
Gelatin + H2O
?
-
700147, 701422, 710106, 710575, 710585, 710695, 708304, 709595, 709614, 709646, 709682, 709920, 709948
Substrates: -
Products: -
Products: -
?
islet amyloid polypeptide + H2O
?
Substrates: enzyme MMP-9 degrades amyloidogenic humanislet amyloid polypeptide but not nonamyloidogenic mouse islet amyloid polypeptide
Products: -
Products: -
?
islet amyloid polypeptide + H2O
?
Substrates: enzyme MMP-9 degrades amyloidogenic human islet amyloid polypeptide but not nonamyloidogenic mouse islet amyloid polypeptide
Products: -
Products: -
?
islet amyloid polypeptide + H2O
?
Substrates: enzyme MMP-9 degrades amyloidogenic human islet amyloid polypeptide but not nonamyloidogenic mouse islet amyloid polypeptide
Products: -
Products: -
?
pro-urokinase + H2O
active urokinase + prosequence of urokinase
-
Substrates: -
Products: -
Products: -
?
pro-urokinase + H2O
active urokinase + prosequence of urokinase
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: active host MMP-9 is expressed in walls and fluids of hydatid cysts of parasite Echinococcus granulosus in the environment of granulomatous reaction, in vivo activation of MMP-9 suggests its involvement in inflammatory reaction and in the chemotaxis of inflammatory cells to the cyst. However, the parasite can deal efficiently with MMP-9, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: prefers hydrophobic aliphatic residues in subsite P1'
Products: -
Products: -
?
additional information
?
-
-
Substrates: Asp432, Asp433, and His400 residues are important for the activity of gelatinase B, His400 may act as a zinc-binding ligand, Asp432 and Asp433 are probably involved in stabilization of the active site of the enzyme
Products: -
Products: -
?
additional information
?
-
-
Substrates: tolerates only small amino acids such as Gly and Ala in P1
Products: -
Products: -
?
additional information
?
-
Substrates: associated with degradation of the extracellular matrix in normal and pathological conditions
Products: -
Products: -
?
additional information
?
-
-
Substrates: central role in the degradation of the extracellular matrix
Products: -
Products: -
?
additional information
?
-
-
Substrates: leading role in the catabolism of the macromolecular components of the extracellular matrix in a variety of normal and pathological processes, involved in inflammation, tissue remodeling and cancer
Products: -
Products: -
?
additional information
?
-
-
Substrates: may be responsible for the pathological degradation and/or normal turnover of vitronectin
Products: -
Products: -
?
additional information
?
-
-
Substrates: possible role of the enzyme in the structural tissue remodeling of the developing embryo
Products: -
Products: -
?
additional information
?
-
-
Substrates: plays a role in tumor cell invasion and in destruction of cartilage in arthritis
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme may play a role in the destruction of the extracellular matrix, perhaps acting in concert with the metalloproteases produced by activated endothelial cells
Products: -
Products: -
?
additional information
?
-
-
Substrates: cells resistant to protein kinase C potentiated, transkription factor p53 mediated apoptosis express a higher level of matrix metalloproteinases MMP-9 and MMP-10. Matrix metalloproteinases function confers protection from protein kinase C/p53 induced apoptosis and are implicated in tumor cell resistance
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme and leucocyte elastase are essential for granulocyte-mediated proteolysis resulting in dermal-epidermal separation in epidermolysis bullosa acquisita and bullous pemphigoid patients skin
Products: -
Products: -
?
additional information
?
-
-
Substrates: collagen binding domains of matrix metalloproteinases MMP-2 and MMP-9 bind the same or closely positioned sites on type I collagen
Products: -
Products: -
?
additional information
?
-
-
Substrates: no substrate: L-Pro-L-Pro(OH)-Gly-L-Gln-Gly-L-Ala(CH3)-L-Thr-Gly-L-Glu-L-Pro(OH)-Gly-CONH2
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is involved in breakdown of extracellular matrix components, and basement membrane disruption, stroma and blood vessel penetration, and metastasis. It participates in tumor growth and angiogensis, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: MMP-9 expression is increased in cancers, inhibition of MMP-9 has a therapeutic benefit to cancer
Products: -
Products: -
?
additional information
?
-
-
Substrates: MMP-9 is activated by monomeric hemin and by MMP-3 cleaving at Glu40-Met41 and Arg87-Phe88, and at Glu40-Met41 and Leu52-Leu53, respectively, no effect by hemoglobin, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: MMP-9 is secreted by macrophages at wound sites and is involved in wound repair together with relaxin, molecular mechanism, overview. Transcription factor NF-kappaB is important in MMP gene regulation in macrophage cells, overview, relaxin-induced tissue remodeling through increasing MMP-9 expression is dependent on NF-kappaB activation
Products: -
Products: -
?
additional information
?
-
-
Substrates: activation of MMP-9 may contribute to dentin matrix degradation, which occurs during caries progression and follows resin bonding. Inhibition of MMP-9 proteolytic activity may slow caries progression and increase the durability of resin-dentin bond, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: gelatinase B expression is a prognostic factor in patients with stage II/III rectal carcinoma treated by postoperative adjuvant therapy, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: MMP-9 activity is associated with poor prognosis in T3-T4 node-negative colorectal cancer, its expression is not correlated with MMP-2 and reversion-inducing cysteine-rich protein, RECK, expression in cancer cells, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: MMP-9 is involved in development of endometriosis, MMP-9 levels are decreased by about 50% after operation of endometriosis, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: activated MMP-9 initially induces conformational changes in platelet membranes, affecting membrane fluidity, and hydroxyl radical formation and inhibits the Na+/H+ pump, both leading to inhibition of platelet aggregation, the latter via reduced Ca2+ mobilization, overview. MMP-9 also inhibits arachidonic acid, ADP, and U46619 inducetion of platelet aggregation, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: varied enzyme conformations and in facilitating independent movements of the terminal domains may endorse recognition, binding, and processing of substrates, ligands, as well as receptors and marks this domain as an additional target for the design of selective regulators, overview
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme cleaves many substrates
Products: -
Products: -
?
additional information
?
-
Substrates: 4-aminophenylmercuric acetate activation induces an autoproteolytic activation of the enzyme zymogen causing the removal of the propeptide followed by a further breakage and subsequent formation of a N- and C-truncated form of 67 kDa
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme activity is determined using human teeth as substrate
Products: -
Products: -
?
additional information
?
-
Substrates: autoantigens incorporated into immune complexes, but not immunoglobulin heavy or light chains, are cleaved by MMP-9. Active MMP-9 cleaves autoantigens in immune complexes and dissolves human SLE immune complexes
Products: -
Products: -
-
additional information
?
-
-
Substrates: peptide A16 SGRR LLSRTA and peptide C11 SGRR LIHHTA are no substrates
Products: -
Products: -
?
additional information
?
-
-
Substrates: MMP-9 is essential for neutrophil infiltration during zymosan peritonitis
Products: -
Products: -
?
additional information
?
-
-
Substrates: acrolein subtypes A and C from cigarette smoke induces persistent mucin production via activation of matrix metalloproteinase 9 through induction of pro-MMP-9 cleavage and activation and EGFR/MAPK signaling also leading to MMP-9 activation, regulation, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: gastric gelatinase B is rapidly increased in Helicobacter felis-infected mice and is involved in induction of gastritis
Products: -
Products: -
?
additional information
?
-
-
Substrates: MMP-9 activity plays a central role in modulating the clinical course and severity of respiratory tularemia, Pro-Gly-Pro, a potent neutrophil chemotactic tripeptide, is released from extracellular matrix through the action of MMP-9, MMP-9 is involved in leukocyte recruitment, pulmonary infection with the Gram-negative intracellular bacterium Francisella tularensis, a category A biological threat agent, induces MMP-9 expression, MMP-9 is associated with higher bacterial burdens in pulmonary and extrapulmonary tissues, development of more extensive histopathology predominated by neutrophils, and increased morbidity and mortality compared to mice lacking MMP-9
Products: -
Products: -
?
additional information
?
-
-
Substrates: MMP-9 plays an important role in degradation of gastric extracellular matrix proteins, MMP-9 is reduced by melatonin produced during gastric ulcer development, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: nitric oxide regulates matrix metalloproteinase-9 activity by guanylyl-cyclase-dependent and -independent pathways, Sper/NO shows biphasic regulation of MMP-9 inactivated macrophages, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: MMP-9 inhibitor completely inhibits PAF-induced B16F10 metastasis
Products: -
Products: -
?
additional information
?
-
-
Substrates: MMP-9 is involved in murine peritonitis by participating in cellular migration, molecular mechanism, overview
Products: -
Products: -
?
additional information
?
-
Substrates: autoantigens incorporated into immune complexes, but not immunoglobulin heavy or light chains, are cleaved by MMP-9
Products: -
Products: -
-
additional information
?
-
-
Substrates: MMP-9 plays an important role in degradation of gastric extracellular matrix proteins, MMP-9 is reduced by melatonin produced during gastric ulcer development, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: MMP-9 is involved in murine peritonitis by participating in cellular migration, molecular mechanism, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: MMP-9 is essential for neutrophil infiltration during zymosan peritonitis
Products: -
Products: -
?
additional information
?
-
-
Substrates: gastric gelatinase B is rapidly increased in Helicobacter felis-infected mice and is involved in induction of gastritis
Products: -
Products: -
?
additional information
?
-
-
Substrates: nitric oxide regulates matrix metalloproteinase-9 activity by guanylyl-cyclase-dependent and -independent pathways, Sper/NO shows biphasic regulation of MMP-9 inactivated macrophages, overview
Products: -
Products: -
?
additional information
?
-
Substrates: autoantigens incorporated into immune complexes, but not immunoglobulin heavy or light chains, are cleaved by MMP-9
Products: -
Products: -
-
additional information
?
-
-
Substrates: MMP-9 activity plays a central role in modulating the clinical course and severity of respiratory tularemia, Pro-Gly-Pro, a potent neutrophil chemotactic tripeptide, is released from extracellular matrix through the action of MMP-9, MMP-9 is involved in leukocyte recruitment, pulmonary infection with the Gram-negative intracellular bacterium Francisella tularensis, a category A biological threat agent, induces MMP-9 expression, MMP-9 is associated with higher bacterial burdens in pulmonary and extrapulmonary tissues, development of more extensive histopathology predominated by neutrophils, and increased morbidity and mortality compared to mice lacking MMP-9
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme may be necessary for initiating or completing degradation of type I/type V copolymeric fibrils for growth and remodeling of extracellular collagen
Products: -
Products: -
?
additional information
?
-
-
Substrates: independent of its proteolytic function, enzyme has a biphasic effect on smooth muscle cell-mediated collagen gel contraction
Products: -
Products: -
?
additional information
?
-
-
Substrates: astrocyte-released MMP-9 is involved in interleukin-1beta induced neurotoxicity, probably via urokinase plasminogen activator, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: inhibition of MMP-9 prevents neutrophilic inflammation in ventilator-induced lung injury, VILI, and pulmonary hemorrhage, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: myogenic reactivity, inhibited in small renal arteries isolated from nonpregnant rats treated with recombinant human relaxin, is completely restored by incubation with MMP-9, MMP-9 rather than MMP-2 plays a central role in the vasodilatory effect of short-term relaxin administration, overview
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
actin + H2O
?
Substrates: the substrate is incorporated into immune complexes
Products: -
Products: -
?
alphaB-crystallin + H2O
?
Substrates: the substrate is incorporated into immune complexes
Products: -
Products: -
?
dentin sialoprotein + H2O
?
Substrates: the enzyme highly efficiently cleaves dentin sialoprotein into distinct fragments in vitro, and the deletion of Mmp9 causes improper processing of dentin sialoprotein in natural teeth
Products: -
Products: -
?
epidermal growth factor + H2O
?
-
Substrates: MMP-9 induces TGF-beta1 production in the airway epithelium through the cleavage of epidermal growth factor, EGF, and membrane-bound EGF-like ligands and activating epidermal growth factor receptor
Products: -
Products: -
?
transforming growth factor-beta + H2O
?
-
Substrates: MMP9 mediates activation of latent transforming growth factor-beta
Products: -
Products: -
?
apolipoprotein-B 100 + H2O
?
Substrates: the substrate is incorporated into immune complexes
Products: -
Products: -
?
Collagen + H2O
?
-
Substrates: MMP-9 inhibits collagen-induced platelet aggregation
Products: -
Products: -
?
Elastin + H2O
?
-
Substrates: MMP-9 activity leads to elastin breakdown in an animal model of Kawasaki disease, a multisystem vasculitis leading to damage in the coronary circulationand aneurysm formation, overview
Products: -
Products: -
?
fibrillar collagen + H2O
?
-
Substrates: degradation, MMP-9 is involved in development of osteoarthritis, overview
Products: -
Products: -
?
Gelatin + H2O
?
-
Substrates: MMP-9 is involved in the degradation of the extracellular matrix, and is implicated in a variety of pathological conditions including cardiovascular and neoplastic diseases
Products: -
Products: -
?
Gelatin + H2O
?
-
Substrates: -
Products: -
Products: -
?
Gelatin + H2O
?
-
Substrates: -
Products: -
Products: -
?
islet amyloid polypeptide + H2O
?
Substrates: enzyme MMP-9 degrades amyloidogenic humanislet amyloid polypeptide but not nonamyloidogenic mouse islet amyloid polypeptide
Products: -
Products: -
?
islet amyloid polypeptide + H2O
?
Substrates: enzyme MMP-9 degrades amyloidogenic human islet amyloid polypeptide but not nonamyloidogenic mouse islet amyloid polypeptide
Products: -
Products: -
?
islet amyloid polypeptide + H2O
?
Substrates: enzyme MMP-9 degrades amyloidogenic human islet amyloid polypeptide but not nonamyloidogenic mouse islet amyloid polypeptide
Products: -
Products: -
?
pro-urokinase + H2O
active urokinase + prosequence of urokinase
-
Substrates: -
Products: -
Products: -
?
pro-urokinase + H2O
active urokinase + prosequence of urokinase
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: active host MMP-9 is expressed in walls and fluids of hydatid cysts of parasite Echinococcus granulosus in the environment of granulomatous reaction, in vivo activation of MMP-9 suggests its involvement in inflammatory reaction and in the chemotaxis of inflammatory cells to the cyst. However, the parasite can deal efficiently with MMP-9, overview
Products: -
Products: -
?
additional information
?
-
Substrates: associated with degradation of the extracellular matrix in normal and pathological conditions
Products: -
Products: -
?
additional information
?
-
-
Substrates: central role in the degradation of the extracellular matrix
Products: -
Products: -
?
additional information
?
-
-
Substrates: leading role in the catabolism of the macromolecular components of the extracellular matrix in a variety of normal and pathological processes, involved in inflammation, tissue remodeling and cancer
Products: -
Products: -
?
additional information
?
-
-
Substrates: may be responsible for the pathological degradation and/or normal turnover of vitronectin
Products: -
Products: -
?
additional information
?
-
-
Substrates: possible role of the enzyme in the structural tissue remodeling of the developing embryo
Products: -
Products: -
?
additional information
?
-
-
Substrates: plays a role in tumor cell invasion and in destruction of cartilage in arthritis
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme may play a role in the destruction of the extracellular matrix, perhaps acting in concert with the metalloproteases produced by activated endothelial cells
Products: -
Products: -
?
additional information
?
-
-
Substrates: cells resistant to protein kinase C potentiated, transkription factor p53 mediated apoptosis express a higher level of matrix metalloproteinases MMP-9 and MMP-10. Matrix metalloproteinases function confers protection from protein kinase C/p53 induced apoptosis and are implicated in tumor cell resistance
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme and leucocyte elastase are essential for granulocyte-mediated proteolysis resulting in dermal-epidermal separation in epidermolysis bullosa acquisita and bullous pemphigoid patients skin
Products: -
Products: -
?
additional information
?
-
-
Substrates: collagen binding domains of matrix metalloproteinases MMP-2 and MMP-9 bind the same or closely positioned sites on type I collagen
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is involved in breakdown of extracellular matrix components, and basement membrane disruption, stroma and blood vessel penetration, and metastasis. It participates in tumor growth and angiogensis, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: MMP-9 expression is increased in cancers, inhibition of MMP-9 has a therapeutic benefit to cancer
Products: -
Products: -
?
additional information
?
-
-
Substrates: MMP-9 is activated by monomeric hemin and by MMP-3 cleaving at Glu40-Met41 and Arg87-Phe88, and at Glu40-Met41 and Leu52-Leu53, respectively, no effect by hemoglobin, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: MMP-9 is secreted by macrophages at wound sites and is involved in wound repair together with relaxin, molecular mechanism, overview. Transcription factor NF-kappaB is important in MMP gene regulation in macrophage cells, overview, relaxin-induced tissue remodeling through increasing MMP-9 expression is dependent on NF-kappaB activation
Products: -
Products: -
?
additional information
?
-
-
Substrates: activation of MMP-9 may contribute to dentin matrix degradation, which occurs during caries progression and follows resin bonding. Inhibition of MMP-9 proteolytic activity may slow caries progression and increase the durability of resin-dentin bond, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: gelatinase B expression is a prognostic factor in patients with stage II/III rectal carcinoma treated by postoperative adjuvant therapy, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: MMP-9 activity is associated with poor prognosis in T3-T4 node-negative colorectal cancer, its expression is not correlated with MMP-2 and reversion-inducing cysteine-rich protein, RECK, expression in cancer cells, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: MMP-9 is involved in development of endometriosis, MMP-9 levels are decreased by about 50% after operation of endometriosis, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: activated MMP-9 initially induces conformational changes in platelet membranes, affecting membrane fluidity, and hydroxyl radical formation and inhibits the Na+/H+ pump, both leading to inhibition of platelet aggregation, the latter via reduced Ca2+ mobilization, overview. MMP-9 also inhibits arachidonic acid, ADP, and U46619 inducetion of platelet aggregation, overview
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme cleaves many substrates
Products: -
Products: -
?
additional information
?
-
Substrates: autoantigens incorporated into immune complexes, but not immunoglobulin heavy or light chains, are cleaved by MMP-9. Active MMP-9 cleaves autoantigens in immune complexes and dissolves human SLE immune complexes
Products: -
Products: -
-
additional information
?
-
-
Substrates: MMP-9 is essential for neutrophil infiltration during zymosan peritonitis
Products: -
Products: -
?
additional information
?
-
-
Substrates: acrolein subtypes A and C from cigarette smoke induces persistent mucin production via activation of matrix metalloproteinase 9 through induction of pro-MMP-9 cleavage and activation and EGFR/MAPK signaling also leading to MMP-9 activation, regulation, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: gastric gelatinase B is rapidly increased in Helicobacter felis-infected mice and is involved in induction of gastritis
Products: -
Products: -
?
additional information
?
-
-
Substrates: MMP-9 activity plays a central role in modulating the clinical course and severity of respiratory tularemia, Pro-Gly-Pro, a potent neutrophil chemotactic tripeptide, is released from extracellular matrix through the action of MMP-9, MMP-9 is involved in leukocyte recruitment, pulmonary infection with the Gram-negative intracellular bacterium Francisella tularensis, a category A biological threat agent, induces MMP-9 expression, MMP-9 is associated with higher bacterial burdens in pulmonary and extrapulmonary tissues, development of more extensive histopathology predominated by neutrophils, and increased morbidity and mortality compared to mice lacking MMP-9
Products: -
Products: -
?
additional information
?
-
-
Substrates: MMP-9 plays an important role in degradation of gastric extracellular matrix proteins, MMP-9 is reduced by melatonin produced during gastric ulcer development, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: nitric oxide regulates matrix metalloproteinase-9 activity by guanylyl-cyclase-dependent and -independent pathways, Sper/NO shows biphasic regulation of MMP-9 inactivated macrophages, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: MMP-9 inhibitor completely inhibits PAF-induced B16F10 metastasis
Products: -
Products: -
?
additional information
?
-
-
Substrates: MMP-9 is involved in murine peritonitis by participating in cellular migration, molecular mechanism, overview
Products: -
Products: -
?
additional information
?
-
Substrates: autoantigens incorporated into immune complexes, but not immunoglobulin heavy or light chains, are cleaved by MMP-9
Products: -
Products: -
-
additional information
?
-
-
Substrates: MMP-9 plays an important role in degradation of gastric extracellular matrix proteins, MMP-9 is reduced by melatonin produced during gastric ulcer development, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: MMP-9 is involved in murine peritonitis by participating in cellular migration, molecular mechanism, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: MMP-9 is essential for neutrophil infiltration during zymosan peritonitis
Products: -
Products: -
?
additional information
?
-
-
Substrates: gastric gelatinase B is rapidly increased in Helicobacter felis-infected mice and is involved in induction of gastritis
Products: -
Products: -
?
additional information
?
-
-
Substrates: nitric oxide regulates matrix metalloproteinase-9 activity by guanylyl-cyclase-dependent and -independent pathways, Sper/NO shows biphasic regulation of MMP-9 inactivated macrophages, overview
Products: -
Products: -
?
additional information
?
-
Substrates: autoantigens incorporated into immune complexes, but not immunoglobulin heavy or light chains, are cleaved by MMP-9
Products: -
Products: -
-
additional information
?
-
-
Substrates: MMP-9 activity plays a central role in modulating the clinical course and severity of respiratory tularemia, Pro-Gly-Pro, a potent neutrophil chemotactic tripeptide, is released from extracellular matrix through the action of MMP-9, MMP-9 is involved in leukocyte recruitment, pulmonary infection with the Gram-negative intracellular bacterium Francisella tularensis, a category A biological threat agent, induces MMP-9 expression, MMP-9 is associated with higher bacterial burdens in pulmonary and extrapulmonary tissues, development of more extensive histopathology predominated by neutrophils, and increased morbidity and mortality compared to mice lacking MMP-9
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme may be necessary for initiating or completing degradation of type I/type V copolymeric fibrils for growth and remodeling of extracellular collagen
Products: -
Products: -
?
additional information
?
-
-
Substrates: independent of its proteolytic function, enzyme has a biphasic effect on smooth muscle cell-mediated collagen gel contraction
Products: -
Products: -
?
additional information
?
-
-
Substrates: astrocyte-released MMP-9 is involved in interleukin-1beta induced neurotoxicity, probably via urokinase plasminogen activator, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: inhibition of MMP-9 prevents neutrophilic inflammation in ventilator-induced lung injury, VILI, and pulmonary hemorrhage, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: myogenic reactivity, inhibited in small renal arteries isolated from nonpregnant rats treated with recombinant human relaxin, is completely restored by incubation with MMP-9, MMP-9 rather than MMP-2 plays a central role in the vasodilatory effect of short-term relaxin administration, overview
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Zn2+
additional information
the MMP-9 is an enzyme of the metalloproteinase group and particularly zinc (Zn2+) and calcium (Ca2+) dependent
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2E)-3-(N-hydroxycarbamoyl)-2-(3-phenylpropylidene)propionyl-L-tryptophan-N-methylamide
-
-
(2E)-3-(N-hydroxycarbamoyl)-2-heptylidenepropionyl-L-tryptophan-N-methylamide
-
-
(2E)-3-(N-hydroxycarbamoyl)-2-[(2E)-3-phenylprop-2-en-1-ylidene]propionyl-L-tryptophan-N-methylamide
-
-
(2E)-3-(N-hydroxycarbamoyl)-2-[(2E)-but-2-en-1-ylidene]propionyl-L-tryptophan-N-methylamide
-
-
(R)-2-(N-((6-fluoropyridin-3-yl)methyl)-4-methoxyphenyl-sulfonamido)-N-hydroxy-3-methylbutanamide
-
-
(S)-2,6-bis[(2,3-dihydroxybenzoyl)amino]hexanoamide
-
shows 33% inhibition against MMP-9 at 0.00025 mM
(S)-2-benzoylamino-6-[(2,3-dihydroxybenzoyl)amino]-hexanoic acid methyl ester
-
-
(S)-6-benzoylamino-2-[(2,3-dihydroxybenzoyl)amino]-hexanoic acid methyl ester
-
-
2-[(biphenyl-4-ylsulfonyl)(isobutyl)amino]-N-hydroxyacetamide
-
50% inhibition at 34 nM, comparison with inhibitory effect on matrix metalloproteinases MMP-3, MMp-7, MMP-2
3',4'-di-O-methylbutin-7-O-[(6''->1''')-3''',11'''-dimethyl-7'''-methylenedodeca-3''',10'''-dienyl]-beta-D-glucopyranoside
-
0.0065-0.0259 mM suppresses MMP-9 activity in lipopolysaccharide-stimulated human monocytic cells without cytotoxicity
3',4'-di-O-methylquercetin-7-O-[(4''->13''')-2''',6''',10''',14'''-tetramethylhexadec-13'''-ol-14'''-enyl]-beta-D-glucopyranoside
-
0.0065-0.0259 mM suppresses MMP-9 activity in lipopolysaccharide-stimulated human monocytic cells without cytotoxicity
4'-O-methylbutin-7-O-[(6->1''')-3''',11'''-dimethyl-7'''-hydroxymethylenedodecanyl]-beta-D-glucopyranoside
-
0.0065-0.0259 mM suppresses MMP-9 activity in lipopolysaccharide-stimulated human monocytic cells without cytotoxicity
4'-O-methylkaempferol-3-O-[(4''->13''')-2''',6''',10''',14'''-tetramethylhexadecan-13'''-olyl]-beta-D-glucopyranoside
-
0.0065-0.0259 mM suppresses MMP-9 activity in lipopolysaccharide-stimulated human monocytic cells without cytotoxicity
5-(1,5-dihydroxypentan-3-yl)-5-(4-phenoxyphenyl)pyrimidine-2,4,6(1H,3H,5H)-trione
-
-
5-(4-hydroxybutan-2-yl)-5-(4-phenoxyphenyl)pyrimidine-2,4,6(1H,3H,5H)-trione
-
-
5-(4-phenoxyphenyl)-5-(3-(1-nitrooxy-methyl)piperidin-1-yl)-pyrimidine-2,4,6(1H,3H,5H)-trione
-
-
5-(4-phenoxyphenyl)-5-(4-(1-nitrooxy-ethyl)piperidin-1-yl)-pyrimidine-2,4,6(1H,3H,5H)-trione
-
-
5-(4-phenoxyphenyl)-5-(4-(2-nitrooxy-ethyl)piperazin-1-yl)-pyrimidine-2,4,6(1H,3H,5H)-trione
-
-
5-(4-phenoxyphenyl)-5-(4-(2-nitrooxy-ethyl)piperidin-1-yl)-pyrimidine-2,4,6(1H,3H,5H)-trione
-
-
5-(4-phenoxyphenyl)-5-(bis-(2-nitrooxy-ethyl)-amino)pyrimidine-2,4,6(1H,3H,5H)-trione
-
-
5-(4-phenoxyphenyl)-5-(methyl-(2-nitrooxy-ethyl)-amino)-pyrimidine-2,4,6(1H,3H,5H)-trione
-
-
5-[3-(hydroxymethyl)piperidin-1-yl]-5-(4-phenoxyphenyl)pyrimidine-2,4,6(1H,3H,5H)-trione
-
-
5-[4-(2-hydroxyethyl)piperazin-1-yl]-5-(4-phenoxyphenyl)pyrimidine-2,4,6(1H,3H,5H)-trione
-
-
5-[4-(2-hydroxyethyl)piperidin-1-yl]-5-(4-phenoxyphenyl)pyrimidine-2,4,6(1H,3H,5H)-trione
-
-
5-[4-(hydroxymethyl)piperidin-1-yl]-5-(4-phenoxyphenyl)pyrimidine-2,4,6(1H,3H,5H)-trione
-
-
6-(N-Cbz)amino-2-[(4'-chloro[1,1'-biphenyl]-4-sulfonyl)amino]hexanoic acid
IC50 ratio MMP2 to MMP9 is 160
6-(N-Cbz)amino-2-[(4'-methyl[1,1'-biphenyl]-4-sulfonyl)amino]hexanoic acid
IC50 ratio MMP2 to MMP9 is 125
6-(N-Cbz)amino-2-[(coumaryl-7-sulfonyl)amino]hexanoic acid
IC50 ratio MMP2 to MMP9 is 7.5
6-(N-Cbz)amino-2-[([1,1'-biphenyl]-4-sulfonyl)amino]hexanoic acid
IC50 ratio MMP2 to MMP9 is 36
6-amino-2-[(4'-chloro[1,1'-biphenyl]-4-sulfonyl)amino]hexanoic acid
IC50 ratio MMP2 to MMP9 is 100
6-amino-2-[(4'-methyl[1,1'-biphenyl]-4-sulfonyl)amino]hexanoic acid
IC50 ratio MMP2 to MMP9 is 118
6-amino-2-[([1,1'-biphenyl]-4-sulfonyl)amino]hexanoic acid
IC50 ratio MMP2 to MMP9 is 44
adiponectin
-
adiponectin can markedly suppress protein expression and activity of MMP9 in brain, induced by 1 h ischemia followed by 23 h reperfusion
-
Ag-3340
-
i.e. N-hydroxy-2,2-dimethyl-4-[(4-phenoxyphenyl)sulfonyl]thiomorpholine-3-carboxamide, 50% inhibition at 0.26 nM, comparison with inhibitory effect on matrix metalloproteinases MMP-3, MMp-7, MMP-2
antibody REGA-3G12
highly selective, potent MMP-9 inhibition, the antibody recognizes the N-terminal part, not the C-terminal hemopexin and O-glycosylated domains, epitope mapping, overview
-
astaxanthin
from extracts of Halorubrum tebenquichense strain SU10 (isolated from salt crystals collected on Uyuni saltern of Bolivia)
bacterioruberin
a haloarchaeal pigment that shows inhibition of human MMP-9. Ligand preparation from extracts of Natronoccoccus sp. strain TC6 (isolated from El Golea Sebkha, a salt lake on Algerian Sahara) and Halorubrum tebenquichense strain SU10 (isolated from salt crystals collected on Uyuni saltern of Bolivia) and molecular docking to the human enzyme structure (PDB ID 1L6J), molecular dynamics simulations, detailed overview. Analysis of in silico inhibition of MMP-9 by carotinoids including bacterioruberin
BIIL284
-
BIIL284 treatment (3 mg/kg once daily for 2 weeks) significantly reduces the extracellular matrix metalloproteinase-9 activity in stented arteries
bisahnydrobacterioruberin
from extracts of Natronoccoccus sp. strain TC6 (isolated from El Golea Sebkha, a salt lake on Algerian Sahara) and Halorubrum tebenquichense strain SU10 (isolated from salt crystals collected on Uyuni saltern of Bolivia)
-
CGS27023A
-
50% inhibition at 8 nM, comparison with inhibitory effect on matrix metalloproteinases MMP-3, MMp-7, MMP-2
chitooligosaccharides
-
different molecular weight, inhibit both MMP-9 expression and activity, especially 1- to 3-kDa chitooligosaccharides, chitooligosaccharides-I in HT-1080 cells
dihydrorhodopin
from extracts of Halorubrum tebenquichense strain SU10 (isolated from salt crystals collected on Uyuni saltern of Bolivia)
-
doxycyclin
-
doxycycline significantly inhibits MMP-9 activity in gel zymography and also suppressed in situ gelatinase activity
hemopexin domain of MMP-9
the hemopexin domain of MMP-9 inhibits the degradation of gelatin. It also abolishes the degradation of gelatin by MMP-2. Blades 1 and 4 of the PEX9 domain are responsible for the gelatin degradation inhibitory activity of PEX9. The hemopexin domain of MMP-9 does not prevent the degradation of other MMP-9 substrates, such as a fluorogenic peptide, alphaB crystalline, or nonmuscular actin
-
isovitexin
interacts with enzyme residues Glu241, Ala242, Pro255, Pro254, Thr251, Leu222, Tyr248, Arg241, Met247, His226, and Glu227, binding structure analysis, and modeling, overview
minocycline
-
0.02 mM minocycline displays inhibitory action on MMP-9 expression and activity
monoanhydrobacterioruberin
from extracts of Natronoccoccus sp. strain TC6 (isolated from El Golea Sebkha, a salt lake on Algerian Sahara)
N,N'-[(2S)-6-[[(2,3-dihydroxyphenyl)carbonyl]amino]hexane-1,2-diyl]bis(2,3-dihydroxybenzamide)
-
-
N-hydroxy-2-(isobutyl[(4-methoxyphenyl)sulfonyl]amino)acetamide
-
50% inhibition at 2.9 nM, comparison with inhibitory effect on matrix metalloproteinases MMP-3, MMp-7, MMP-2
N-[(5R)-5-[[(2,3-dihydroxyphenyl)carbonyl]amino]-6-hydroxyhexyl]-2,3-dihydroxybenzamide
-
-
N-[(5S)-5-[[(2,3-dihydroxyphenyl)carbonyl]amino]-6-hydroxyhexyl]-2,3-dihydroxybenzamide
-
-
N-[(5S)-6-amino-5-[[(2,3-dihydroxyphenyl)carbonyl]amino]hexyl]-2,3-dihydroxybenzamide
-
-
norcantharidin
-
i.e. exo-7-oxabicylo-[2.2.1] heptane-2,3-dicarboxylic anhydride, norcantharidin inhibits gelatinase activity of MM-9 in a concentration- and time-dependent manner
pioglitazone
-
pioglitazone reduces the upregulation of active form of MMP-9 after ischemia
proanthocyanidins
-
from the american cranberry, Vaccinium macrocarpon, decrease cellular viability of DU-145 cells via inhibition of MMP-9. The proanthocyanidins PACs increase the expression of TIMP-2, a known inhibitor of MMP activity, and decrease the expression of EMMPRIN, an inducer of MMP expression. Cranberry proanthocyanidins decrease MMP activity through the induction and/or inhibition of specific temporal MMP regulators, and by affecting either the phosphorylation status and/or expression of MAP kinase, PI-3 kinase, NF-kappaB and AP-1 pathway proteins
-
procyanidin oligomers
-
from Japanese quince, Chaenomeles japonica, fruit inhibit activity of MMP-9
-
REGA-3G12 scFv with (His6)2
-
monoclonal antibody REGA-3G12 single-chain variable fragment, 0.005 mM, 66% inhibition
-
tissue inhibitor of metalloproteinases 2
-
TIMP-2, complete inhibition at 0.5 mg
-
tissue inhibitor of metalloproteinases-1
-
i.e. TIMP-1, plays a crucial role in the pathogenesis of hepatic fibrosis and thus may represent an important therapeutic target in the design of anti-fibrotic strategiesfor chronic liver disease, overview, molecular modeling of the three-dimensional structure of the MMP-9/TIMP-1 complex, overview
-
trisahnydrobacterioruberin
from extracts of Natronoccoccus sp. strain TC6 (isolated from El Golea Sebkha, a salt lake on Algerian Sahara) and Halorubrum tebenquichense strain SU10 (isolated from salt crystals collected on Uyuni saltern of Bolivia)
-
vitexin
interacts with enzyme residues Gly186, Pro246, His236, Met247, Tyr248, Val223, and Leu188, binding structure analysis, and modeling, overview
doxycycline
-
doxyxycline inhibits directlyMMP-9 enzymatic activity derived from tumor necrosis factor-alpha-stimulated vascular smooth muscle cells
doxycycline
-
inhibitory mechanism and effect on osteoclastogenesis signaling induced by RANKL, both in vitro and in vivo, overview. Although Dox inhibits RANKL-induced osteoclastogenesis and down-modulates the mRNA expression of functional osteoclast markers, it neither affects RANKL-induced MAPKs phosphorylation nor NFATc1 gene expression in RAW264.7 monocytic cells
EDTA
2 mM, severely inhibits enzyme activity due to chelation of metal ions
Melatonin
-
i.e. N-acetyl-5-methoxytryptamine, used in protection during gastric ulcer, arresting cell injury, protein carbonyl formation, and lipid peroxidation in mice during gastroprotection, inhibits MMP-9 expression and activity
SB-3CT
in HBMEC, treatment with the MMP9 inhibitor significantly lowers Abeta-induced lipoprotein receptor levels in the extracellular media
SB-3CT
a MMP9 inhibitor, administration of SB-3CT to apoE4 animals significantly enhanced amyloid beta clearance from the brain to the periphery following intracranial administration of amyloid beta
SB-3CT
-
MMP9-specific inhibitor, MMP9 activity is reduced with SB-3CT resulting in reduced brain injury
Tissue inhibitor of metalloproteinase-1
-
exogenous tissue inhibitor of metalloproteinase-1 has a greater inhibitory effect on endogenously active MMP-9 than on 4-aminophenylmercuric acetate-activated MMP-9
-
tissue inhibitor of metalloproteinases 1
-
TIMP-1, complete inhibition at 0.5 mg
-
tissue inhibitor of metalloproteinases 1
TIMP-1, the zymogen proMMP-9 trimers possess a 50fold higher affinity for TIMP-1 than the monomers, with a higher extent of TIMP-1 inhibition of angiogenesis induced by trimers compared with monomers
-
tissue inhibitor of metalloproteinases 1
TIMP-1, the 65 kDa enzyme form lacking both the N- and C-terminal domains cannot be inhibited by TIMP-1 in contrast to the mature 82 kDa enzyme form
-
additional information
-
the 230 kDa enzyme does not remain intact in 4 M urea, 0.5 M NaCl, 4 M CsCl or 4 M GdHCl. Glycosaminoglycan chains may interfere with inhibitors
-
additional information
-
computational model of MMP9 activation and inhibition, overview
-
additional information
-
pre-exposure to pyrrolidine dithiocarmate suppresses pro-MMP-9 activity and protein levels in relaxin-treated THP-1 cells
-
additional information
-
following overexpression of arylsulfatase B, MMP9 declines 51%
-
additional information
-
MMP-9 is specifically regulated by p21-activated-kinase-1, ectopic expression of p21-activated-kinase-1 variants impairs Jun N-terminal kinase but not necrosis factor-kappaB pathway, which in turn suppresses the promoter activation and transcription of MMP-9
-
additional information
-
MMP-9 is decreased 12 months after natalizumab treatment in patients with relapsing-remitting multiple sclerosis
-
additional information
-
doublecortin synthesis suppresses the expression and activation of MMP9
-
additional information
-
downregulation of E26 transformation-specific DNA binding domain transcription factors suppresses the non-endothelial E26 transformation-specific DNA binding domain-target gene MMP9
-
additional information
-
hesperidin inhibits the secreted and cytosolic MMP-9 forms in HepG2 cells through the inhibition of nuclear factor-kappaB and AP-1
-
additional information
-
synthesis and inhibitory activity against MMP-9 of nobiletin metabolites, overview. The key intermediate is 2'0-hydroxy-3',4',5',6'-tetramethoxyacetophenone
-
additional information
-
design and synthesis of barbiturate-nitrate hybrids, barbiturate-based MMP inhibitors incorporating a nitric oxide donor/mimetic group, that inhibit MMP-9 activity and secretion, reducing effects on cell viability by inhibitors, overview
-
additional information
Ficus deltoidea leaf extract inhibits matrix metalloproteinase-2, 8 and 9, molecular docking, molecular dynamics, molecular dynamic simulation analysis, overview. Computational docking analysis reveals that vitexin and isovitexin binds to the active site of the three tested MMPs
-
additional information
omega-3 and omega-6 fatty acids act as inhibitors of matrix metalloproteinase-9 activity. Omega-3 and omega-6 fatty acids contribute to the structure and function of the phospholipid bilayers in cellular membranes and act as precursors of lipid-mediated signaling molecules
-
additional information
-
no inhibition by SCH772984 (a potent ERK1/2 inhibitor) or PDTC (a potent NFkappaB inhibitor)
-
additional information
matrix metallopeptidase 9 is a host protein target for chloroquine and melatonin in immunoregulation during COVID-19. Melatonin appears to be the more promising repurposed drug against MMP9 for better immunocompromisation in COVID-19
-
additional information
with respect to low-density lipoprotein receptor (LDLR), treatment with the broad spectrum MMP inhibitor, marimastat (0.001 mM), or SB-3CT (0.001 mM) in human brain endothelial cells (HBMEC) significantly reduces soluble LDLR levels (both about 40%) compared with Abeta alone
-
additional information
-
epitope tagging of MMP-9 with monoclonal antibodies, overview
-
additional information
-
both NF-jB and AP-1 inhibitors inhibit MMP-9 expression
-
additional information
-
gene expression of MMP-9 is significantly suppressed in the hearts of eplerenone-treated mice compared with controls
-
additional information
-
integrin-linked kinase gene knockdown leads to reduced MMP9 expression
-
additional information
-
downregulation of E26 transformation-specific DNA binding domain transcription factors suppresses the non-endothelial E26 transformation-specific DNA binding domain-target gene MMP9
-
additional information
-
no inhibition by amiloride or plasminogen activator/plasmin inhibitor D-Phe-Pro-Arg-chloromethylketone dihydrochloride
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2,3,7,8-tetrachlorodibenzo-p-dioxin
-
both MMP-9 mRNA expression and enzymatic activity are gradually increased with the concentration increase of 2,3,7,8-tetrachlorodibenzo-p-dioxin in media and these changes can be reversed by resveratrol treatment in a dose-dependent manner, c-Jun mediates 2,3,7,8-tetrachlorodibenzo-p-dioxin-induced MMP-9 expression and activity
4-amino phenylmercuric acetate
-
pro-MMP-9 is activated with 1 mM 4-amino phenylmercuric acetate in assay buffer at 37°C for 1.5 h
acrolein
-
activates MMP-9 via EGFR/MAPK signaling and stimulation of pro-MMP-9 cleavage
cathepsin G
-
MMP9 is released in an inactive form and requires proteolytic activation, cathepsin G mediates activation of pro-matrix metalloproteinase 9
-
chymase
-
chymase converts promatrix metalloproteinase-9 to matrix metalloproteinase-9
-
fibronectin
-
fibronectin enhances, in a PKC-dependent manner, the net activity of MMP-9, but not its expression
-
homocysteine
-
homocysteine activates matrix metalloproteinase-9, muscimol ameliorates the homocysteine-mediated MMP-9 activation
lipopolysaccharide
-
lipopolysaccharide challenge (0.001 mg/ml) increases the protein level of MMP-9 and induces the activity of MMP-9 in H9c2 cardiomyoblasts through ERK1/2 signaling pathway
matrix metalloproteinase-7
MMP-9 is activated by matrix metalloproteinase-7
-
platelet-activating factor
-
i.e. 1-O-alkyl-2-acetyl-sn-glyceryl-3-phosphorylcholine, induces MMP-9 enzyme expression, and increases enzyme content and activity
4-aminophenylmercuric acetate
-
APMA activation of MMP-9 affects tissue inhibitor of metalloproteinase-1 binding to the enzyme resulting in the loss of natural enzyme inhibition
4-aminophenylmercuric acetate
-
after treatment with 4-aminophenylmercuric acetate, affinity-purified W-256 cell gelatinase is converted to a final processed form of 66000 Da
4-aminophenylmercuric acetate
-
1 mM 4-aminophenylmercuric acetate-mediated activation of MMP-9 provokes autocatalytic cleavage of recombinant MMP-9
phorbol 12-myristate 13-acetate
-
the effect of phorbol 12-myristate 13-acetate (1.3 nM), a known activator of MMP-9 secretion, is about 10fold greater than that of 0.01 mM arachidonic acid. Addition of 0.001 mM and 0.01 mM arachidonic acid, eicosapentaenoic acid or docosapentaenoic acid along with phorbol 12-myristate 13-acetate does not affect MMP-9 production.
phorbol 12-myristate 13-acetate
-
30 nM 12-phorbol 13-myristate acetate is used to activate MMP-9, aqueous extract isolated from Prunella vulgaris reduces 12-phorbol 13-myristate acetate-induced activation of MMP-9
phorbol 12-myristate 13-acetate
-
30 nM 12-phorbol 13-myristate acetate is used to activate MMP-9, aqueous extract isolated from Prunella vulgaris reduces 12-phorbol 13-myristate acetate-induced activation of MMP-9
additional information
-
binding of the zymogen to fetuin or asialofetuin results in activation
-
additional information
-
activation of pro-MMP-9 by 4-aminophenylmercuric acetate
-
additional information
-
beta-hematin, and not hemin, accelerates the activation of MMP-9, activation of MMP-9 by hemin and MMP-3, overview
-
additional information
-
activation by trypsin, MMP3, and MMP10, computational model of MMP9 activation and inhibition, overview
-
additional information
-
relaxin induces enzyme expression in THP-1 cells, while it reduces expression of NF-kappaB inhibitor protein, IkappaB-alpha, overview
-
additional information
-
dermal fibroblasts and hepatic stellate cells require type-I collagen which boosts Jun N-terminal kinase activity to maximally induce MMP-9
-
additional information
-
Notch1 may be involved in MMP9 activation either by enhancing its expression or by stabilizing the protein
-
additional information
-
activator protein-4 expression may play an important role in the induction of synthesis of MMP-9
-
additional information
-
MMP-9 is activated by a whole-cell extract from Prevotella nigrescens ATCC 33563
-
additional information
-
several members of the vascular endothelial growth factor family and the three vascular endothelial growth factor receptors are responsible for secretion of MMP-9 via an autocrine loop
-
additional information
-
0.001-0.04 mM arachidonic acid increases matrix metalloproteinase 9 secretion and expression at the mRNA level
-
additional information
-
eicosapentaenoic acid, docosapentaenoic acid or docosahexaenoic acid by themselves have no effect on MMP-9 secretion
-
additional information
-
the MMP-9 mRNA expression is inducible by vascular endothelial growth factor
-
additional information
-
treatment with phorbol 12-myristate 13-acetate (100 ng/ml) induces MMP-9 expression in glandular epithelia, supportive connective tissue, and muscle tissue cell lines
-
additional information
-
cells treated with more than 1 ng/ml of tissue growth factor-beta1 secrete pro-MMP-9 in a dose dependant manner, addition of 20 ng/ml of tissue necrosis factor-alpha further upregulates pro-MMP-9 expression
-
additional information
-
MMP-9 expression is increased after a 16 h acetaldehyde treatment (0.1 mM)
-
additional information
-
human arteries subjected to ex vivo angioplasty and stent implantation display increased in-stent intimal hyperplasia and higher MMP-9 activity in the presence of leukotriene B4
-
additional information
-
treatment with tissue necrosis factor increases MMP9 release while pre-treatment with alpha-lipoic acid (6,8-dithio-octanoic acid) inhibits this tissue necrosis factor-induced effect
-
additional information
-
the presence of an intact active site and hemopexin domain are required for full angiogenesis-inducing activity of the MMP-9 enzyme
-
additional information
enzyme MMP-9 is released in the inactive form as proenzyme and can be secreted in physical association with its specific tissue inhibitor (TIMP-1) as proMMP-9/TIMP-1 complex or as TIMP-1 free protein. Activation of MMP-9 requires a complex network of mechanisms involving other matrix metalloproteases
-
additional information
-
gastric gelatinase B is rapidly increased in Helicobacter felis-induced gastritis
-
additional information
-
MMP-9 is upregulated by tumor necrosis factor alpha, TNFalpha
-
additional information
-
pulmonary infection with the Gram-negative intracellular bacterium Francisella tularensis, a category A biological threat agent, induces MMP-9 expression
-
additional information
-
ectopic Fra-1 markedly stimulates MMP-9 mRNA expression
-
additional information
-
MMP-9 is significantly upregulated on day 2 after wounding in the impaired healing (macrophage depleted) animals that receive hyperbaric oxygen treatment as compared with impaired healing animals that does not receive hyperbaric oxygen treatment
-
additional information
-
ATP non-transcriptionally increases MMP-9 activity by activation of P2Y and PI3K, the increased activity of secreted MMP-9 is due to the increased protein secretion, but not by the increased MMP-9 mRNA and protein expression
-
additional information
upon infection with Toxocara canis, matrix metalloproteinase MMP-2 and MMP-9 activities remarkably increase, with concomitant granuloma formation
-
additional information
-
implantation of 9L glioma cells into brain increases the expression of MMP-9, overview
-
additional information
-
MMP-9 is induced in small renal arteries by recombinant human relaxin, up-regulation of 70%
-
additional information
an increase in hypoxia-inducible factor-1alpha is followed by a significant increase in MMP-9 gene expression at 4 h at 24 h post-traumatic brain injury, traumatic brain injury increases MMP-9 mRNA and protein levels in cortical and hippocampal regions early at 4 h post-traumatic brain injury, persisting for 5 days
-
additional information
-
high glucose (25 mM) induces expression of MMP-9
-
additional information
-
benzo[a]pyrene increases the mRNA level of matrix metalloproteinase 9
-
additional information
-
tissue kallikrein is a potent activator of latent proenzyme
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00422 - 0.00496
N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl-7-methoxycoumarin-4-yl acetyl
0.00422
N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl-7-methoxycoumarin-4-yl acetyl
-
pH 7.6, 25°C, wild type
0.00496
N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl-7-methoxycoumarin-4-yl acetyl
-
pH 7.6, 25°C, recombinant enzyme
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.04 - 1.97
(7-methoxycoumaryl-4yl)acetylPLGLA2pr(2,4-dinitrophenol)-AR-NH2
pH 7.5, 37°C, dimeric form
2.72
(7-methoxycoumaryl-4yl)acetylPLGLA2pr(2,4-dinitrophenol)-AR-NH2
pH 7.5, 37°C, monomeric form
3 - 6
(7-methoxycoumaryl-4yl)acetylPLGLA2pr(2,4-dinitrophenol)-AR-NH2
pH 7.5, 37°C, monomeric form
8.67
(7-methoxycoumaryl-4yl)acetylPLGLA2pr(2,4-dinitrophenol)-AR-NH2
pH 7.5, 37°C, dimeric form
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000045
(2E)-3-(N-hydroxycarbamoyl)-2-(3-phenylpropylidene)propionyl-L-tryptophan-N-methylamide
Homo sapiens
-
-
0.01
(2E)-3-(N-hydroxycarbamoyl)-2-heptylidenepropionyl-L-tryptophan-N-methylamide
Homo sapiens
-
above
0.000017
(2E)-3-(N-hydroxycarbamoyl)-2-isopropionyl-L-tryptophan-N-methylamide
Homo sapiens
-
-
0.000038
(2E)-3-(N-hydroxycarbamoyl)-2-[(2E)-3-phenylprop-2-en-1-ylidene]propionyl-L-tryptophan-N-methylamide
Homo sapiens
-
-
0.000974
(2E)-3-(N-hydroxycarbamoyl)-2-[(2E)-but-2-en-1-ylidene]propionyl-L-tryptophan-N-methylamide
Homo sapiens
-
-
0.0000005
(R)-2-(N-((6-fluoropyridin-3-yl)methyl)-4-methoxyphenyl-sulfonamido)-N-hydroxy-3-methylbutanamide
Mus musculus
-
-
0.000026
5-(1,5-dihydroxypentan-3-yl)-5-(4-phenoxyphenyl)pyrimidine-2,4,6(1H,3H,5H)-trione
Homo sapiens
-
pH 7.5, 37°C
0.000145
5-(4-hydroxybutan-2-yl)-5-(4-phenoxyphenyl)pyrimidine-2,4,6(1H,3H,5H)-trione
Homo sapiens
-
pH 7.5, 37°C
0.000104
5-(4-phenoxyphenyl)-5-(3-(1-nitrooxy-methyl)piperidin-1-yl)-pyrimidine-2,4,6(1H,3H,5H)-trione
Homo sapiens
-
pH 7.5, 37°C
0.000152
5-(4-phenoxyphenyl)-5-(4-(1-nitrooxy-ethyl)piperidin-1-yl)-pyrimidine-2,4,6(1H,3H,5H)-trione
Homo sapiens
-
pH 7.5, 37°C
0.000092
5-(4-phenoxyphenyl)-5-(4-(2-nitrooxy-ethyl)piperazin-1-yl)-pyrimidine-2,4,6(1H,3H,5H)-trione
Homo sapiens
-
pH 7.5, 37°C
0.000202
5-(4-phenoxyphenyl)-5-(4-(2-nitrooxy-ethyl)piperidin-1-yl)-pyrimidine-2,4,6(1H,3H,5H)-trione
Homo sapiens
-
pH 7.5, 37°C
0.000091
5-(4-phenoxyphenyl)-5-(bis-(2-nitrooxy-ethyl)-amino)pyrimidine-2,4,6(1H,3H,5H)-trione
Homo sapiens
-
pH 7.5, 37°C
0.000048
5-(4-phenoxyphenyl)-5-(methyl-(2-nitrooxy-ethyl)-amino)-pyrimidine-2,4,6(1H,3H,5H)-trione
Homo sapiens
-
pH 7.5, 37°C
0.0000062
5-[3-(hydroxymethyl)piperidin-1-yl]-5-(4-phenoxyphenyl)pyrimidine-2,4,6(1H,3H,5H)-trione
Homo sapiens
-
pH 7.5, 37°C
0.0000081
5-[4-(2-hydroxyethyl)piperazin-1-yl]-5-(4-phenoxyphenyl)pyrimidine-2,4,6(1H,3H,5H)-trione
Homo sapiens
-
pH 7.5, 37°C
0.000012
5-[4-(2-hydroxyethyl)piperidin-1-yl]-5-(4-phenoxyphenyl)pyrimidine-2,4,6(1H,3H,5H)-trione
Homo sapiens
-
pH 7.5, 37°C
0.000097
5-[4-(hydroxymethyl)piperidin-1-yl]-5-(4-phenoxyphenyl)pyrimidine-2,4,6(1H,3H,5H)-trione
Homo sapiens
-
pH 7.5, 37°C
0.000005
6-(N-Cbz)amino-2-[(4'-chloro[1,1'-biphenyl]-4-sulfonyl)amino]hexanoic acid
Homo sapiens
pH 7.5, 25°C
0.0000028
6-(N-Cbz)amino-2-[(4'-methyl[1,1'-biphenyl]-4-sulfonyl)amino]hexanoic acid
Homo sapiens
pH 7.5, 25°C
0.008
6-(N-Cbz)amino-2-[(coumaryl-7-sulfonyl)amino]hexanoic acid
Homo sapiens
pH 7.5, 25°C
0.00005
6-(N-Cbz)amino-2-[([1,1'-biphenyl]-4-sulfonyl)amino]hexanoic acid
Homo sapiens
pH 7.5, 25°C
0.00005
6-amino-2-[(4'-chloro[1,1'-biphenyl]-4-sulfonyl)amino]hexanoic acid
Homo sapiens
pH 7.5, 25°C
0.000045
6-amino-2-[(4'-methyl[1,1'-biphenyl]-4-sulfonyl)amino]hexanoic acid
Homo sapiens
pH 7.5, 25°C
0.0009
6-amino-2-[([1,1'-biphenyl]-4-sulfonyl)amino]hexanoic acid
Homo sapiens
pH 7.5, 25°C
0.017
3',4',5,6,7,8-hexamethoxyflavone
Homo sapiens
-
TNF-alpha-treated cells, pH and temperature not specified in the publication
0.0209
3',4',5,6,7,8-hexamethoxyflavone
Homo sapiens
-
PMA-treated cells, pH and temperature not specified in the publication
0.0108
3',4'-dihydroxy-5,6,7,8-tetramethoxyflavone
Homo sapiens
-
TNF-alpha-treated cells, pH and temperature not specified in the publication
0.0123
3',4'-dihydroxy-5,6,7,8-tetramethoxyflavone
Homo sapiens
-
PMA-treated cells, pH and temperature not specified in the publication
0.0164
3'-hydroxy-4',5,6,7,8-pentamethoxyflavone
Homo sapiens
-
TNF-alpha-treated cells, pH and temperature not specified in the publication
0.0169
3'-hydroxy-4',5,6,7,8-pentamethoxyflavone
Homo sapiens
-
PMA-treated cells, pH and temperature not specified in the publication
0.0037
4'-hydroxy-3',5,6,7,8-pentamethoxyflavone
Homo sapiens
-
PMA-treated cells, pH and temperature not specified in the publication
0.0055
4'-hydroxy-3',5,6,7,8-pentamethoxyflavone
Homo sapiens
-
TNF-alpha-treated cells, pH and temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
coupled assay method using MMP-9 catalyzes activation of urokinase and susequent reaction of urokinase with the fluorogenic substrate S-2444 for spectrophotometric quantification, overview
additional information
-
MMP-9 activity in relaxin-treated and untreated renal artery, overview
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
7.5
7.6
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
37
-
assay at
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
31070, 31089, 31090, 31091, 31092, 31212, 31213, 31214, 31215, 31217, 31218, 31224, 667516, 667542, 667579, 667917, 668151, 669731, 670149, 683037, 683114, 683170
-
-
brenda
-
683230, 683233, 683376, 683429, 683458, 683485, 683512, 683518, 683579, 683665, 683710, 683749, 683844, 683881, 684069, 684107, 691877, 695655, 695947, 696571
-
-
brenda
-
696967, 696980, 697075, 697085, 697383, 697548, 697747, 697751, 698149, 698261, 698353, 698359, 699032, 699092, 699186, 699222, 699345, 699642, 699656, 699677, 699932, 699939, 699946, 700406, 700527, 700530, 700536, 700539, 700540, 700581, 700893, 701178, 701192, 701274, 701316, 702513, 707123, 707146, 707366, 707452, 707631, 707654, 707953, 707964, 707978, 708020, 708070, 708086, 708088, 708089, 708144, 708170, 708171, 708198, 708232, 708245, 708409, 708542, 708548, 708773, 708775, 708784, 708810, 708814, 708820, 708828, 709051, 709277, 709288, 709301, 709302, 709336, 709413, 709574, 709613, 709619, 709620, 709700, 709811, 709819, 709880, 709919, 710077, 710091, 710174, 710177, 710225, 710245, 710452, 710531, 710542, 710557, 710584, 710587, 710650, 717299, 717349, 717503, 717522, 717898, 717980, 718069, 718385
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733303, 733634, 734108, 734590, 753945, 754132, 754641, 754869, 755299, 755324, 769334, 769565, 770216
UniProt
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patients with benign prostate hyperplasia, localized prostate cancer or metastatic disease
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patients with pleural effusions, such as malignant pleural effusion, breast carcinoma or lung carcinoma
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697147, 697149, 697726, 697810, 698141, 698338, 699126, 699477, 699716, 700893, 701421, 707043, 707062, 707298, 707302, 707451, 707928, 708024, 708188, 708547, 708548, 708653, 708690, 708695, 708703, 708724, 708740, 708746, 709178, 709239, 709249, 709303, 709382
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709650, 709680, 709734, 709787, 709791, 709904, 709950, 710065, 710067, 710102, 717577, 717960, 718355
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
increased enzyme expression, the positive ratio of MMP-9 tends to increase from Grade II to Grade IV glioma and strong positive MMP-9 staining is more frequently detected in high-grade glioma, association between matrix metalloproteinase-9 expression and survival of patients
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bone marrow-derived cells are the major source of MMP-9 in the ischemic brain
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localized mainly in the cytoplasm of neoplastic astrocytes
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expression and activity of MMP-9 during premature rupture of chorioamniotic membranes, secretion of proMMP-9 from the amniochorion after application of lipopolysacchride to either sides of the membrane is increased, overview
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coronary arteritis is induced by Lactobacillus casei cell wall extract injection
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demineralized dentin matrix, extraction is best at acidic conditions of pH 2-3 compared to pH 7.4-EDTA-containing extracts
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MMP-9 is expressed at very low levels in endometrioid adenocarcinoma cells
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MMP-9 protein is localized at the leading-edge keratinocytes in front of the migrating epidermal layer
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high expression level of MMP-9 increasing during growth
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expression analysis of MMP 9 in benign, premalignant and malignant laryngeal lesions, e.g. carcinoma and dysplasia, the enzyme is upregulated in malignant tissue, immunohistochemic analysis, overview
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the level of MMP-9 activity in lens epithelial cells is highest in eyes with cortical cataract
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atrophic acnd nonatrophic oral lichen planus
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MMP-9 is expressed at very low levels in serous cystoadenocarcinoma cells
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transfected with a construct expressing enzyme. Enzyme overexpressing cells show a significantly reduced collagen gel contraction
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Mycobacterium tuberculosis stimulates matrix metalloproteinases secretion in the host. Analysis of the patterns of matrix metalloproteinase 9 (MMP-9) and 2 (MMP-2) isoforms in sputum samples, overview. Variations in MMP-9 isoforms are observed, which coincide with the progression of tuberculosis infection
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MMP9 is expressed in teeth from early embryonic to adult stage
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additional information
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a macrophage cell line established by immortalization of bone marrow macrophages from C57BL/6 mice with J2 recombinant retrovirus-expressing v-myc/v-raf oncogenes
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a macrophage cell line established by immortalization of bone marrow macrophages from C57BL/6 mice with J2 recombinant retrovirus-expressing v-myc/v-raf oncogenes
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enzyme expression is slightly induced by HIV and strongly induced by TNF alpha, while matrix metalloproteinase MMP-2 and tissue inhibitor of metalloproteinase-1 and tissue inhibitor of metalloproteinase-2 are only slightly affected. Astrocytes are a major source of enzyme in the inflamed brain
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murine melanoma cell line, with platelet-activating factor-induced experimental pulmonary metastasis, which is inhibited by both NF-jB and c-jun inhibitors and completelyby MMP-9 inhibitor
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plasma active MMP-9 and TIMP-1 are measured at three time-points in 163 individuals, thereof 129 males and all with average age of 62.8 years. Active MMP-9 and TIMP-1 are similar irrespective of the months of the year the sample, and are thus independent of season and storage time
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serum MMP9 levels are significantly associated with hyperlipidaemia
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articular chondrocyte of the late-stage osteoarthritis cartilage with surface fibrillation and chondrocyte clusters, not in healthy chondrocytes, overview
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stage II/III rectal carcinoma, expression analysis, the MMP-9 expression is related to tumor growth, overview
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from SC40-transformed cells, normal alveolar macrophages, phorbol ester-differentiated monocytic leukemia U937 cells, fibrosarcoma HT1080 cells, cultured keratinocytes
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enzyme protein is present in cells within granulomas and in scattered epitheloid cells
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proteolytic activity and expression of gelatinase B in serum of gastric cancer patients and their correlation with the stage of the tumor
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the enzyme is upregulated compared to control brain
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unstimulated/resident and inflammatory, peritoneal leukocytes, constitutive expression
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unstimulated/resident and inflammatory, peritoneal leukocytes, constitutive expression
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method development and evaluation for immunostaining MMP-9 in mouse lung paraffin-embedded tissue utilizing human ovary as a control, overview. MMP-9 localization in lung tissue of a murine model of allergic asthma induced by chicken ovalbumin. The murine model of allergic asthma consists of a tissue inhibitor of metalloproteinase (TIMP)-1 genetic knockout backcrossed over 10 generations from 129/sv mice on a C57Bl/6 background
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method development and evaluation for immunostaining MMP-9 in mouse lung paraffin-embedded tissue utilizing human ovary as a control, overview. MMP-9 localization in lung tissue of a murine model of allergic asthma induced by chicken ovalbumin. The murine model of allergic asthma consists of a tissue inhibitor of metalloproteinase (TIMP)-1 genetic knockout backcrossed over 10 generations from 129/sv mice on a C57Bl/6 background
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increased MMP-9 activity and expression during ventilator-induced lung injury, overview
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secretion of MMP-9, transcription factor NF-kappaB is important in MMP gene regulation in macrophage cells
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secretion of MMP-9 in the early phase of peritonitis, no MMP-9 production in unstimulated macrophages
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macrophages contribute significantly to the elevated levels of MMP-9 in dystrophic muscle
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secretion of MMP-9 in the early phase of peritonitis, no MMP-9 production in unstimulated macrophages
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treatment of blood-derived mast cells with TNF-alpha significantly increases expression of enzyme mRNA and upregulates enzyme activity. TNF-alpha also increases the invasiveness of mast cells across Matrigel-coated membranes. INF-gamma is inhibitory to enzyme mRNA and protein expression
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distribution of MMP9 in both emigrating and migrating neural crest cells, overview
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distribution of MMP9 in both emigrating and migrating neural crest cells, overview
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secretion of MMP-9, high MMP-9 expression in the early phase and especially in the late phase of peritonitis
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secretion of MMP-9, high MMP-9 expression in the early phase and especially in the late phase of peritonitis
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F1NGT3
gene MMP9 is significantly upregulated in 23-wk-old (laying phase) chicken ovaries compared with 6-wk-old ovaries (prepubertal phase). In reproductively active chicken ovary, the enzyme expression level increases during follicular maturation. Enzyme MMP9 mRNA expression continues to rise in postovulatory follicle 1 and postovulatory follicle 2 after ovulation
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gene MMP9 is significantly upregulated in 23-wk-old (laying phase) chicken ovaries compared with 6-wk-old ovaries (prepubertal phase). In reproductively active chicken ovary, the enzyme expression level increases during follicular maturation. Enzyme MMP9 mRNA expression continues to rise in postovulatory follicle 1 and postovulatory follicle 2 after ovulation
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infundibulum, magnum, isthmus, and shell gland. Developmental changes, overview
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Gallus gallus Hy-Line Brown
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infundibulum, magnum, isthmus, and shell gland. Developmental changes, overview
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in zymosan-treated mice inducing peritonitis, MMP-9 and ZIMP-1 are located in the peritoneal fluid and plasma at the time of peritoneal neutrophil infiltration and persist there until time of monocyte/macrophage influx
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in zymosan-treated mice inducing peritonitis, MMP-9 and ZIMP-1 are located in the peritoneal fluid and plasma at the time of peritoneal neutrophil infiltration and persist there until time of monocyte/macrophage influx
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no association between plasma MMP-9 activity and the concentrations of lead in whole blood or plasma, overview
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in zymosan-treated mice inducing peritonitis, MMP-9 and ZIMP-1 are located in the peritoneal fluid and plasma at the time of peritoneal neutrophil infiltration and persist there until time of monocyte/macrophage influx
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in zymosan-treated mice inducing peritonitis, MMP-9 and ZIMP-1 are located in the peritoneal fluid and plasma at the time of peritoneal neutrophil infiltration and persist there until time of monocyte/macrophage influx
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670741, 668514, 668996, 684107, 697548, 701178, 710177, 710452, 710542, 710584, 708232, 708245, 708784, 708814, 709619, 709819
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additional information
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active host MMP-9 is expressed in walls and fluids of hydatid cysts of parasite Echinococcus granulosus in the environment of granulomatous reaction, immunohistochemic analysis, positive reaction to MMP-9 is found in cyst-surrounding cells, epithelioid and giant cells, and in the germinal layer of cyst wall, overview
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additional information
F1NGT3
immunohistochemic localization analysis, overview
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additional information
quantitative enzyme tissue expression analysis in the chicken oviduct during maturation
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additional information
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quantitative enzyme tissue expression analysis in the chicken oviduct during maturation
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additional information
Gallus gallus Hy-Line Brown
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quantitative enzyme tissue expression analysis in the chicken oviduct during maturation
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additional information
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immunohistochemic localization analysis, overview
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additional information
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MMP-9 is not expressed in mucinous and clear cell adenocarcinoma cells
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additional information
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levels of MMP-9 in choriodecidua and amnion increases 4 and 8fold, respectively, after simultaneous infection with Escherichia coli added to either the amniotic or the choriodecidual face or to both
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additional information
quantitative real time PCR enzyme expression analysis and immunohistochemic analysis in glioblastoma, MMP-9 activity is constitutively heightened in tissue samples from primary glioblastoma multiforme, the most common and aggressive malignant primary brain tumor in humans
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additional information
enzyme MMP-9 is released in the inactive form as proenzyme and can be secreted in physical association with its specific tissue inhibitor (TIMP-1) by monocyte/macrophage cells as proMMP-9/TIMP-1 complex or as TIMP-1 free protein by tertiary granules of neutrophil cells
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additional information
enzyme immunohistochemic analysis of 237 samples, overview
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additional information
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enzyme immunohistochemic analysis of 237 samples, overview
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MMP-9 expression analysis in peritonitis, overview
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MMP-9 co-localizes with macrophages and neutrophils in gastritic stomach, overview
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additional information
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MMP-9 levels are increased in acute pancreatitis
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additional information
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MMP-9 expression analysis in peritonitis, overview
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additional information
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MMP-9 co-localizes with macrophages and neutrophils in gastritic stomach, overview
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additional information
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MMP-9 levels are increased in acute pancreatitis
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additional information
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MMP-9 is increased in tumor cells, no expression in healthy/untreated brain tissue, brain expression analysis after implantation of 9L glioma cells, overview
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MMP-9 activity is increased in fibroblasts when the cells are in contact with fibronectin and laminin, while in myoblasts, enhanced activity of the secreted enzyme occurs only in presence of collagen
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
MMP9 co-localizes with cortactin and talin2 in invadopodia. Talin2-beta-integrin interaction is essential for MMP9 vesicles to attach to the ventral plasma membrane
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additional information
additional information
enzyme localization and comparison to other MMPs, immunohistochemic analysis
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additional information
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enzyme localization and comparison to other MMPs, immunohistochemic analysis
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additional information
Gallus gallus Hy-Line Brown
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enzyme localization and comparison to other MMPs, immunohistochemic analysis
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secretion of proMMP-9 from the amniochorion after application of lipopolysacchride to either sidesof the membrane is increased, overview
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additional information
talin2 controls MMP9 vesicles docking to ventral plasma membranes and secretion. Endosomal transport takes part in MMP9 trafficking. Talin2-mediated vesicle docking prevents MMP9 vesicles from being rerouted and degraded
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Highest Expressing Human Cell Lines
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
matrix metallopeptidase 9 (MMP9) is a member of zinc-metalloproteinases family
malfunction
metabolism
physiological function
additional information
malfunction
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mice that lack matrix metalloproteinase-9 display delayed wound healing associated with delayed reepithelization and disordered collagen fibrillogenesis
malfunction
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MMP-9 knockout mice are resistant to dextran sodium sulfate-, Salmonella typhimurium-, or trinitrobenzene sulfonic acid-induced colitis
malfunction
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increased levels of MMP-9 protein cause myopathy in dystrophin-deficient mdx mice. Deletion of Mmp9 gene in mdx mice improves skeletal muscle structure and functions and reduces muscle injury, inflammation and fiber necrosis. Heterozygous or homozygous deletion of MMP-9 attenuates accumulation of macrophages, fiber necrosis and improves force production in skeletal muscle of mdx mice. Genetic deletion of MMP-9 attenuates fibrosis in diaphragm of mdx mice. Genetic ablation of MMP-9 inhibits the activation of activator protein-1 and nuclear factor-kappaB transcription factors, reduces the serum level of creatine kinase and improves skeletal muscle structure in mdx mice. Genetic ablation of MMP-9 augments myofiber regeneration, improves sarcolemmal structure and augments the cellular levels of beta-dystroglycan and nNOS in skeletal muscle of mdx mice
malfunction
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in mice lacking MMP-9 the enhanced COX-1-PGE2 decreases caspase-3 expression and activity leading to impaired apoptosis of inflammatory neutrophils resulting in abnormal accumulation of the cells at the inflammatory focus
malfunction
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matrix metalloprotease-9 inhibition improves amyloid beta-mediated cognitive impairment and neurotoxicity in mice
malfunction
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while a lack of MMP-9 does not alter vein graft wall area or cellularity, grafts from MMP-9 knockout mice accumulate more collagen and have earlier linear expansive remodelling, possibly due to an early compensatory increase in MMP-2
malfunction
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matrix metalloproteinase-9 deficiency leads to prolonged foreign body response in the brain associated with increased IL-1beta levels and leakage of the blood-brain barrier, increased levels of interleukin-1beta and the delayed repair of blood-brain barrier are associated with prolongation of the foreign body response in MMP-9-null mice
malfunction
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mice that lack matrix metalloproteinase-9 display delayed wound healing associated with delayed reepithelization and disordered collagen fibrillogenesis, MMP-9-null wounds display compromised reepithelialization, reduced clearance of fibrin clots and normal tensile strength
malfunction
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MMP-9 knockdown blocks SGC-7901 cells' invasion, migration and proliferation
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MMP-9 deficiency impairs ischemia-induced neovascularization, deficiency of MMP-9 reduces endothelial progenitor cell-like cell mobilization, lack of MMP-9 attenuates C-kit-positive bone marrow cell adhesion and migration
malfunction
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inhibition of matrix metalloproteinase-9 activity by doxycycline ameliorates RANK ligand-induced osteoclast differentiation in vitro and in vivo, overview. Doxycycline treatment abrogates RANKL-induced osteoclastogenesis and TRAP activity in mouse calvaria along with the suppression of MMP9 enzyme activity, again without affecting the expression of MMP9 protein
malfunction
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the broad-spectrum inhibitor of MMPs, BB-94, markedly reduces activation of trypsinogen, levels of CXCL2, infiltration of neutrophils, and tissue damage in acute pancreatitis
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inhibition of MMP activity, especially MMP-9, has the potential to inhibit tumor growth and metastasis
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infection of chorioamniotic membranes with Escherichia coli induces an increase in the secretion of inactive forms and an association to extracellular matrix of active forms of MMP-2 and MMP-9 without changes in inhibitor TIMP-1, -2, and -4.These changes explain the significant decrease of collagen content and loss of structural continuity
malfunction
administration of MMP-9 specific siRNA to the lungs of sensitized animals would abrogate development of an asthma phenotype, with endpoints of reduced airway hypersensitivity, less inflammation and tissue remodeling, less cellular migration of lymphocytes and eosinophils, and less activation of inflammatory cells, in both BAL fluids and lung tissues
malfunction
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enzyme inhibition prevents neural crest cells delamination and migration
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a truncated 65 kDa enzyme lacks the haemopexin domain required for the high-affinity binding of the tissue inhibitor TIMP-1, and can be evaluated by activity assay in the presence of tissue inhibitor of metalloproteinases 1, TIMP-1
malfunction
in an islet culture model where human islet amyloid polypeptide transgenic mouse islets develop amyloid but nontransgenic islets do not, a broad spectrum MMP inhibitor (GM6001) and an MMP-2/9 inhibitor increases amyloid formation and the resultant beta-cell apoptosis
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in an islet culture model where human islet amyloid polypeptide transgenic mouse islets develop amyloid but nontransgenic islets do not, a broad spectrum MMP inhibitor (GM6001) and an MMP-2/9 inhibitor increases amyloid formation and the resultant beta-cell apoptosis
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the enzyme is important for tooth development. Teeth of Mmp9-/- mice displayed a phenotype similar to dentinogenesis imperfecta, including decreased dentin mineral density, abnormal dentin architecture, widened predentin and irregular predentin-dentin boundary
malfunction
treatment of brain endothelial cells with a MMP9 inhibitor (SB-3CT) mitigates Abeta-induced lipoprotein receptor shedding the brains of apoE4 animals. Administration of SB-3CT to apoE4 animals significantly enhanced Abeta clearance from the brain to the periphery following intracranial administration of Abeta. MMP9 inhibition can facilitate Abeta clearance across the BBB, which could be an effective approach to lowering Abeta levels in the brain and mitigating the AD phenotype, particularly in subjects carrying the apoE4 allele
malfunction
treatment of brain endothelial cells with a MMP9 inhibitor (SB-3CT) mitigates Abeta-induced lipoprotein receptor shedding in brain endothelial cells
malfunction
ablation of talin2 in MDA-MB-231 cells inhibits the secretion of matrix metallopeptidase 9 (MMP9), but ablation of talin2 does not inhibit MMP9 expression. In talin2-depleted cells unsecreted MMP9 vesicles are rerouted and accumulate in enlarged early, late endosomes and autophagosomes, and subsequently to lysosomes. Depletion of talin2 could result in an increase in MMP9 mRNA levels, which are probably caused by a feedback regulation. Ablation of talin2 inhibited MMP2 and MMP9 secretion and causes a reduction in MMP9 vesicles targeting to ventral plasma membrane. Enlarged MMP9 vesicles are surrounded by LC3beta autophagosome marker and localize to lysosomes in talin2-KO cells
malfunction
duality of specific MMP-9 inhibition for treatment of inflammatory bowel diseases, overview
malfunction
the levels of immunocomplexes (IC) are higher in the systemic lupus erythematosus (SLE) mouse model when MMP-9 is genetically deleted, phenotype, detailed overview. Lack of MMP-9 increase the levels of immune complexes in plasma and local complement activation in spleen and kidney in the LPR-/- mouse model of SLE. Lack of MMP-9 correlates with decreased clearance of IC in vivo. Analysis of LPR-/-MMP-9-/- double knockout mice suggests that MMP-9 plays a protective role in autoantigen clearance in SLE
malfunction
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the broad-spectrum inhibitor of MMPs, BB-94, markedly reduces activation of trypsinogen, levels of CXCL2, infiltration of neutrophils, and tissue damage in acute pancreatitis
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malfunction
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administration of MMP-9 specific siRNA to the lungs of sensitized animals would abrogate development of an asthma phenotype, with endpoints of reduced airway hypersensitivity, less inflammation and tissue remodeling, less cellular migration of lymphocytes and eosinophils, and less activation of inflammatory cells, in both BAL fluids and lung tissues
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malfunction
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treatment of brain endothelial cells with a MMP9 inhibitor (SB-3CT) mitigates Abeta-induced lipoprotein receptor shedding the brains of apoE4 animals. Administration of SB-3CT to apoE4 animals significantly enhanced Abeta clearance from the brain to the periphery following intracranial administration of Abeta. MMP9 inhibition can facilitate Abeta clearance across the BBB, which could be an effective approach to lowering Abeta levels in the brain and mitigating the AD phenotype, particularly in subjects carrying the apoE4 allele
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malfunction
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the levels of immunocomplexes (IC) are higher in the systemic lupus erythematosus (SLE) mouse model when MMP-9 is genetically deleted, phenotype, detailed overview. Lack of MMP-9 increase the levels of immune complexes in plasma and local complement activation in spleen and kidney in the LPR-/- mouse model of SLE. Lack of MMP-9 correlates with decreased clearance of IC in vivo. Analysis of LPR-/-MMP-9-/- double knockout mice suggests that MMP-9 plays a protective role in autoantigen clearance in SLE
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malfunction
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inhibition of matrix metalloproteinase-9 activity by doxycycline ameliorates RANK ligand-induced osteoclast differentiation in vitro and in vivo, overview. Doxycycline treatment abrogates RANKL-induced osteoclastogenesis and TRAP activity in mouse calvaria along with the suppression of MMP9 enzyme activity, again without affecting the expression of MMP9 protein
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malfunction
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enzyme inhibition prevents neural crest cells delamination and migration
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malfunction
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in an islet culture model where human islet amyloid polypeptide transgenic mouse islets develop amyloid but nontransgenic islets do not, a broad spectrum MMP inhibitor (GM6001) and an MMP-2/9 inhibitor increases amyloid formation and the resultant beta-cell apoptosis
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metabolism
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auto-amplified NFATc1 plays a key role in upregulating expressions of genes required for osteoclastmaturation, such as TRAP, cathepsin K, or MMP-9,which are requisite for the bone resorption processes mediated by mature osteoclasts
metabolism
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activities of MMP-9 synthesized by fibroblasts tend to be regulated by the specific extracellular protein the cells are in contact with, whereas the gelatinolytic actions of proteases produced by myoblasts are more responsive to the mechanical deformation
metabolism
determination of the concentrations of MMP-9 and proinflammatory and adaptive immunity cytokines, interleukin (IL)-1alpha, IL-1beta, interferon gamma, IL-2, IL-4, IL-6, and IL-10 in follicular fluid of women who are prepared for the in vitro fertilization procedure, and examination of the association between the women's underlying fertility problem and immunological profile
metabolism
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auto-amplified NFATc1 plays a key role in upregulating expressions of genes required for osteoclastmaturation, such as TRAP, cathepsin K, or MMP-9,which are requisite for the bone resorption processes mediated by mature osteoclasts
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physiological function
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the increased expression of MMP-9 may contribute to pathologic angiogenesis and/or to the instability of the vascular structure and could thereby cause hemorrhage in moyamoya disease
physiological function
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MMP-9 is involved in both bacterial translocation and polymorphonuclear neutrophil granulocytes transmigration in rat severe acute pancreatitis
physiological function
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MMP-9 directly delays wound healing through interference with re-epithelialization, MMP-9 interferes with the basement membrane protein structure, which in turn impedes keratinocyte migration, attachment, and the reestablishment of the epidermis
physiological function
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MMP-9 released from bone marrow-derived cells influences the progression of blood-brain barrier disruption in the ischemic brain, bone marrow-derived cell-derived MMP-9 contributes to blood-brain barrier dysfunction during early reperfusion period
physiological function
-
MMP-9 is the key factor involved in blood-brain barrier disruption and subsequent brain injury after photothrombotic cerebral ischemia in rats
physiological function
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MMP-9 is involved in cardiomyocytes contractility dysfunction, MMP-9 treatment attenuates the voltage-induced contraction of primary cardiomyocytes
physiological function
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MMP-9 activity induced by iNOS-derived NO leads to detachment of hepatocytes from the extracellular matrix and cell death, in addition to regulating leukocyte migration across extracellular matrix barriers
physiological function
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MMP-9 plays an important role in wound healing, angiogenesis, inflammation, tumor invasion, and metastasis
physiological function
-
overexpression of MMP-9 in neoplastic and inflammatory cells in GC plays an important role in the progress of this carcinoma
physiological function
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epithelial-derived MMP-9 is an important mediator of tissue injury in colitis
physiological function
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matrix metalloproteinase 9 plays a key role in lyme arthritis but not in dissemination of Borrelia burgdorferi. MMP-9 cleavage of type I collagen results in increased monocyte chemoattraction, MMP-9 plays an important role in regulating inflammation in Lyme arthritis, potentially through the cleavage of collagen type I
physiological function
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the cooperation of p38 and MMP-9 may contribute to the mucin overproduction after inflammatory challenge with 4.0 ppm of acrolein for 21 days
physiological function
-
MMP-9 plays an important role in the pathogenesis of acute graft-versus-host disease
physiological function
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changes in MMP-9 activity may be essential to the tissue reorganization necessary for ovulation in the equine ovary
physiological function
-
MMP-9 catalytically induces angiogenesis via a basic fibroblast growth factor-2/fibroblast growth factor receptor-2 pathway. The enhanced angiogenesis catalyzed by neutrophil MMP-9 evokes also a localized, low threshold level vascular endothelial growth factor/vascular endothelial growth factor receptor-2 pathway, likely functioning in the formation and/or stabilization of blood vessels
physiological function
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the recruitment of mesoangioblasts requires the secretion of MMP-9 by M2 cells
physiological function
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MMP-9 is required for tissue remodeling in response to natural hydroxyapatite
physiological function
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MMP-9- mediated occludin degradation represents an important mechanism for blood brain barrier disruption in ischemic stroke
physiological function
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activated MMP-9 degrades components of the neurovascular unit, mediates blood-brain barrier leakage, and facilitates brain edema and hemorrhage
physiological function
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MMP-9 plays an important role in the function of the blood-brain barrier, the prolonged imbalance of MMP-9 and tissue inhibitor of metalloproteinase 1 is associated with the pathogenesis of non-herpetic acute limbic encephalitis
physiological function
expression of MMP-9 mRNA is associated with abnormal apparent diffusion coefficient after global cerebral ischemia
physiological function
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matrix metalloproteinase-9 controls N-methyl-D-aspartate receptor surface diffusion through integrin beta1 signaling, enzymatic activity of MMP-9 increases lateral diffusion of NR1- N-methyl-D-aspartate receptors without cleavage of NR subunits, MMP-9 does not affect GluR2-alpha-amino-3-hydroxy-5-methyl-4-isoxazole-propionic acid receptor surface diffusion, MMP-9 affects N-methyl-D-aspartate receptors lateral diffusion via integrin signaling
physiological function
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MMP-9 plays a causative role in blood-brain barrier disruption after peripheral thermal injury
physiological function
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MMP-9 plays a causal role in amyloid beta-induced cognitive impairment and neurotoxicity
physiological function
-
MMP-9 plays a pivotal role in vascular remodeling and development of atherosclerotic lesion
physiological function
-
MMP-9 is essential for ischemia-induced neovascularization by modulating bone marrow-derived endothelial progenitor cells
physiological function
-
MMP-9 soluble pro-enzyme is implicated in pathological events including cancer invasion. During skin wound healing, MMP-9 is expressed by the migrating leading-edge keratinocytes upon re-epithelialization of the wound
physiological function
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MMP-9 is involved in the mechanism of cell-to-cell HIV-1 endocytosis in dendritic cells
physiological function
-
neutrophil-derived matrix metalloproteinase-9 is a potent activator of trypsinogen in acinar cells in acute pancreatitis
physiological function
-
MMPs can promote cancer cell invasion by degradation of various extracellular matrix components resulting in release of growth factor and cytokines
physiological function
-
MMP-9 significantly induced Smad3 phosphorylation and subsequent fibroblast proliferation. MMP cleaves membrane-bound precursor proteins and releases epidermal growth factor-like ligands that subsequently bind to epidermal growth factor receptor, and it stimulates the airway epithelium to produce fibrogenic mediators through activation of membrane-bound receptors. MMP-9 is required to cleave membrane-bound growth factors
physiological function
-
MMP-9 has a role as essential mediator in degradation/damage of the extracellular matrix of fetal membranes
physiological function
the enzyme act as important oncogenes that improve invasiveness of cancer cells. MMP-9 activity is constitutively heightened in tissue samples from primary glioblastoma multiforme, the most common and aggressive malignant primary brain tumor in humans
physiological function
-
enzyme matrix metalloproteinase 9/gelatinase B is required for neural crest cell migration, which are neuroepithelial progenitors that convert into mesenchyme and migrate along defined paths throughout the embryo. The enzyme plays a role during neural crest cell detachment from the neural tube, overview
physiological function
matrix metalloproteinase-9 reduces islet amyloid formation by degrading islet amyloid polypeptide, the constituent of amyloid deposits in Alzheimer's disease
physiological function
because islet MMP-9 mRNA levels are decreased in type 2 diabetic subjects, islet MMP-9 activity may also be decreased in human type 2 diabetes, thereby contributing to increased islet amyloid deposition and beta-cell loss. Matrix metalloproteinase-9 reduces islet amyloid formation by degrading islet amyloid polypeptide, the constituent of amyloid deposits in Alzheimer's disease
physiological function
matrix metalloproteinase-9 is a phase-specific effector molecule, independent from Fas, in experimental autoimmune encephalomyelitis. MMP-9 triggers multiple sclerosis and the animal model of experimental autoimmune encephalomyelitis by the breakdown of the blood-brain barrier
physiological function
potential role of the MMP system in avian oviduct development, avian reproductive system differs from that of mammals. The gelatinases, stromelysins and matrilysins, all belonging to the MMP family, are capable of degrading major constituents of basement membranes, including type IV collagen, laminin and fibronectin. Gelatinolytic activity of MMPs in the chicken oviduct during maturation, overview
physiological function
variations in MMP-9 isoforms are observed, which coincide with the progression of tuberculosis infection. MMP-9 isoforms might influence the formation and progression of granuloma
physiological function
matrix metalloproteinase 9 (MMP9) is involved in apolipoprotein E2 receptor proteolytic shedding at the cell surface. Lipoprotein receptor transport across the blood-brain barrier (BBB) mediates beta-amyloid (Abeta) accumulation in the brain and may be a contributing factor in Alzheimer's disease pathogenesis. MMP9 impacts lipoprotein receptor shedding and Abeta transit across the BBB, in an apoE isoform-specific manner
physiological function
matrix metalloproteinase 9 (MMP9) is involved in apolipoprotein E2 receptor proteolytic shedding at the cell surface. Lipoprotein receptor transport across the blood-brain barrier (BBB) mediates beta-amyloid (Abeta) accumulation in the brain and may be a contributing factor in Alzheimer's disease pathogenesis. Treatment with MMP9 dose-dependently elevates lipoprotein receptor shedding in brain endothelial cells
physiological function
matrix metallopeptidase 9 (MMP9) is one of the key proteins required for cancer invasion and invadopodia formation. MMP9 is a proteinase involved in extracellular matrix degradation in invadopodium maturation and metastasis. Talin2, localized to invadopodia, mediates MMP9 secretion to modulate invadopodium maturation and cell invasio. Talin2 controls MMP9 vesicles docking to ventral plasma membranes and secretion
physiological function
enzyme MMP9 is involved in both systemic and local pathologies. Active MMP-9 efficiently cleaves and complexes plasma alpha-2-macroglobulin (alpha2M) in human plasma
physiological function
upon knockout of either MMP2 (EC 3.4.24.24) or MMP9 or both, MMP2 is found to be involved merely in intramembranous ossification which leads to a smaller skull and inferior cortical parameters upon its loss. MMP9 is found to affect only the endochondral ossification process, which leads to shorter long-bones in its absence. Double knockout mice demonstrate a combination of both the skull and long bone phenotypes as found in the single-knockouts, and not a severer additive phenotype
physiological function
-
the matrix metalloproteinases (MMPs) are involved in plaque formation by degrading the extracellular matrix to weaken the arterial wall and cause cardiovascular remodeling. Matrix metallopeptidase 9 (MMP9) contributes to the beginning of plaque. Active human MMP9 (act-hMMP9) increases gene and protein expressions of MCP-1, ICAM-1, and VCAM-1 in human coronary artery smooth muscle cells (HCASMCs), and enhances macrophage adhesion. Serum MMP9 is measured and it correlates with carotid artery or coronary artery plaques. MMP-9 is involved in atherosclerotic plaque rupture and tissue remodeling after a cardiac event. act-hMMP9 promotes MCP-1 expression in HCASMCs through ERK1/2/NFkB signaling pathway. In addition to ERK1/2, act-hMMP9 induces NFkappaB activity. act-hMMP9 activates ICAM-1 and VCAM-1 expressions through the P38MAPK/NFkappaB signaling pathway
physiological function
absence of a causative role of MMP-9 in the pathology in animal models of inflammatory bowel diseases (IBD). Endotoxins, crossing the intestinal barrier, induce massive local release of both neutrophil collagenase (MMP-8) and gelatinase B (MMP-9). MMPs modify the activities of cytokines, chemokines and their receptors. MMPs and TIMPs act in an interactive network, possibly having also beneficial effects on IBD evolution. MMP-9 potentiates IL-8/CXCL-8, the most potent neutrophil chemokine, at least 10fold, neutrophils have a central role in inflammatory bowel disease
physiological function
matrix metallopeptidase 9 (MMP-9) dissolves immune complexes from blood samples of systemic lupus erythematosus (SLE) patients. In SLE, mainly intracellular autoantigens generate autoantibodies and these assemble into immune complexes and activate the classical pathway of the complement system enhancing inflammation. Autoantigens incorporated into immune complexes, but not immunoglobulin heavy or light chains, are cleaved by MMP-9. Role of MMP-9 in the clearance of autoantigens, autoantibodies and immune complexes
physiological function
in systemic lupus erythematosus (SLE), mainly intracellular autoantigens generate autoantibodies and these assemble into immune complexes and activate the classical pathway of the complement system enhancing inflammation. Autoantigens incorporated into immune complexes, but not immunoglobulin heavy or light chains, are cleaved by MMP-9. MMP-9 plays a protective role in autoantigen clearance in SLE, role of MMP-9 in the clearance of autoantigens, autoantibodies and immune complexes. MMP-9 dissolves immune complexes from plasma of lupus-prone LPR-/-/MMP-9-/- mice
physiological function
the number of healthy intact embryos achieved is significantly higher in patients with a positive pregnancy (PPG) test than in those with a negative pregnancy (NPG) test, and it is negatively correlated with interleukin (IL)-8 concentrations in follicular fluid
physiological function
matrix metallopeptidase 9 is a host protein target for chloroquine and melatonin in immunoregulation during COVID-19. Melatonin appears to be the more promising repurposed drug against MMP9 for better immunocompromisation in COVID-19. Analysis of protein-protein interaction (PPI) and chemo-protein interaction (CPI) networks in blood samples from patients with COVID-19, identification of top-ranked sub-network and hub-bottleneck nodes within the interactome model of PPI-CPI network for COVID-19, overview. MMP9 shows functional annotations associated with neutrophil mediated immunoinflammation. Angiotensin converting enzyme 2, a membrane receptor of SARS-CoV-2 virus, might have functional cooperativity with MMP9 and possible interaction with both drugs
physiological function
-
neutrophil-derived matrix metalloproteinase-9 is a potent activator of trypsinogen in acinar cells in acute pancreatitis
-
physiological function
-
matrix metalloproteinase 9 (MMP9) is involved in apolipoprotein E2 receptor proteolytic shedding at the cell surface. Lipoprotein receptor transport across the blood-brain barrier (BBB) mediates beta-amyloid (Abeta) accumulation in the brain and may be a contributing factor in Alzheimer's disease pathogenesis. MMP9 impacts lipoprotein receptor shedding and Abeta transit across the BBB, in an apoE isoform-specific manner
-
physiological function
-
in systemic lupus erythematosus (SLE), mainly intracellular autoantigens generate autoantibodies and these assemble into immune complexes and activate the classical pathway of the complement system enhancing inflammation. Autoantigens incorporated into immune complexes, but not immunoglobulin heavy or light chains, are cleaved by MMP-9. MMP-9 plays a protective role in autoantigen clearance in SLE, role of MMP-9 in the clearance of autoantigens, autoantibodies and immune complexes. MMP-9 dissolves immune complexes from plasma of lupus-prone LPR-/-/MMP-9-/- mice
-
physiological function
-
enzyme matrix metalloproteinase 9/gelatinase B is required for neural crest cell migration, which are neuroepithelial progenitors that convert into mesenchyme and migrate along defined paths throughout the embryo. The enzyme plays a role during neural crest cell detachment from the neural tube, overview
-
physiological function
-
matrix metalloproteinase-9 reduces islet amyloid formation by degrading islet amyloid polypeptide, the constituent of amyloid deposits in Alzheimer's disease
-
physiological function
Gallus gallus Hy-Line Brown
-
potential role of the MMP system in avian oviduct development, avian reproductive system differs from that of mammals. The gelatinases, stromelysins and matrilysins, all belonging to the MMP family, are capable of degrading major constituents of basement membranes, including type IV collagen, laminin and fibronectin. Gelatinolytic activity of MMPs in the chicken oviduct during maturation, overview
-
additional information
-
specific inhibition of MMP-9 leads to reduced extents of HIV-1 antigen presentation activity
additional information
F1NGT3
enzymes MMP1, MMP3, and MMP9 are synthesized and secreted by granulosa cells of different follicles in the chicken ovary, overview. The three MMP genes (MMP1, MMP3, and MMP9) are significantly upregulated in 23-wk-old (laying phase) chicken ovaries compared with 6-wk-old ovaries (prepubertal phase). In reproductively active chicken ovary, MMP1 expression (both mRNA and protein) remains low in prehierarchical and preovulatory follicles but increases in postovulatory follicles (POFs). Both MMP3 and MMP9 expression levels increase during follicular maturation. MMP3 reaches maximal expression in the first largest follicle (F1), while MMP9 levels continue to rise in POF1 and POF2 after ovulation
additional information
-
digestion of the intact enzyme with chondroitinase decreases the size of the molecule to 80 kDa
additional information
the enzyme cleaves many substrates and is produced by most cell types as a zymogen, proMMP-9, in complex with the tissue inhibitor of metalloproteinases-1, TIMP-1, molecular modelling, overview
additional information
-
enzyme MMP9 promotes neural crest cell emigration from the neural tube by enhancing breakage of laminin at the basement-membrane, mechanism of activity, overview
additional information
four isoforms of MMP-9 have been reported: the first is a latent form, a zymogen of 92 kDa. The second is obtained by cutting the prodomain of the latent form, resulting in a product of 82 kDa, which produces the active form of the enzyme. The third isoform is a heterodimer that originates from the binding of MMP-9 with the inhibitor TIMP-1, generating a product of 220 kDa. Finally, the fourth isoform corresponds to a 125 kDa heterodimer, made up of MMP-9 associated with lipocalin. Analysis of MMP-9 isoforms identification and determination of activities
additional information
-
four isoforms of MMP-9 have been reported: the first is a latent form, a zymogen of 92 kDa. The second is obtained by cutting the prodomain of the latent form, resulting in a product of 82 kDa, which produces the active form of the enzyme. The third isoform is a heterodimer that originates from the binding of MMP-9 with the inhibitor TIMP-1, generating a product of 220 kDa. Finally, the fourth isoform corresponds to a 125 kDa heterodimer, made up of MMP-9 associated with lipocalin. Analysis of MMP-9 isoforms identification and determination of activities
additional information
monomeric active matrix metalloprotease-9 is efficiently trapped by human plasma alpha-2-macroglobulin, while homotrimeric MMP-9 is an active hitchhiker on alpha-2-macroglobulin partially escaping protease inhibition and internalization. alpha-2-Macroglobulin/trimer complexes escape clearance through the receptor low-density lipoprotein receptor-related protein 1, LRP-1, also known as the alpha-2-macroglobulin receptor. Matrix metalloprotease-9 monomers and trimers are completely different as multimerization enables active matrix metalloprotease-9 to partially avoid alpha-2-macroglobulin regulation both by direct protease inhibition and by removal from the extracellular space by receptor-mediated endocytosis. MMP-9 has an extreme degree of flexibility due to the presence of a central O-glycosylated domain. Endocytosis of alpha2M*/MMP-9 trimer complexes is less efficient than alpha2M*/MMP-9 monomer complexes and hence escapes clearance from the extracellular environment
additional information
MMPs exist as mixtures of proteoforms with different posttranslational modifications and with different specific activities
additional information
-
enzymes MMP1, MMP3, and MMP9 are synthesized and secreted by granulosa cells of different follicles in the chicken ovary, overview. The three MMP genes (MMP1, MMP3, and MMP9) are significantly upregulated in 23-wk-old (laying phase) chicken ovaries compared with 6-wk-old ovaries (prepubertal phase). In reproductively active chicken ovary, MMP1 expression (both mRNA and protein) remains low in prehierarchical and preovulatory follicles but increases in postovulatory follicles (POFs). Both MMP3 and MMP9 expression levels increase during follicular maturation. MMP3 reaches maximal expression in the first largest follicle (F1), while MMP9 levels continue to rise in POF1 and POF2 after ovulation
-
additional information
-
enzyme MMP9 promotes neural crest cell emigration from the neural tube by enhancing breakage of laminin at the basement-membrane, mechanism of activity, overview
-
Show AA Sequence and Transmembrane Helices (1137 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
103000
-
x * 103000, about, pro-MMP9, SDS-PAGE, x * 86000, about, activated MMP-9, SDS-PAGE
105000
-
the molecular mass of recombinant MMP-9 is approximately 105000 Da, SDS-PAGE
130000
135000
-
neutrophil gelatinase-associated lipocalin-MMP-9 complex, SDS-PAGE
150000
-
gelatinolytic activity of MMP-9 is observed at two molecular weights, 150000 Da and 92000 Da, the 150000 Da band represents a complex of MMP-9 with itself, other matrix metallproteinases, or other molecules such as TIMPs or inflammatory molecules
20947
-
x * 70795, calculated, enzyme mutant E402A, x * 20947, calculated, isolated enzyme collagen-binding domain
225000
230000
-
x * 80000, deglycosylated enzyme, SDS-PAGE, x * 230000, glycosylated enzyme, SDS-PAGE
65000
65000 - 82000
major circulating MMP-9 enzyme forms: 92 kDa proMMP-9, and active 82 kDa and 65 kDa enzyme forms
70795
-
x * 70795, calculated, enzyme mutant E402A, x * 20947, calculated, isolated enzyme collagen-binding domain
80000
-
x * 80000, deglycosylated enzyme, SDS-PAGE, x * 230000, glycosylated enzyme, SDS-PAGE
82000
84000
85000
-
85000 Da polypeptide in both cellular and secreted parasite extracts, activated form of MMP-9, SDS-PAGE
86000
88000
89300
x * 89300, about, SDS-PAGE, the natural zymogen proMMP-9 occurs as monomers, homomultimers and heterocomplexes. MMP-9 homomultimers are reduction-sensitive trimers, three-dimensional structure molecular modeling, overview. Homomultimerization of the enzyme involves cysteine bridge formation. The zymogen proMMP-9 monomer includes the propeptide, the fibronectin-like domain, the Zn2+ -binding domain, the catalytic domain, the flexible OG domain, and the haemopexin-like domain
92000
94000
97000
130000
-
x * 92000,enzyme form 1, SDS-PAGE, x * 130000, enzyme form 2, SDS-PAGE, x * 225000, enzyme form 3, SDS-PAGE
225000
-
x * 92000,enzyme form 1, SDS-PAGE, x * 130000, enzyme form 2, SDS-PAGE, x * 225000, enzyme form 3, SDS-PAGE
65000
-
4-aminophenylmercuric acetate produces not only the 82000 Da active enzyme but also a C-terminal truncated form of approximately 65000 Da with activity comparable to that of the 82000 Da form
65000
x * 65000, active matured, truncated enzyme form lacking both the N- and C-terminal domains, SDS-PAGE, x * 82000, activated mature enzyme, SDS-PAGE
82000
-
x * 92000, full-length pro-MMP-9, SDS-PAGE, x * 82000, processed active MMP-9, SDS-PAGE
82000
-
1 * 92000, pro-enzyme, SDS-PAGE, 1 * 82000, recombinant truncated mutant MMP-9, SDS-PAGE
82000
x * 65000, active matured, truncated enzyme form lacking both the N- and C-terminal domains, SDS-PAGE, x * 82000, activated mature enzyme, SDS-PAGE
84000
-
1 * 92000, human SC40-transformed lung cells, proenzyme, SDS-PAGE, 1 * 84000, human SC40-transformed lung cells, activated form, SDS-PAGE
86000
-
x * 103000, about, pro-MMP9, SDS-PAGE, x * 86000, about, activated MMP-9, SDS-PAGE
86000
-
x * 92000, pro-MMP-9, SDS-PAGE, x * 86000, activated MMP-9, SDS-PAGE
86000
-
x * 92000, pro-MMP9, SDS-PAGE, x * 86000, activated MMP-9, SDS-PAGE
92000
-
human SC40-transformed lung cells, gel filtration, glycosylated proenzyme can be activated by organomercurials by removal of 73 amino acids
92000
-
gelatinolytic activity of MMP-9 is observed at two molecular weights, 150000 Da and 92000 Da, the 92000 Da form corresponds to the MMP-9 pro form
92000
-
x * 92000, full-length pro-MMP-9, SDS-PAGE, x * 82000, processed active MMP-9, SDS-PAGE
92000
-
x * 92000, pro-MMP-9, SDS-PAGE, x * 86000, activated MMP-9, SDS-PAGE
92000
-
x * 92000, pro-MMP9, SDS-PAGE, x * 86000, activated MMP-9, SDS-PAGE
92000
-
1 * 92000, pro-enzyme, SDS-PAGE, 1 * 82000, recombinant truncated mutant MMP-9, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
monomer
monomer or homotrimer
MMP-9 has an extreme degree of flexibility due to the presence of a central O-glycosylated domain. This configuration allows independent movement of the N-terminal and C-terminal domains, and allows MMP-9 to crawl along collagen fibrils in search for damaged regions. MMP-9 also forms circle-shaped covalently linked homotrimers which share a similar degree of flexibility. In human plasma, active MMP-9 is efficiently complexed to alpha-2-macroglobulin (alpha2M), resulting in a shift of active MMP-9 into high molecular weight complexes. Although both forms activate and bind alpha2M, alpha2M*/MMP-9 trimer complexes are subjected to reduced alpha2M anti-proteolytic activity, making the alpha2M*/MMP-9 monomer and alpha2M*/MMP-9 trimer complexes functionally completely different in nature
additional information
?
-
x * 80000, deglycosylated enzyme, SDS-PAGE, x * 230000, glycosylated enzyme, SDS-PAGE
?
Gallus gallus Hy-Line Brown
-
x * 82000, mature active enzyme, SDS-PAGE
-
?
-
x * 70795, calculated, enzyme mutant E402A, x * 20947, calculated, isolated enzyme collagen-binding domain
?
-
x * 92000, full-length pro-MMP-9, SDS-PAGE, x * 82000, processed active MMP-9, SDS-PAGE
?
-
x * 92000,enzyme form 1, SDS-PAGE, x * 130000, enzyme form 2, SDS-PAGE, x * 225000, enzyme form 3, SDS-PAGE
?
x * 89300, about, SDS-PAGE, the natural zymogen proMMP-9 occurs as monomers, homomultimers and heterocomplexes. MMP-9 homomultimers are reduction-sensitive trimers, three-dimensional structure molecular modeling, overview. Homomultimerization of the enzyme involves cysteine bridge formation. The zymogen proMMP-9 monomer includes the propeptide, the fibronectin-like domain, the Zn2+ -binding domain, the catalytic domain, the flexible OG domain, and the haemopexin-like domain
?
x * 65000, active matured, truncated enzyme form lacking both the N- and C-terminal domains, SDS-PAGE, x * 82000, activated mature enzyme, SDS-PAGE
?
-
x * 103000, about, pro-MMP9, SDS-PAGE, x * 86000, about, activated MMP-9, SDS-PAGE
dimer
-
2 * 60000-65000, extracellular proteolytically active disulfide-linked MMP-9 dimers, SDS-PAGE
monomer
-
1 * 92000, human SC40-transformed lung cells, proenzyme, SDS-PAGE, 1 * 84000, human SC40-transformed lung cells, activated form, SDS-PAGE
monomer
-
1 * 92000, pro-enzyme, SDS-PAGE, 1 * 82000, recombinant truncated mutant MMP-9, SDS-PAGE
additional information
-
the recombinant enzyme forms mixtures of monomers and other higher oligomeric species, structural model of multidomain full-length pro-MMP-9, including the unique proline-rich and heavily O-glycosylated OG domain, combining small-angle X-ray scattering with single-molecule atomic force microscopy imaging to characterize a full-length structural model of pro-MMP-9, overview
additional information
four isoforms of MMP-9 have been reported: the first is a latent form, a zymogen of 92 kDa. The second is obtained by cutting the prodomain of the latent form, resulting in a product of 82 kDa, which produces the active form of the enzyme. The third isoform is a heterodimer that originates from the binding of MMP-9 with the inhibitor TIMP-1, generating a product of 220 kDa. Finally, the fourth isoform corresponds to a 125 kDa heterodimer, made up of MMP-9 associated with lipocalin. Analysis of MMP-9 isoforms identification and determination of activities
additional information
-
four isoforms of MMP-9 have been reported: the first is a latent form, a zymogen of 92 kDa. The second is obtained by cutting the prodomain of the latent form, resulting in a product of 82 kDa, which produces the active form of the enzyme. The third isoform is a heterodimer that originates from the binding of MMP-9 with the inhibitor TIMP-1, generating a product of 220 kDa. Finally, the fourth isoform corresponds to a 125 kDa heterodimer, made up of MMP-9 associated with lipocalin. Analysis of MMP-9 isoforms identification and determination of activities
additional information
-
molecular modeling of the three-dimensional structure of the MMP-9/TIMP-1 complex, overview
additional information
-
MMP-9 is composed of the classical MMP domains including the pro-, catalytic, zinc-binding, and hemopexin domains. MMP-9 contains three fibronectin type II repeats facilitating its binding to collagen. An O-glycosylated linker region unique for MMP-9 connects the protease domain with the hemopexin domains
additional information
-
molecular modeling of the three-dimensional structure of the MMP-9/TIMP-1 complex, overview
-
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
proteolytic modification
additional information
glycoprotein
-
the enzyme contains covalently bound glycosaminoglycan i.e. chondroitin sulfate chains, deglycosylation by protease-free chondroitinase ABC
glycoprotein
the enzyme is O-glycosylated at Trp116-Lys214 sequence of the C-terminal part
proteolytic modification
-
MMP-3 and hemin activate MMP-9 cleaving at Glu40-Met41 and Arg87-Phe88, and at Glu40-Met41 and Leu52-Leu53, respectively, overview
proteolytic modification
-
activation by trypsin, MMP3, and MMP10, kinetics, overview
proteolytic modification
-
4-aminophenylmercuric acetate proteolytically activates the enzyme
proteolytic modification
-
the inactive zymogen is cleaved at the pro-peptide and activated to the mature MMP-9
proteolytic modification
the enzyme is produced by most cell types as a zymogen, proMMP-9
proteolytic modification
enzyme MMP-9 is released in the inactive form as proenzyme as proMMP-9/TIMP-1 complex or as TIMP-1 free protein. Activation of MMP-9 requires a complex network of mechanisms involving other matrix metalloproteases. In vitro activation of enzyme matrix metalloproteinase-9 with MMP-3, EC 3.4.24.17, shows the presence of two different forms: an 82 kDa, N-terminal truncated form, and a 65 kDa, N- and C-terminal truncated form. 4-Aminophenylmercuric acetate activation induces an autoproteolytic activation causing the removal of the propeptide followed by a further breakage and subsequent formation of a N- and C-truncated form of 67 kDa
proteolytic modification
activation of pro-MMP-2 with 1 mM APMA (p-aminophenylmercuric acetate) overnight at 37°C, in buffer containing 50 mM Tris-HCl, pH 7.5, 150 mM NaCl, 10 mM CaCl2, and 0.05% Brij L23
proteolytic modification
-
acrolein stimulates pro-MMP-9 cleavage and activation
additional information
-
digestion of the intact enzyme with chondroitinase decreases the size of the molecule to 80 kDa
additional information
-
activation of pro-MMP-2 by 4-aminophenylmercuric acetate
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E402A
P574R
-
the mutant is associated with a non-significant decreased risk of coronary artery disease when compared with the wild type genotype
R279Q
R668Q
-
the mutant is associated with a non-significant decreased risk of coronary artery disease when compared with the wild type genotype
E402H/H411E
-
site-directed mutagenesis, proteolytic inactive MMP-9 mutant, application of the MMP-9 mutant decreases portal and periportal accumulation of collagen and inhibits fibrogenesis induced by CCl4 in mice
E402Q
-
site-directed mutagenesis, proteolytic inactive MMP-9 mutant, application of the MMP-9 mutant decreases portal and periportal accumulation of collagen and inhibits fibrogenesis induced by CCl4 in mice, the MMP-9 mutant suppresses transdifferentiation of hepatic stellate cells to the myofibroblast-like phenotype in vitro and in vivo. Adenoviral application of the mutant leads to increased apoptosis of activated hepatic stellate cells
H401A
-
site-directed mutagenesis, proteolytic inactive MMP-9 mutant, application of the MMP-9 mutant decreases portal and periportal accumulation of collagen and inhibits fibrogenesis induced by CCl4 in mice, the MMP-9 mutant suppresses transdifferentiation of hepatic stellate cells to the myofibroblast-like phenotype in vitro and in vivo. Adenoviral application of the mutant leads to increased apoptosis of activated hepatic stellate cells
E402H/H411E
-
site-directed mutagenesis, proteolytic inactive MMP-9 mutant, application of the MMP-9 mutant decreases portal and periportal accumulation of collagen and inhibits fibrogenesis induced by CCl4 in mice
-
E402Q
-
site-directed mutagenesis, proteolytic inactive MMP-9 mutant, application of the MMP-9 mutant decreases portal and periportal accumulation of collagen and inhibits fibrogenesis induced by CCl4 in mice, the MMP-9 mutant suppresses transdifferentiation of hepatic stellate cells to the myofibroblast-like phenotype in vitro and in vivo. Adenoviral application of the mutant leads to increased apoptosis of activated hepatic stellate cells
-
H401A
-
site-directed mutagenesis, proteolytic inactive MMP-9 mutant, application of the MMP-9 mutant decreases portal and periportal accumulation of collagen and inhibits fibrogenesis induced by CCl4 in mice, the MMP-9 mutant suppresses transdifferentiation of hepatic stellate cells to the myofibroblast-like phenotype in vitro and in vivo. Adenoviral application of the mutant leads to increased apoptosis of activated hepatic stellate cells
-
additional information
E402A
-
no enzymic activity, competition with isolated collagen-binding domain and with matrix metalloproteinase MMP-2 binding to native and denatured type I collagen
E402A
-
site-directed mutagenesis of the catalytic Glu402 results in an inactive enzyme
R279Q
-
there is no relationship between R279Q polymorphism and atrial fibrillation hypertensive heart disease patients of Chinese Han population
R279Q
-
the mutant is associated with a non-significant decreased risk of coronary artery disease when compared with the wild type genotype
additional information
-
recombinant enzyme collagen-binding domain, competition with binding to gelatin of either enzyme mutant E402A or matrix metalloproteinase MMP-2 mutant E404A
additional information
-
construction of proteolytically inactive truncated MMP-9 mutant: MMP-9DELTAHem, lacking the hemopexin domain, MMP-9DELTAOG, lacking the OG domain, and MMP-9DELTAOGHem, lacking both the hemopexin and the OG domain
additional information
-
the functional-1562C/T polymorphism is associated with schizophrenia
additional information
-
the -1562CNT polymorphism of MMP-9 gene is significantly associated with atrial fibrillation risk in Chinese Han patients with hypertensive heart disease
additional information
-
no difference in MMP-9 C-1562T polymorphism is observed between multiple sclerosis and healthy subjects, whereas (CA)n genotypes and alleles are associated with multiple sclerosis
additional information
-
variant genotypes -1562 CT/TT, 279 RQ/QQ, 574 PR/RR and 668 RQ/QQ have a 51% decreased risk of coronary artery disease
additional information
-
patients with bipolar mood disorder had significant preponderance of T allele versus C allele of 1562C/T polymorphism of the MMP-9 gene
additional information
generation of the catalytically inactive mutant of zymogen proMMP-9, proMMP-9 MutE
additional information
in an islet culture model where human islet amyloid polypeptide transgenic mouse islets develop amyloid but nontransgenic islets do not, a broad spectrum MMP inhibitor (GM6001) and an MMP-2/9 inhibitor increases amyloid formation and the resultant beta-cell apoptosis
additional information
-
in an islet culture model where human islet amyloid polypeptide transgenic mouse islets develop amyloid but nontransgenic islets do not, a broad spectrum MMP inhibitor (GM6001) and an MMP-2/9 inhibitor increases amyloid formation and the resultant beta-cell apoptosis
additional information
U2OS cells are transfected with MMP9-DsRed and plated onto Oregon Green 488-labeled gelatin. Cells are then fixed and stained for talin2. Enzyme MMP9 co-localizes with cortactinand talin2 at the digestion holes in invadopodia
additional information
-
human act-hMMP9 injection increases wall thickness and reduces inner circumference of the carotid arteries in mice a T2DM mouse mode (early atherosclerosis development in diabetes). act-hMMP9 injection increases lipid accumulation and Galectin-3+ macrophage accumulation in the carotid arteries, phenoytpes, detailed overview
additional information
-
enzyme-deficient MPP-9-/- mice show impaired neutrophil infiltration during zymosan peritonitis, overview
additional information
-
MMP-9 knockout mice show delayed inflammatory response and macrophage infiltration in gastritis
additional information
-
MMP-9 mutants reduce type I collagen protein, TIMP-1, and MMP-2 expression in vivo, overview
additional information
-
MMP-9-deficient mice show eliminated elastin breakdown in coronary artery in the Kawasaki disease
additional information
-
MMP-9-/- mice show reduced bacterial burdens in pulmonary and extrapulmonary tissues, less extensive histopathology predominated by neutrophils, and decreased morbidity and mortality compared to wild-type mice, MMP-9-/- mice are able to resolve infection with either the virulence-attenuated type B, live vaccine strain, or the highly virulent type A strain of Francisella tularensis, overview
additional information
-
MMP-9 deprived mice show impaired polymorphonuclear leukocyte infiltration at infalmmation sites, overview
additional information
-
generation of a mutant version lacking the O-glycosylated linker region and hemopexin domains and containing only the protease domain, residues 1-447
additional information
in an islet culture model where human islet amyloid polypeptide transgenic mouse islets develop amyloid but nontransgenic islets do not, a broad spectrum MMP inhibitor (GM6001) and an MMP-2/9 inhibitor increases amyloid formation and the resultant beta-cell apoptosis
additional information
-
in an islet culture model where human islet amyloid polypeptide transgenic mouse islets develop amyloid but nontransgenic islets do not, a broad spectrum MMP inhibitor (GM6001) and an MMP-2/9 inhibitor increases amyloid formation and the resultant beta-cell apoptosis
additional information
-
MMP-9 mutants reduce type I collagen protein, TIMP-1, and MMP-2 expression in vivo, overview
-
additional information
-
MMP-9 deprived mice show impaired polymorphonuclear leukocyte infiltration at infalmmation sites, overview
-
additional information
-
enzyme-deficient MPP-9-/- mice show impaired neutrophil infiltration during zymosan peritonitis, overview
-
additional information
-
MMP-9 knockout mice show delayed inflammatory response and macrophage infiltration in gastritis
-
additional information
-
in an islet culture model where human islet amyloid polypeptide transgenic mouse islets develop amyloid but nontransgenic islets do not, a broad spectrum MMP inhibitor (GM6001) and an MMP-2/9 inhibitor increases amyloid formation and the resultant beta-cell apoptosis
-
additional information
-
MMP-9-/- mice show reduced bacterial burdens in pulmonary and extrapulmonary tissues, less extensive histopathology predominated by neutrophils, and decreased morbidity and mortality compared to wild-type mice, MMP-9-/- mice are able to resolve infection with either the virulence-attenuated type B, live vaccine strain, or the highly virulent type A strain of Francisella tularensis, overview
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
the 230 kDa enzyme does not remain intact in 4 M urea, 0.5 M NaCl, 4 M CsCl or 4 M GdHCl
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, stored in 50% glycerol, complete retention of activity forat least 1 month
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme from serum samples by concanavalin-A and gelatin afffinity chromatography, and ultrafiltration
native enzyme from tibia by gelatin-agarose affinity chromatography, anion exchange chromatography, and dialysis
-
purification, refolding and in vitro recovery of active full length recombinant human gelatinase MMP-9
recombinant enzyme
recombinant full-length proMMP-9 and mutant enzymes from Spodoptera frugiperda Sf9 insect cells
-
recombinant secreted mutant enzymes from Hep-G2 cells by gelatin affinity chromatography to homogeneity
-
recombinant wild-type and mutant zymogen from Sf9 insect cells by gelatin affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cDNA encoding the catalytic domain cloned into pCDNA3 and used to transfect HEK 293 cells
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expression in the form of inclusion bodies in Escherichia coli BL21, using pET21a vector
expression of full-length proMMP-9 and of mutant enzymes in Spodoptera frugiperda Sf9 insect cells using the baculovirus infection system
-
expression of mutant enzymes in Hep-G2 cells using recombinant adenoviral vectors adenovirus-2 or adenovirus-5, secretion of the recombinant enzymes, overview
-
expression of wild-type full-length MMP-9 and of a mutant version lacking the O-glycosylated linker region and hemopexin domains in Drosophila melanogaster S2 cells using the Drosophila metallothionein promoter, the native MMP-9 signal peptide is utilized for secretion contained in the beginning of the sequences
-
gene MMP-9, quantitative real time PCR expression analysis in glioblastoma
gene MMP9, cloning of an enzyme fragment, containing an ATG start codon, signal peptide, prodomain sequence, active site, fibronectin II repeat domain and zinc binding sequence,from chondrocyte cDNA, stable recombinant expression in a rat chondrosarcoma cell line
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gene MMP9, quantitative real-time PCR enzyme expression analysis
gene mmp9, quantitative reverse transcriptase PCR enzyme expression analysis
gene MMP9, quantitative RT-PCR enzyme expression analysis
recombinant expression of the wild-type and mutant zymogen in Spodoptera frugiperda Sf9 cells
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
0.025-0.1 mM 6-hydroxydopamine and 0.05-0.5 mM 1-methyl-4-phenylpyridinium ion increase MMP-9 gene expression in a dose-dependent manner by inducing nuclear factor-kappaB and AP-1 binding to the MMP-9 promoter, N-acetylcysteine suppresses both 6-hydroxydopamine- and 1-methyl-4-phenylpyridinium ion-induced MMP-9 promoter activities, LY294002, suppresses 6-hydroxydopamine- and 1-methyl-4-phenylpyridinium ion-induced MMP-9 promoter activities, whereas SB203580 inhibits 6-hydroxydopamine-, but not 1-methyl-4-phenylpyridinium ion-induced promoter activity, neither PD98059 nor SP600125 influence 6-hydroxydopamine or 1-methyl-4-phenylpyridinium ion-induced MMP-9 promoter activity
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10 ng/ml transforming growth factor-beta1 and 10 ng/ml transforming growth factor-beta2 enhance the secretion of matrix metalloproteinase-9 in PC-3 cells 5.4fold and 4.3fold, respectively
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10 nM 12-O-tetradecanoyl phorbol-13-acetate induces MMP-9 expression (9728.9% of the control) after 24 h by the suppression of the Raf/MEK/ERK pathway in MCF-7 human breast cancer cells, 12-O-tetradecanoyl phorbol-13-acetate-induced MMP-9 expression is significantly inhibited by UO126, but not by SP600125 and SB203580
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10% (v/v) Porphyromonas gingivalis supernatant induces about 2.5fold increased MMP-9 expression in human oral epidermoid cells
-
12-O-tetradecanoyl phorbol-13-acetate-induced MMP-9 expression is decreased by 324.8% by 0.1 mM silibinin
-
20 mg doxycycline decreases MMP-9 levels after 1 month, 20 mg doxycycline decreases endometrial MMP-9 at 1 and 6 months compared to baseline
-
50 mg/kg (-)-epigallocatechin gallate administration significantly inhibits the induction of the active form of MMP-9
-
a significant increase in MMP-9 is observed in pulmonary tuberculosis patients as compared to healthy controls
-
A3 receptor stimulation induces an increase of MMP-9 protein levels in cellular extracts of U87MG cells by phosphorylation of extracellular signal-regulated protein kinases, c-Jun N-terminal kinase/stress-activated protein kinase, protein kinase B, and activator protein 1. A3 receptor activation stimulates also an increase of extracellular MMP-9 in the supernatants from U87MG glioblastoma cells
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acrolein exposure induces MMP-9 expression at both protein and mRNA levels in the lung tissue
-
activation of phosphatidylinositol 3-kinase is required for tumor necrosis factor-alpha-induced upregulation of matrix metalloproteinase-9. Red wine extrac and quercetin inhibit significantly the tumor necrosis factor-alpha-induced upregulation of MMP-9 whereas resveratrol does not have significant inhibitory effects
-
activation of the nitric oxide-cyclic guanosine 3,5-monophosphate pathway with nitrite or sildenafil, but not with BAY 41-2272, increases MMP-9 levels, lung microembolization is associated with significant increases in pro-MMP-9 levels
-
active treatment with uric acid (0.5 or 1.0 mg) is associated with reduced levels of active MMP-9 at the end of infusion
-
after 24 h incubation, 0.05 mg/ml aspirin inhibits MMP-9 mRNA expression by 50%. MMP-9 mRNA expression and release are inhibited by fenofibrate (0.1 mM) and 15d-prostaglandin J2 (0.005 mM)
-
aqueous extract isolated from Prunella vulgaris suppresses 12-phorbol 13-myristate acetate-enhanced expression of MMP-9 protein, mRNA and transcription activity levels through suppression of nuclear factor-kappaB activation
auto-amplified NFATc1 plays a key role in upregulating MMP-9
berberine inhibits the expression of MMP-9 at both the mRNA and protein levels in a dose-dependent manner (0.005-0.05 mM) by suppressing the activation of p38 pathway in phorbol 12-myristate 13-acetate-induced macrophages
-
Borrelia burgdorferi induces the host protease, matrix metalloproteinase 9, the induction of MMP-9 may allow the organism to disseminate and produce local tissue destruction
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C-reactive protein increases the expression and activity of MMP-9 in a dose-dependent manner in human THP-1 cells
-
circulating MMP-9 concentrations are higher in patients with abdominal aortic aneurysm than those in subjects without abdominal aortic aneurysm
-
elevated plasma levels of MMP-9 are correlated with brain levels within 24 h of acute cerebral ischemia in rats
-
epidermal growth factor contributes to prostate cancer metastasis through stimulating MMP-9 secretion from prostate cancer cells
-
ethanol extracts of Ocimum sanctum suppresses MMP-9 enzymatic activity in Lewis lung carcinoma cells in a dose-dependent manner (0.025-0.2 mg/ml)
-
exposure of KB cells to Porphyromonas gingivalis supernatant (10% v/v) up-regulates the expression of MMP-9 protein and gene, the JNK inhibitor SP600125 (0.02 mM) significantly attenuates MMP-9 gene expression in KB cells in response to Porphyromonas gingivalis supernatant. JNK and AP-1 are the major signaling for Porphyromonas gingivalis supernatant-stimulated MMP-9 expression in KB cells
-
expression of MMP9 protein and mRNA increases in rat brain tissue after cardiopulmonary resuscitation
-
F(ab')2 fragments or stimulation with lipopolysaccharide have no effect on MMP-9 production
-
heregulin-beta1 stimulates MMP-9 secretion and activation via a transcriptional regulation in human breast cancer cells
-
higher plasma MMP-9 concentrations are found in periodontal disease patients compared with healthy controls
-
immune cell secretion of MMP-9 decreases by 58% after 3 months of omega-3 fatty acid supplementation when compared with baseline levels in patients with relapsing-remitting multiple sclerosis
-
in the extract from the small intestine 24 h after indomethacin administration, the MMP-9 activation is significantly attenuated by 10 mg/kg 2-[4-(5-fluoro-3-methylbenzo[b]thiophen-2-yl)sulfonamido-3-methanesulfonylphenyl] thiazole-4-carboxylic acid
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in the human vascular endothelium, simvastatin and atorvastatin (0.0001-0.01 mM) reduce MMP-9 expression and activity
-
in vivo administration of a nuclear factor-kappa B inhibitory peptide blocks the expression of MMP-9 in dystrophic muscle of mdx mice
-
induction of MMP-9 expression and activity is significantly inhibited by 0.001 mM of the specific cPLA2alpha inhibitor
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interleukin 1beta, interleukin-6, and tumor necrosis factor -alpha stimulate MMP-9 expression
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ischemia and reperfusion induce an upregulation of MMP-9 in the ischemic hemispheric microvessels
-
leucine-zipper and sterile-alpha motif kinase reduces MMP-9 activity by increasing TIMP-1/2 expression in H9c2 cardiomyoblast cells
-
levels of MMP-9 in choriodecidua and amnion increases 4 and 8fold, respectively, after simultaneous infection with Escherichia coli added to either the amniotic or the choriodecidual face or to both
-
levonorgestrel subcutaneous implant increases serum MMP-9 levels after 1 month
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low-energy laser irradiation (wavelength of 810 nm with continuous waves at 100 mW output power) facilitates MMP-9 expression in rats 7 days after treatment
-
matrix metalloproteinase-9 is significantly increased after 8 weeks of very low energy diet-induced weight loss
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mild nonischemic cerebral venous hypertension results in increased MMP-9 activity. MMP-9 activity increases 10fold 1 day after surgery, gradually decreases afterwards, and returns to baseline 2 weeks after surgery
-
MMP-9 activity is increased in fibroblasts when the cells are in contact with fibronectin and laminin, while in myoblasts, enhanced activity of the secreted enzyme occurs only in presence of collagen
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MMP-9 activity is significantly increased to 5.0 and 6.1times of the normal intestinal value 12 and 24 h after indomethacin administration, respectively
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MMP-9 expression and activity significantly increase on day 3 after status epilepticus after pilocarpine injection
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MMP-9 expression in the retinal ganglion cell layer significantly increases in the endothelin-1-induced chronic optic nerve ischemia model
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MMP-9 is markedly increased in both the bronchoalveolar lavage fluid and in the lung parenchyma of bleomycin-treated rats, especially in the early phase with the peak on the 4th day
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MMP-9 is moderately induced by Fusobacterium nucleatum and considerably induced by phorbol 12-myristate-13-acetate in gingival epithelial cells, MMP-9 mRNA up-regulation occurs at 3 h, whereas MMP-9 secretion and activity in cell-free supernatants occurs at 12 h
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MMP-9 is significantly increased in the infarcted tissue compared to the contralateral hemisphere after ischemic stroke
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MMP-9 is upregulated during inflammatory bowel disease, MMP-9 activity is highly upregulated in wild type mice treated with dextran sodium sulfate, Salmonella typhimurium, or trinitrobenzene sulfonic acid
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MMP-9 mRNA expression and release is significantly decreased after treatment with 0.0125-0.05 mg/ml aspirin for 24 h. The aspirin-induced down-regulation of MMP-9 mRNA expression and reduction of MMP-9 release are notably alleviated after pretreatment with specific inhibitors of peroxisome proliferator-activated receptor alpha/gamma
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MMP-9 mRNA expression is induced by interleukin 17, at 200 ng/ml the mRNA level increases about 17times compared with the untreated group
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MMP-9 protein activity is decreased in the media samples of cells from large-healthy follicles compared with those from medium-healthy follicles
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MMP-9 protein activity is detected as early as 2 h after the focal ischemic insult (focal cerebral ischemia by photothrombosis), it rapidly increases at 6 h after ischemia, and reaches a maximum level 48 h after the ischemic event. Thereafter, the MMP-9 level abruptly decreases and returns to the baseline at 72 h after the insult
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MMP-9 protein and mRNA levels are decreased up to 43% after treatment with 0.025 mM panduratin A
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MMP-9 secretion is CnA-isoform specific, i.e. the CnAbeta isoform contributes to the CsA-induced upregulation of MMP-9 while the CnAalpha does not
monomeric Abeta(1-42) treatment in human brain endothelial cells (HBMEC) results in a dose-dependent increase in MMP9 levels in the extracellular media
monomeric alpha-synuclein dose-dependently increases MMP-9 activity as well as mRNA level from cultured rat primary astrocytes and microglial cells (about 3fold stimulation at 200 nM). Same concentration of alpha-synuclein aggregates do not induce MMP-9 activity
-
Mycobacterium tuberculosis stimulates matrix metalloproteinases secretion in the host
myricetin, i.e. 3,3',4',5,5',7-hexahydroxyflavone, suppresses UVB-induced MMP-9 expression through the suppression of Raf kinase activity
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N-2-(4-bromophenyl) ethyl caffeamide inhibits MMP-9 production through the nuclear-targeted down-regulation of nuclear factor-kappaB signaling in human monocytic cells
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no significant difference is observed in the levels of MMP-9 in culture filtrate antigen and live Mycobacterium tuberculosis-stimulated as well as unstimulated cultures of both healthy controls and pulmonary tuberculosis patients
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non-surgical periodontal therapy decreases blood plasma MMP-9 concentration by 39%
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norcantharidin downregulates MMP-9 mRNA and protein expression by inhibiting Sp1 transcriptional activity in colorectal cancer cells, norcantharidin at 0.1 mM completely abolishes the expression of MMP-9 mRNA at 48 h
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normobaric hyperoxia inhibits MMP-9-mediated occludin degradation in the ischemic hemispheric microvessels
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nuclear factor-kappaB is a key transcription factor for the production of MMP-9, tumor necrosis factor-alpha induces expression of MMP-9 at both mRNA and protein levels, tumor necrosis factor-alpha-induced expression of MMP-9 is completely blocked by N-2-(4-bromophenyl) ethyl caffeamide in a concentration-dependent (0.001-0.02 mM) manner
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obese individuals show increased activity of MMP-9/LCN2 complex, while a positive correlation between MMP-9 activity and body mass index is observed
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orthodontic pressure induces gene transcription MMP-9 in pressure gingival soft tissue
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overexpression of reversion-inducing cysteine-rich protein with Kazal motifs in HT-1080 cells decreases MMP-9 mRNA levels, reversion-inducing cysteine-rich protein with Kazal motifs-mediated suppression of MMP-9 promoter activity requires 12-O-tetradecanoylphorbol-13-acetate-responsive element and KB sites
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penta-O-galloyl-beta-D-glucose inhibits epidermal growth factor-induced MMP-9 expression in a dose- and time-dependent manner by reducing the MMP-9 transcriptional activity
-
peroxisome proliferators-activated receptor gamma antagonist GW9662 has little effect on MMP-9 expression
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polyclonal immunoglobulins (IVIg) induce expression of MMP-9 in microglia
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propranolol significantly reduces MMP-9 secretion upon treatment with phorbol 12-myristate 13-acetate which is correlated with a decrease in MMP-9 gene expression
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pterostilbene (i.e. trans-3,5-dimethoxy-4'-hydroxystilbene) down-regulates matrix metalloproteinase-9 activity and inhibits protein and mRNA expression of MMP-9 driven by heregulin-beta1
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resveratrol (i.e. trans-3,4',5-trihydroxystilbene) inhibits MMP-9 mRNA and protein expression in a concentration-dependent manner (0.0025-0.01 mM) by up-regulating peroxisome proliferators-activated receptor alpha expression, The effect of resveratrol on MMp-9 can be offset partially by MK886
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serum MMP-9 concentrations are significantly higher in patients with non-herpetic acute limbic encephalitis in acute and convalescent stages than in control patients
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significant increases of MMP9 activity and protein expression are detected in B19-VP1u IgG group, phosphatidylinositol 3-phosphate kinase and phosphorylated extracellular signal-regulated kinase proteins are involved in the induction of MMP9
-
silibinin suppresses 12-O-tetradecanoyl phorbol-13-acetate-induced MMP-9 expression through inhibition of COX-2 (106% decrease of expression at 0.2 mM silibinin), 12-O-tetradecanoyl phorbol-13-acetate-induced MMP-9 expression is inhibited by celecoxib in a dose-dependent fashion, 12-O-tetradecanoyl phorbol-13-acetate-induced MMP-9 expression is decreased by UO126
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Skp2 overexpression increases the expression of MMP-9, Sp1 is involved in the induction of MMP-9 by Skp2
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superparamagnetic iron oxide nanoparticle-mmp9 retention in global cerebral ischemia animals shows that striatal mmp-9 mRNA expression is 2fold greater than that of the control group and the elevation in cortical mmp-9 mRNA is less than 2fold in live brains, global cerebral ischemia in mice induces MMP-9 activity in regions with hyperintense diffusion-weighted imaging
tear MMP-9 activity is significantly higher in patients with dysfunctional tear syndrome, this activity is associated with increased mRNA expression of MMP-9
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the antihemorrhagic effect of PJ34, a potent PARP inhibitor, is associated with a 57% decrease in MMP-9 overexpression, glucocorticoid increases TIMP-1 in the brain endothelial cell line cEND to reduce the levels of MMP-9
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the broad-spectrum matrix metalloproteinase inhibitor doxycycline reduces pulmonary expression of active MMP-9
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the early increase in MMP-9 blood plasma activity in patients with acute coronary syndrome is related to MMPs activation in the unstable atherosclerotic plaque
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the enzyme expression is induced in chick embryonic tibias cultured with lipopolysaccharide
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the ethanolic extract from Kaempferia pandurata significantly decreases MMP-9 expression at both protein and mRNA levels in a dose-dependent manner(0.002-0.01 mg/ml). Treatment of ethanolic Kaempferia pandurata extract at 0.002, 0.005 and 0.01 mg/ml shows decreases in MMP-9 mRNA levels up to 10%, 13%, and 45%, respectively. Kaempferia pandurata interfers Porphyromonas gingivalis supernatant-induced MMP-9 expression in the oral epidermoid cell line ATCC CCL-17
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the expression of MMP-9 in neoplastic and inflammatory cells increases with more advance tumor stage, depth of tumor invasion and presence of lymph node as well as distant metastases
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the expression of MMP-9 is elevated after cerebral ischemia, expression of MMP-9 increases after permanent middle cerebral artery occlusion and transient middle cerebral artery occlusion. interleukin-1beta, tissue necrosis factor-alpha, fibroblast growth facor, and epidermal growth factor can stimulate the secretion of MMP-9
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the gelatinolytic activity of MMP-9 is constitutively activated in Lewis lung carcinoma cells
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the inability of iNOS-deficient mice to generate iNOS-derived nitric oxide profoundly inhibits MMP-9 activity in livers after ischemia/reperfusion injury, exposure of isolated murine neutrophils and macrophages to exogenous nitric oxide increases MMP-9 activity in both cell types, nitric oxide may activate MMP-9 in leukocytes by either autocrine or paracrine mechanisms
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the interleukin-1beta-induced MMP-9 gene expression is mediated through the activation of p42/p44 mitogen-activated protein kinase, p38 mitogen-activated protein kinase, and JNK1/2 in A-549 cells. The interleukin-1beta-induced MMP-9 gene expression is also mediated through the translocation of NF-kappaB (p65) into the nucleus and the degradation of IkappaBalpha
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the intracerebroventricular injection of amyloid beta25-35, amyloid beta1-40, and amyloid beta1-42, but not amyloid beta40-1, transiently increases MMP-9 activity and protein expression in the hippocampus, the expression of MMP-9 is increased in both neurons and glial cells in the hippocampus after amyloid beta treatment
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the level of MMP-9 expression was significantly increased by 4945% and 4412% of the control level following treatment with 20 nM 12-O-tetradecanoyl phorbol-13-acetate in breast cancer cells
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the levels of MMP-9 and reactive oxygen species in the gut of rats with severe acute pancreatitis are significantly higher than those of the rats treated with anti-rat polymorphonuclear neutrophil granulocytes serum or BB-94
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the levels of MMP-9 are increased in the brain and in the peripheral organs after induction of experimental autoimmune encephalomyelitis. After 40 days all the animals recover and do not show signs of experimental autoimmune encephalomyelitis. The absence of MMP-9 in the remission phase suggests a protective role of MMP-9 in the late phase of the disease, because single mmp-9-/- mice present a delayed remission in comparison with wild-type animals suggesting a phase-dependent role of MMP-9 in the disease. MMP-9 levels remain increased in the brains and, to a higher extend, in the spleens of the wild-type mice even during the remission phase, which is in line with the role of MMP-9 as a useful marker and a protective factor for experimental autoimmune encephalomyelitis in the remission phase
the mRNA levels of MMP-9 are significantly higher in diaphragm muscle from 3-, 6- and 8-week-old mdx mice compared with age-matched C57BL/10 control mice
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the mRNA of MMP9 in the granulosa cells is induced by TGFB1 but not follicle-stimulating hormone, luteinizing hormone, progesterone, or estrogen. Luciferase reporter and mutagenesis analysis indicate the AP1 and NFkappaB elements located in the promoter region from -1700 to -2400 bp are critical for both basal and TGFB1-induced MMP9 transcription
the serum MMP-9 level is significantly higher in moyamoya disease than in healthy controls
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there are significant increases in MMP-9 protein expression and enzyme activity 7 h after thermal injury
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there is a highly significant relationship between the expression of MMP-9 and macrophage count in eosinophilic granulomas
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there is no difference in expression of MMP-9 for any follicle size or health status class
-
there is significant reduction in MMP-9 expression on day 7 in all cases, it decreases considerably on day 14 and is almost negligible on day 21 reflecting corneal healing with succinylated collagen bandage lenses
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thrombin stimulation induces MMP-9 secretion of monocytes dose- and time-dependently through activation of extracellular signaling-regulated protein kinase 1/2 and p38. Thrombin up-regulates mRNA and protein levels of MMP-9. NFkappaB activation is necessary for thrombin-induced MMP-9 upregulation in human monocytes. 1,2-bis (aminophenoxy) ethane-N,N,N',N'-tetraacetoxymethyl ester, a Ca2+ chelator, abolishes the thrombin-induced MMP-9 secretion
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total Panax notoginsenosides downregulate expression of MMP-9 apolipoprotein E-knockout mice
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treatment with 0.05 mM glycitein downregulates MMP-9 gene expression and inhibits the phorbol myristate acetate-induced MMP-9 secretion in U87MGcells
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vitamin D3 significantly reduces the MMP-9 level in antigen stimulated and unstimulated cultures of pulmonary tuberculosis as compared to healthy controls
-
aqueous extract isolated from Prunella vulgaris suppresses 12-phorbol 13-myristate acetate-enhanced expression of MMP-9 protein, mRNA and transcription activity levels through suppression of nuclear factor-kappaB activation
-
aqueous extract isolated from Prunella vulgaris suppresses 12-phorbol 13-myristate acetate-enhanced expression of MMP-9 protein, mRNA and transcription activity levels through suppression of nuclear factor-kappaB activation
-
the mRNA of MMP9 in the granulosa cells is induced by TGFB1 but not follicle-stimulating hormone, luteinizing hormone, progesterone, or estrogen. Luciferase reporter and mutagenesis analysis indicate the AP1 and NFkappaB elements located in the promoter region from -1700 to -2400 bp are critical for both basal and TGFB1-induced MMP9 transcription
F1NGT3
the mRNA of MMP9 in the granulosa cells is induced by TGFB1 but not follicle-stimulating hormone, luteinizing hormone, progesterone, or estrogen. Luciferase reporter and mutagenesis analysis indicate the AP1 and NFkappaB elements located in the promoter region from -1700 to -2400 bp are critical for both basal and TGFB1-induced MMP9 transcription
-
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
the effect of pH (in the range of 4.5-9.5) is investigated on the refolding of recombinant human MMP-9 by urea gradient method. Maximum recovery is obtained at pH 7.8 (with NaCl and Tris-HCl buffer)
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
diagnostics
drug development
medicine
diagnostics
-
in patients with clinical signs of meningitis, but without cerebrospinal fluid pleocytosis, enzyme and MMP-8, MMP-13 are highly sensitive markers for intrathecal inflammation
diagnostics
-
circulating concentrations of MMP-9 may be a marker helping in the diagnosis and prognosis of cardiovascular and neoplastic diseases
diagnostics
-
gelatinase B expression as a prognostic factor in patients with stage II/III rectal carcinoma treated by postoperative adjuvant therapy, overview
diagnostics
-
MMP-9 expression is an independent and significant factor for prediction of a poor prognosis in colorectal cancer
diagnostics
matrix metalloproteinase-9 expression in glioma is an independent prognostic factor of patients, which might be a potential diagnostic and therapeutic target of astrocytic glioma
diagnostics
-
serum matrix metallopeptidase 9 (MMP9) is a potential biomarker for the early identification of atherosclerosis in asymptomatic patients with diabetes, and a potential biomarker for assessing arterial plaque
drug development
-
MMP-9 is a therapeutic target in autoimmune diseases, vascular pathologies, and cancer
drug development
-
MMP-9 is an attractive target for therapeutic intervention studies in mouse models
medicine
-
MMP-9 is suggested as a regulator of the angiogenic switch in tumor development
medicine
-
cells resistant to protein kinase C potentiated, transcription factor p53 mediated apoptosis express a higher level of matrix metalloproteinases MMP-9 and MMP-10. Matrix metalloproteinases function confers protection from protein kinase C/p53 induced apoptosis and are implicated in tumor cell resistance
medicine
-
abundant expression of enzyme by synovial tissue mast cells in patients with rheumatoid arthritis but not in normal control
medicine
-
in children with aseptic and bacterial meningitis, both enzyme and collagenase MMP-8 show increased levels in cerebrospinal fluid. In patients with clinical signs of meningitis, but without cerebrospinal fluid pleocytosis, enzyme and MMP-8, MMP-13 are highly sensitive markers for intrathecal inflammation
medicine
-
expression of enzyme is significantly higher in malignant than in nonmalignant prostate tissues. Significant difference in enzymatic activity among normal prostate, benign prostate hyperplasia, localized and metastatic tissue, and serum
medicine
-
enzyme levels are significantly elevated in cerebrospinal fluid of patients with vascular dementia compared to those with Alzheimer disease and to control
medicine
-
proenzyme and enzyme levels are significantly increased in patients with proliferative diabetic retinopathy. Additionally, levels of tissue inhibitor of metalloproteinases-1 are significantly increased and functionally inhibit activation of enzyme in vitreous samples. Enzyme levels in vitreous samples of patients with hemorrhage are significantly higher than those in proliferative diabetic retinopathy patients and strongly correlate with hemoglobin levels
medicine
-
enzyme is present in extracts from leaking bleb tissue of glaucoma patients, but not in bleb leak fluid or aqueous humor samples
medicine
-
ratio of matrx metalloproteinases MMP-9/MMP-2 is enhanced in cancer patients copared with benign diseases and healthy individuals. No correlation between gelatinolytic activity and high tumoral marker values is found
medicine
-
enzyme and leucocyte elastase are essential for granulocyte-mediated proteolysis resulting in dermal-epidermal separation in epidermolysis bullosa acquisita and bullous pemphigoid patients skin. Selective inhibition of enzyme by single-chain variable fragment of a monoclonal antibody results in suppression of blistering
medicine
-
endogenous urokinase plasminogen activator from cultured hepatic stellate cells significantly induces the active forms of enzyme and matrix metalloproteinase MMP-2 in cirrhotic tissue slices. Transfection of hepatic stellate cells with urokinase plasminogen activator gene results in overactivation of enzyme and matrix metalloproteinases MMP-3 and MMP-2
medicine
-
majority of urine samples from patients with bladder cancer show enzyme activity. Enzyme content is enhanced in the urine from patieints with high-grade and advanced-stage bladder tumors. Urinary values of biomarkers tissue polypeptide-specific antigen and protein 22 of nuclear matrix correlate with the increase in enzyme activity in high-grade and advanced-stage bladder tumors
medicine
-
neutrophils of patients with rheumatoid arthritis release considerable amounts of enzyme. Enzyme acts on fragments of collagen type II obtained by cleavage with collagenases MMP-1, MMP-8, or MMP-13. Enzyme produces small remnant peptides with still intact immunodominant epitopes. Lysines in the main immunodominant epitope are modified by partial hydroxylation and partial glycosylation
medicine
-
enzyme, as well as monocyte chemotactic protein-1 and stromal cell-derived factor-1 may have a pathogenic role in the recruitment of leukocytes into the eye in sympathetic ophthalmia
medicine
-
matrix metalloproteinase is an independent predictor of the reduced nitrate-mediated dilatation in the type 1 diabetes mellitus
medicine
-
cervicovaginal MMP-9 correlates with cervical ripening before labor at term, however, cervicovaginal MMP-9 does not change with spontaneous labor or rupture of membranes at term and does not predict success of labor induction
medicine
-
brain levels of matrix metalloproteinase-9 are a marker of neuroinflammation, MMP-9 appears to be upregulated in microvessels within ischemic brain, MMP-9 levels are markedly lower in CD47 knockout brains compared to wild type brains
medicine
-
there is an association of the allele distribution at the TIMP-1 +372 T/C locus, the levels of TIMP-1, -2, and MMP-9 in noninflamed tissue, and smoking habit with diagnostic and/or surgical recurrence of Crohn's disease
medicine
-
matrix metalloproteinase-9 is an independent prognostic marker in laryngeal and hypopharyngeal cancer
medicine
-
a positive correlation between MMP-9 values and gestational age is observed in normal pregnant women
medicine
-
MMP-9 is an inflammatory marker in the tears of patients with ocular surface disease, pro-MMP-9 levels are significantly elevated in blepharitis, in allergic eye disease, in dry eye, and in conjunctivochalasis in comparison to controls
medicine
-
MMP-9 genotype polymorphisms are primary predictors for oral squamous cell carcinoma risk
medicine
-
MMP-9 expression positively correlates with prognosis of oral squamous cell carcinoma
medicine
-
higher levels of MMP-9 mRNA expression in the apical periodontitis when compared to healthy periapical ligaments, suggest that MMP-9 can be directly involved in tissue remodeling/destruction during lesion development
medicine
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the expression of the mRNA of MMP-9 is not significantly elevated with the progression of biliary-associated liver fibrosis
medicine
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the functional polymorphism C1562T in the promoter of matrix metalloproteinase-9 gene is associated with susceptibility to knee osteoarthritis in the Turkish population
medicine
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the reduction of MMP-9 activity may have a possible therapeutic effect for the management of brain injury after focal ischemia
medicine
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pretreatment serum levels of MMP-9 are powerful prognostic markers in patients with oral squamous cell carcinoma, patients with MMP-9 serum levels higher than median have significantly shorter overall survival than those with levels lower than median
medicine
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imbalance between total MMP-9 and TIMP-1 may contribute to the pathogenesis of lupus nephritis
medicine
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MMP-9 overexpression is an early marker of breast carcinogenesis preceding tumor invasion
medicine
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MMP-9 is a potential target for cerebral ischemic treatment in human stroke therapy
medicine
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pharmacological inhibition of MMP-9 activity ameliorates skeletal muscle pathogenesis and enhanced myofiber regeneration in mdx mice. MMP-9 represents as one of the most promising therapeutic targets for the prevention of disease progression in Duchenne muscular dystrophy
medicine
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the serum levels of MMP-9 significantly correlate with the occurrence and severity of acute graft-versus-host disease
medicine
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higher circulating MMP-9 concentrations are associated with abdominal aortic aneurysm presence
medicine
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MMP-9 is a potentially useful biomarker for diagnosing, classifying, and monitoring dysfunctional tear syndrome
medicine
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MMP-9 plasma levels are predictive of cognitive performance following carotid endarterectomy
medicine
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down-regulation of the expression and activity of MMP-9 is a treatment alternative for plaque stabilization by inhibiting the nuclear factor-kappaB activation
medicine
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MMP-9 is a promising target for a neuroprotective approach to preventing seizure-induced hippocampal damage
medicine
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controlling MMP-9 expression has therapeutic potential in Parkinson's disease
medicine
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MMP-9 induces TGF-beta1 production in the airway epithelium through the cleavage of EGF and EGF-like ligands and activating EGFR, suggesting potential targets of therapeutic intervention in airway fibrotic disorders
medicine
matrix metalloproteinase-9 expression in glioma is an independent prognostic factor of patients, which might be a potential diagnostic and therapeutic target of astrocytic glioma
medicine
serum MMP9 levels are significantly associated with hyperlipidaemia
medicine
MMP9 inhibition can facilitate Abeta clearance across the BBB, which could be an effective approach to lowering Abeta levels in the brain and mitigating the AD phenotype, particularly in subjects carrying the apoE4 allele
medicine
MMP9 inhibition can facilitate Abeta clearance across the BBB, which could be an effective approach to lowering Abeta levels in the brain and mitigating the AD phenotype, particularly in subjects carrying the apoE4 allele
medicine
upon infection with Toxocara canis, matrix metalloproteinase MMP-2 and MMP-9 activities remarkably increase, with concomitant granuloma formation
medicine
inhibition of MMP-9 is not recommended for treatment of inflammatory bowel diseases (IBD), overview
medicine
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MMP9 inhibition can facilitate Abeta clearance across the BBB, which could be an effective approach to lowering Abeta levels in the brain and mitigating the AD phenotype, particularly in subjects carrying the apoE4 allele
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Release 2026.1 (March 2026)
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