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(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
-
-
-
-
?
(7-methoxycoumarin-4-yl)-acetyl-Pro-Leu-Gly-Leu-(3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-Ala-Arg-NH2 + H2O
?
-
-
-
-
?
(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
?
-
-
?
2,4-dinitrophenyl-Pro-beta-cyclohexylalanyl-Gly-Cys(Me)-His-Ala-Lys(N-Me-2-aminobenzoyl)-NH2 + H2O
?
-
a quenched fluorogenic substrate
-
-
?
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
-
and peptide substrates derived from, utility of substrate mapping form examining the subsite specificities and the optimization of proteinase substrates
-
?
60 S ribosomal protein L6 + H2O
?
-
-
-
-
?
65000 MW form of vitronectin + H2O
?
-
-
-
-
?
Ac-L-Pro-L-Pro(OH)-Gly-L-Gln-Gly-L-Ala-L-Thr-Gly-L-Glu-L-Pro(OH)-Gly-NH2 + H2O
?
-
-
-
-
?
ADAM 2 + H2O
?
-
putative protein substrate with potential cleavage site
-
?
Aggrecan core protein + H2O
?
-
-
-
-
?
alpha 1(I) collagen + H2O
?
-
-
-
?
alpha 1(V) collagen + H2O
?
-
-
-
?
alpha 1(XI) collagen + H2O
?
-
-
-
?
alpha 2(V) collagen + H2O
?
-
-
-
?
alpha-amylase precursor + H2O
?
-
-
-
-
?
alpha-enolase + H2O
?
-
-
-
-
?
alpha-N-acetylglucosaminidase + H2O
?
-
-
-
-
?
amyloid protein precursor + H2O
?
-
-
-
-
?
amyloid-beta A4 protein precursor + H2O
?
-
-
-
-
?
annexin I + H2O
?
-
-
-
-
?
Arp2/3 complex subunit + H2O
?
-
-
-
-
?
arylsulfatase B precursor + H2O
?
-
-
-
-
?
beta-glucuronidase precursor + H2O
?
-
-
-
-
?
beta-hexosaminidase beta chain precursor + H2O
?
-
-
-
-
?
beta1-integrin + H2O
?
-
-
-
-
?
beta2 integrin subunit CD18 + H2O
?
-
-
-
-
?
betaB1 crystallin + H2O
?
-
main enzyme substrate in lens extract
-
-
?
Cartilage link protein + H2O
?
-
-
-
?
cathepsin E precursor + H2O
?
-
-
-
-
?
CB3 alpha 1(IV) collagen + H2O
?
-
-
-
?
CD25 + H2O
?
-
CD25 is proteolytic cleaved to its soluble form by MMP-9
-
-
?
CD316 antigen + H2O
?
-
-
-
-
?
chondroitin sulfate proteoglycan + H2O
?
-
-
-
-
?
citrate synthase + H2O
?
-
-
-
-
?
collagen I + H2O
?
-
-
-
-
?
collagen type II + H2O
?
-
-
-
-
?
Collagen type III + H2O
?
collagen type VII + H2O
?
-
-
-
-
?
collagen type XI + H2O
?
-
-
-
-
?
dentin sialoprotein + H2O
?
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
-
-
?
desmoglein 3 + H2O
?
-
putative protein substrate with potential cleavage site
-
?
DGRNIYNIHVEDSLECVKGPNVAA + H2O
?
-
-
-
-
?
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
-
-
-
?
ECVKGPNVAAIVGGT + H2O
ECVKGPNVAA + IVGGT
-
-
-
-
?
endoglin + H2O
?
-
putative protein substrate with potential cleavage site
-
?
endothilin receptor + H2O
?
-
putative protein substrate with potential cleavage site
-
?
epidermal growth factor + H2O
?
epididymis-specific alpha-mannosidase precursor + H2O
?
-
-
-
-
?
fibrillar collagen + H2O
?
filamin B + H2O
?
-
-
-
-
?
fragments of human collagen type II + H2O
?
-
fragments obtained by cleavage with collagenases MMP-1, MMP-8, or MMP-13. Enzyme produces small remnant peptides with still intact immunodominant epitopes
-
-
?
galectin 3 + H2O
?
-
-
-
?
gelsolin + H2O
?
-
-
-
-
?
Golgi apparatus protein 1 precursor + H2O
?
-
-
-
-
?
heat shock protein 27 + H2O
?
-
-
-
-
?
heat shock protein 70 + H2O
?
-
-
-
-
?
heat shock protein 90 + H2O
?
-
-
-
-
?
histidyl-tRNA synthetase + H2O
?
-
-
-
-
?
HMGB1 protein + H2O
?
-
-
-
-
?
integrin beta5 + H2O
?
-
putative protein substrate with potential cleavage site
-
?
interleukin-1beta + H2O
?
-
-
-
-
?
islet amyloid polypeptide + H2O
?
kallikrein + H2O
?
-
putative protein substrate with potential cleavage site
-
?
L-Pro-L-Pro(OH)-Gly-L-Gln-Gly-L-Ala-L-Thr-Gly-L-Glu-L-Pro(OH)-Gly-NH2 + H2O
?
-
-
-
-
?
ladinin 1 + H2O
?
-
putative protein substrate with potential cleavage site
-
?
laminin alpha3 chain + H2O
?
-
putative protein substrate with potential cleavage site
-
?
lipase A + H2O
?
-
-
-
-
?
LS276-THP + H2O
?
-
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
-
-
?
Mca-KPLGL-(Dpa)-AR-NH2 + H2O
?
-
-
-
?
myelin basic protein + H2O
?
-
-
-
?
N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl-7-methoxycoumarin-4-yl acetyl + H2O
?
-
-
-
?
N-acetylglucosamine-6-sulfatase precursor + H2O
?
-
-
-
-
?
N-alpha-benzoyl-arginine p-nitroanilide + H2O
N-alpha-benzoyl-Arg + 4-nitroaniline
-
i.e. BAPNA
-
-
?
N-cadherin + H2O
?
-
-
-
-
?
Neonatal human proteoglycan + H2O
?
-
poor substrate, cleavage of the His16-Ile17 bond
-
-
?
nonmuscular actin + H2O
?
-
-
-
?
nucleolin + H2O
?
-
-
-
-
?
occludin + H2O
?
-
-
-
-
?
pancreatic alpha-amylase isozyme + H2O
?
-
-
-
-
?
peptide A13 + H2O
?
-
-
-
?
peptide A13R + H2O
?
-
-
-
?
peptide A3 + H2O
?
-
-
-
?
peptide A34 + H2O
?
-
-
-
?
peptide B74 + H2O
?
-
-
-
?
peptide C15 + H2O
?
-
non-selective peptide substrate
-
?
peptide C9 + H2O
?
-
-
-
?
peptide m1A11 + H2O
?
-
non-selective peptide substrate
-
?
peroxiredoxin 4 + H2O
?
-
-
-
-
?
phosphate regulating neutral endopeptidase + H2O
?
-
putative protein substrate with potential cleavage site
-
?
platelet factor 4 precursor + H2O
?
-
-
-
-
?
pro-urokinase + H2O
active urokinase + prosequence of urokinase
Proteoglycan + H2O
?
-
-
-
-
?
retinoic acid early inducible protein 1 alpha-precursor + H2O
?
-
-
-
-
?
retinoid-inducible serine carboxypeptidase precursor + H2O
?
-
-
-
-
?
SGFGSRYLTA + H2O
?
-
-
-
?
SGKGPRQITA + H2O
?
-
-
-
?
SGKIPRRLTA + H2O
?
-
-
-
?
SGKIPRTATA + H2O
?
-
-
-
?
SGKIPRTLTA + H2O
?
-
-
-
?
SGLKALMITA + H2O
?
-
-
-
-
?
SGLKAMITA + H2O
?
-
-
-
?
SGLPAKSTA + H2O
?
-
-
-
?
SGLRPAKSTA + H2O
?
-
-
-
-
?
SGPLFYSVTA + H2O
?
-
-
-
?
SGPRAVSTTA + H2O
?
-
-
-
?
SGQPHYLTTA + H2O
?
-
-
-
?
snRNP D3 + H2O
?
-
-
-
-
?
stathmin + H2O
?
-
-
-
-
?
stromelysin 1 + H2O
?
-
-
?
stromelysin1 + H2O
?
-
-
-
?
succinylated gelatin + H2O
?
-
-
-
-
?
tissue factor pathway inhibitor + H2O
?
-
-
-
?
transforming growth factor-beta + H2O
?
-
MMP9 mediates activation of latent transforming growth factor-beta
-
-
?
tubulin + H2O
?
-
-
-
-
?
Type IV collagen + H2O
?
-
-
-
-
?
type V collagen + H2O
?
-
-
-
-
?
type XI collagen + H2O
?
-
-
-
-
?
vascular endothelial-cadherin + H2O
?
-
-
-
?
Vitronectin + H2O
?
-
65000 MW and 75000 MW form of vitronectin
-
-
?
vitronectin of MW 65000 + H2O
?
-
-
-
-
?
vitronectin of MW 75000 + H2O
?
-
-
-
-
?
additional information
?
-
(7-methoxycoumarin-4-yl)acetyl-Pro-Leu-Gly-Leu-beta-(2,4-dinitrophenylamino)Ala-Ala-Arg-NH2 + H2O
?
-
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Pro-Leu-Gly-Leu-beta-(2,4-dinitrophenylamino)Ala-Ala-Arg-NH2 + H2O
?
-
-
-
-
?
Collagen + H2O
?
-
-
-
-
?
Collagen + H2O
?
-
type IV
-
-
?
Collagen + H2O
?
-
type I, not native
-
-
?
Collagen + H2O
?
-
type I (denatured)
-
-
?
Collagen + H2O
?
-
type IV (native)
-
-
?
Collagen + H2O
?
-
cleavage of the carboxyl-terminal triple helix-containing region
-
-
?
Collagen + H2O
?
-
type I, binding, no cleavage
-
-
?
Collagen + H2O
?
-
type V (native)
-
-
?
Collagen + H2O
?
-
type XIV
-
-
?
Collagen + H2O
?
-
MMP-9 inhibits collagen-induced platelet aggregation
-
-
?
Collagen + H2O
?
-
-
-
-
?
Collagen + H2O
?
-
type V
-
-
?
Collagen + H2O
?
-
cleaves between residues Gly439-Val in both alpha1(V) and alpha(XI) and between residues Gly445-Leu in the alpha2(V) chain
-
-
?
Collagen + H2O
?
-
-
-
-
?
Collagen type I + H2O
?
-
-
-
-
?
Collagen type I + H2O
?
-
soluble, native collagen type I, zymography
-
-
?
Collagen type I + H2O
?
-
-
-
-
?
Collagen type III + H2O
?
-
-
-
-
?
Collagen type III + H2O
?
-
MMP-9 cleaves native, triple helical type III collagen to generate a 3/4 fragment, zymography
-
-
?
collagen type IV + H2O
?
-
-
-
-
?
collagen type IV + H2O
?
-
collagen zymography
-
-
?
collagen type IV + H2O
?
-
-
-
-
?
collagen type V + H2O
?
-
-
-
-
?
collagen type V + H2O
?
-
-
-
-
?
Elastin + H2O
?
-
-
-
-
?
Elastin + H2O
?
-
-
-
-
?
Elastin + H2O
?
-
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
-
-
?
epidermal growth factor + H2O
?
-
-
-
-
?
epidermal growth factor + H2O
?
-
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
-
-
?
fibrillar collagen + H2O
?
-
degradation
-
-
?
fibrillar collagen + H2O
?
-
degradation, MMP-9 is involved in development of osteoarthritis, overview
-
-
?
fibrillar collagen + H2O
?
-
degradation, cleavage within the triple helix
-
-
?
Fibronectin + H2O
?
-
-
-
-
?
Fibronectin + H2O
?
-
-
-
-
?
Galectin-3 + H2O
?
-
-
-
-
?
Galectin-3 + H2O
?
-
a galactoside-binding protein, major cleavage site is the Ala62-Tyr63 bond
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
gelatin zymography, mass spectrometrical analysis, overview
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
Gallus gallus Hy-Line Brown
-
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
-
683170, 683233, 683579, 683710, 683749, 683844, 683881, 684107, 695947, 696980, 697383, 699222, 699345, 699642, 699656, 699946, 700530, 702513, 707123, 707366, 707452, 707631, 707654, 707953, 707964, 707978, 708020, 708070, 708086, 708088, 708089, 708171, 708245, 708409, 708548, 708773, 708775, 708810, 708828, 709051, 709277, 709288, 709301, 709302, 709413, 709700, 709811, 710077, 710174, 710225, 710245, 710452, 710531, 710587, 717898, 717980, 718385 -
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
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
-
-
?
Gelatin + H2O
?
-
gelatin zymography
-
-
?
Gelatin + H2O
?
gelatin zymography
-
-
?
Gelatin + H2O
?
-
gelatin zymography using gelatin and fluorescence-conjugated gelatin peptides
-
-
?
Gelatin + H2O
?
-
gelatin zymography, from porcine skin
-
-
?
Gelatin + H2O
?
-
-
683055, 683111, 683480, 683555, 683733, 683816, 696037, 696751, 699477, 707062, 707298, 707302, 707451, 707928, 708024, 708188, 708547, 708548, 708690, 708695, 708703, 708740, 708746, 709178, 709239, 709249, 709382, 709650, 709680, 709734, 709787, 709791, 709904, 710065, 710067, 710102, 717577, 718355 -
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
gelatin zymography
-
-
?
Gelatin + H2O
?
-
gelatin zymography, gelatin from porcine skin
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
gelatin zymography, gelatin from porcine skin
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
gelatin zymography
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
gelatin zymography
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
-
683051, 683412, 683427, 683874, 700147, 701422, 708304, 709595, 709614, 709646, 709682, 709920, 709948, 710106, 710575, 710585, 710695 -
-
?
Gelatin + H2O
?
-
gelatin zymography
-
-
?
Gelatin + H2O
?
-
zymographic analysis
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
-
-
-
?
islet amyloid polypeptide + H2O
?
enzyme MMP-9 degrades amyloidogenic humanislet amyloid polypeptide but not nonamyloidogenic mouse islet amyloid polypeptide
-
-
?
islet amyloid polypeptide + H2O
?
enzyme MMP-9 degrades amyloidogenic human islet amyloid polypeptide but not nonamyloidogenic mouse islet amyloid polypeptide
-
-
?
islet amyloid polypeptide + H2O
?
enzyme MMP-9 degrades amyloidogenic human islet amyloid polypeptide but not nonamyloidogenic mouse islet amyloid polypeptide
-
-
?
Laminin + H2O
?
-
degradation
-
-
?
Laminin + H2O
?
-
degradation
-
-
?
Laminin + H2O
?
-
-
-
-
?
Laminin + H2O
?
-
-
-
-
?
Laminin + H2O
?
-
-
-
-
?
pro-urokinase + H2O
active urokinase + prosequence of urokinase
-
-
-
-
?
pro-urokinase + H2O
active urokinase + prosequence of urokinase
-
-
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
specificity overview
-
-
?
additional information
?
-
-
prefers hydrophobic aliphatic residues in subsite P1'
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
tolerates only small amino acids such as Gly and Ala in P1
-
-
?
additional information
?
-
-
may be responsible for the pathological degradation and/or normal turnover of vitronectin
-
-
?
additional information
?
-
-
possible role of the enzyme in the structural tissue remodeling of the developing embryo
-
-
?
additional information
?
-
-
plays a role in tumor cell invasion and in destruction of cartilage in arthritis
-
-
?
additional information
?
-
-
enzyme may play a role in the destruction of the extracellular matrix, perhaps acting in concert with the metalloproteases produced by activated endothelial cells
-
-
?
additional information
?
-
associated with degradation of the extracellular matrix in normal and pathological conditions
-
?
additional information
?
-
-
central role in the degradation of the extracellular matrix
-
?
additional information
?
-
-
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
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
collagen binding domains of matrix metalloproteinases MMP-2 and MMP-9 bind the same or closely positioned sites on type I collagen
-
-
?
additional information
?
-
-
enzyme and leucocyte elastase are essential for granulocyte-mediated proteolysis resulting in dermal-epidermal separation in epidermolysis bullosa acquisita and bullous pemphigoid patients skin
-
-
?
additional information
?
-
-
no substrate: L-Pro-L-Pro(OH)-Gly-L-Gln-Gly-L-Ala(CH3)-L-Thr-Gly-L-Glu-L-Pro(OH)-Gly-CONH2
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
gelatinase B expression is a prognostic factor in patients with stage II/III rectal carcinoma treated by postoperative adjuvant therapy, overview
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
MMP-9 expression is increased in cancers, inhibition of MMP-9 has a therapeutic benefit to cancer
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
MMP-9 is involved in development of endometriosis, MMP-9 levels are decreased by about 50% after operation of endometriosis, overview
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
the enzyme cleaves many substrates
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
enzyme activity is determined using human teeth as substrate
-
-
?
additional information
?
-
-
peptide A16 SGRR LLSRTA and peptide C11 SGRR LIHHTA are no substrates
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
gastric gelatinase B is rapidly increased in Helicobacter felis-infected mice and is involved in induction of gastritis
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
MMP-9 inhibitor completely inhibits PAF-induced B16F10 metastasis
-
-
?
additional information
?
-
-
MMP-9 is essential for neutrophil infiltration during zymosan peritonitis
-
-
?
additional information
?
-
-
MMP-9 is involved in murine peritonitis by participating in cellular migration, molecular mechanism, overview
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
MMP-9 is involved in murine peritonitis by participating in cellular migration, molecular mechanism, overview
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
gastric gelatinase B is rapidly increased in Helicobacter felis-infected mice and is involved in induction of gastritis
-
-
?
additional information
?
-
-
MMP-9 is essential for neutrophil infiltration during zymosan peritonitis
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
enzyme may be necessary for initiating or completing degradation of type I/type V copolymeric fibrils for growth and remodeling of extracellular collagen
-
-
?
additional information
?
-
-
independent of its proteolytic function, enzyme has a biphasic effect on smooth muscle cell-mediated collagen gel contraction
-
-
?
additional information
?
-
-
astrocyte-released MMP-9 is involved in interleukin-1beta induced neurotoxicity, probably via urokinase plasminogen activator, overview
-
-
?
additional information
?
-
-
inhibition of MMP-9 prevents neutrophilic inflammation in ventilator-induced lung injury, VILI, and pulmonary hemorrhage, overview
-
-
?
additional information
?
-
-
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Aggrecan core protein + H2O
?
-
-
-
-
?
chondroitin sulfate proteoglycan + H2O
?
-
-
-
-
?
collagen I + H2O
?
-
-
-
-
?
Collagen type I + H2O
?
-
-
-
-
?
Collagen type III + H2O
?
-
-
-
-
?
collagen type XI + H2O
?
-
-
-
-
?
dentin sialoprotein + H2O
?
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
-
-
?
epidermal growth factor + H2O
?
-
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
-
-
?
fibrillar collagen + H2O
?
islet amyloid polypeptide + H2O
?
pro-urokinase + H2O
active urokinase + prosequence of urokinase
transforming growth factor-beta + H2O
?
-
MMP9 mediates activation of latent transforming growth factor-beta
-
-
?
additional information
?
-
Collagen + H2O
?
-
MMP-9 inhibits collagen-induced platelet aggregation
-
-
?
Collagen + H2O
?
-
-
-
-
?
collagen type IV + H2O
?
-
-
-
-
?
collagen type IV + H2O
?
-
-
-
-
?
collagen type V + H2O
?
-
-
-
-
?
collagen type V + H2O
?
-
-
-
-
?
Elastin + H2O
?
-
-
-
-
?
Elastin + H2O
?
-
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
-
-
?
fibrillar collagen + H2O
?
-
degradation
-
-
?
fibrillar collagen + H2O
?
-
degradation, MMP-9 is involved in development of osteoarthritis, overview
-
-
?
Fibronectin + H2O
?
-
-
-
-
?
Fibronectin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
Gallus gallus Hy-Line Brown
-
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
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
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
-
-
-
?
islet amyloid polypeptide + H2O
?
enzyme MMP-9 degrades amyloidogenic humanislet amyloid polypeptide but not nonamyloidogenic mouse islet amyloid polypeptide
-
-
?
islet amyloid polypeptide + H2O
?
enzyme MMP-9 degrades amyloidogenic human islet amyloid polypeptide but not nonamyloidogenic mouse islet amyloid polypeptide
-
-
?
islet amyloid polypeptide + H2O
?
enzyme MMP-9 degrades amyloidogenic human islet amyloid polypeptide but not nonamyloidogenic mouse islet amyloid polypeptide
-
-
?
Laminin + H2O
?
-
degradation
-
-
?
Laminin + H2O
?
-
degradation
-
-
?
Laminin + H2O
?
-
-
-
-
?
Laminin + H2O
?
-
-
-
-
?
Laminin + H2O
?
-
-
-
-
?
pro-urokinase + H2O
active urokinase + prosequence of urokinase
-
-
-
-
?
pro-urokinase + H2O
active urokinase + prosequence of urokinase
-
-
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
may be responsible for the pathological degradation and/or normal turnover of vitronectin
-
-
?
additional information
?
-
-
possible role of the enzyme in the structural tissue remodeling of the developing embryo
-
-
?
additional information
?
-
-
plays a role in tumor cell invasion and in destruction of cartilage in arthritis
-
-
?
additional information
?
-
-
enzyme may play a role in the destruction of the extracellular matrix, perhaps acting in concert with the metalloproteases produced by activated endothelial cells
-
-
?
additional information
?
-
associated with degradation of the extracellular matrix in normal and pathological conditions
-
?
additional information
?
-
-
central role in the degradation of the extracellular matrix
-
?
additional information
?
-
-
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
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
collagen binding domains of matrix metalloproteinases MMP-2 and MMP-9 bind the same or closely positioned sites on type I collagen
-
-
?
additional information
?
-
-
enzyme and leucocyte elastase are essential for granulocyte-mediated proteolysis resulting in dermal-epidermal separation in epidermolysis bullosa acquisita and bullous pemphigoid patients skin
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
gelatinase B expression is a prognostic factor in patients with stage II/III rectal carcinoma treated by postoperative adjuvant therapy, overview
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
MMP-9 expression is increased in cancers, inhibition of MMP-9 has a therapeutic benefit to cancer
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
MMP-9 is involved in development of endometriosis, MMP-9 levels are decreased by about 50% after operation of endometriosis, overview
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
the enzyme cleaves many substrates
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
gastric gelatinase B is rapidly increased in Helicobacter felis-infected mice and is involved in induction of gastritis
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
MMP-9 inhibitor completely inhibits PAF-induced B16F10 metastasis
-
-
?
additional information
?
-
-
MMP-9 is essential for neutrophil infiltration during zymosan peritonitis
-
-
?
additional information
?
-
-
MMP-9 is involved in murine peritonitis by participating in cellular migration, molecular mechanism, overview
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
MMP-9 is involved in murine peritonitis by participating in cellular migration, molecular mechanism, overview
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
gastric gelatinase B is rapidly increased in Helicobacter felis-infected mice and is involved in induction of gastritis
-
-
?
additional information
?
-
-
MMP-9 is essential for neutrophil infiltration during zymosan peritonitis
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
enzyme may be necessary for initiating or completing degradation of type I/type V copolymeric fibrils for growth and remodeling of extracellular collagen
-
-
?
additional information
?
-
-
independent of its proteolytic function, enzyme has a biphasic effect on smooth muscle cell-mediated collagen gel contraction
-
-
?
additional information
?
-
-
astrocyte-released MMP-9 is involved in interleukin-1beta induced neurotoxicity, probably via urokinase plasminogen activator, overview
-
-
?
additional information
?
-
-
inhibition of MMP-9 prevents neutrophilic inflammation in ventilator-induced lung injury, VILI, and pulmonary hemorrhage, overview
-
-
?
additional information
?
-
-
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(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-isopropionyl-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)-2,4-bis[(2,3-dihydroxybenzoyl)amino]butyric acid methyl ester
-
-
(S)-2,5-bis[(2,3-dihydroxybenzoyl)amino]pentanoic acid methyl ester
-
-
(S)-2,6-bis[(2,3-dihydroxybenzoyl)amino]-N-hydroxyhexanoamide
-
-
(S)-2,6-bis[(2,3-dihydroxybenzoyl)amino]hexanenitrile
-
-
(S)-2,6-bis[(2,3-dihydroxybenzoyl)amino]hexanoamide
-
shows 33% inhibition against MMP-9 at 0.00025 mM
(S)-2,6-bis[(2,3-dihydroxybenzoyl)amino]hexanoic acid
-
-
(S)-2,6-bis[(2,3-dihydroxybenzoyl)amino]hexanoic acid methyl ester
-
-
(S)-2,6-bis[(2,3-dimethoxybenzoyl)amino]hexanoic acid methyl ester
-
-
(S)-2,7-bis[(2,3-dihydroxybenzoyl)amino]heptanoic acid methyl ester
-
-
(S)-2-acetyl-6-[(2,3-dihydroxybenzoyl)amino]hexanoic acid methyl ester
-
-
(S)-2-benzoylamino-6-[(2,3-dihydroxybenzoyl)amino]-hexanoamide
-
-
(S)-2-benzoylamino-6-[(2,3-dihydroxybenzoyl)amino]-hexanoic acid methyl ester
-
-
(S)-6-benzoylamino-2-[(2,3-dihydroxybenzoyl)amino]-hexanoic acid methyl ester
-
-
1,5-bis[(2,3-dihydroxybenzoyl)amino]pentane
-
-
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',5,6,7,8-hexamethoxyflavone
-
i.e. nobiletin
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
3',4'-dihydroxy-5,6,7,8-tetramethoxyflavone
-
-
3'-hydroxy-4',5,6,7,8-pentamethoxyflavone
-
-
4'-hydroxy-3',5,6,7,8-pentamethoxyflavone
-
-
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
-
-
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
-
BIIL284
-
BIIL284 treatment (3 mg/kg once daily for 2 weeks) significantly reduces the extracellular matrix metalloproteinase-9 activity in stented arteries
carboxy-derivatized glucosamine
-
62% inhibition of MMP-9 at 0.5 mg/ml
-
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
cyclic CTT peptide
-
a gelatinase inhibitor peptide
cyclic CTTHWGFTLC
-
a specific gelatinase inhibitor
D-penicillamine
-
10 mg/l, 43% inhibition
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
-
Immunoglobulins purified from antisera raised against gelatinase
-
-
-
isovitexin
interacts with enzyme residues Glu241, Ala242, Pro255, Pro254, Thr251, Leu222, Tyr248, Arg241, Met247, His226, and Glu227, binding structure analysis, and modeling, overview
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
minocycline
-
0.02 mM minocycline displays inhibitory action on MMP-9 expression and activity
MMP-9i
-
MMP-9 inhibitor, an anthranilate hydroxamic acid derivative
-
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-isobutyl-N-(4-methoxyphenylsulfonyl)glycyl hydroxamic acid
NNGH
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
polyhistidine
-
0.001 mM, 68% inhibition
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
-
reversion-inducing cysteine-rich protein with Kazal motifs
-
-
TIMP1
-
interaction analysis and structure modeling, overview
-
TIMP2
-
interaction analysis and structure modeling, overview
-
tissue inhibitor of matrix metalloproteinase 1
-
strong inhibitor of MMP-9
-
tissue inhibitor of matrix metalloproteinase-1
-
TIMP-1
-
tissue inhibitor of metalloproteinase 1
-
-
-
tissue inhibitor of metalloproteinase TIMP-1
-
-
tissue inhibitor of metalloproteinase TIMP-2
-
-
Tissue inhibitor of metalloproteinase-1
-
Tissue inhibitor of metalloproteinase-2
-
-
tissue inhibitor of metalloproteinases 1
-
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
-
vitexin
interacts with enzyme residues Gly186, Pro246, His236, Met247, Tyr248, Val223, and Leu188, binding structure analysis, and modeling, overview
1,10-phenanthroline
-
strong inhibition at 1 mM
1,10-phenanthroline
-
10 mM, 100% inhibition
1,10-phenanthroline
-
totally inhibited by 10 mM 1,10-phenanthroline
BB-94
-
broad-spectrum MMP inhibitor
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
doxycycline
-
totally inhibited by 10 mM doyxycline
EDTA
-
complete inhibition at 10 mM
EDTA
-
10 mM, 74% inhibition
EDTA
2 mM, severely inhibits enzyme activity due to chelation of metal ions
EDTA
-
complete inhibition at 10 mM
GM6001
-
GM6001
-
MMP-9-specific inhibitor
GM6001
-
MMP inhibitor, complete inhibition at 0.025 mM
ilomastat
-
-
ilomastat
-
a pan-MMP inhibitor, strong inhibition
MMP-9 inhibitor I
-
MMP-9 inhibitor I
-
highly specific inhibition of MMP-9
SB-3CT
-
MMP-9-specific inhibitor
SB-3CT
-
MMP9-specific inhibitor, MMP9 activity is reduced with SB-3CT resulting in reduced brain injury
TIMP-1
-
-
-
TIMP-1
-
formation of proMMP-9/TIMP-1 complexes
-
TIMP-1
-
major inhibitor of MMP-9
-
TIMP-1
-
i.e. tissue inhibitor of metalloproteinase 1, a natural inhibitor
-
TIMP-2
-
-
-
TIMP-2
-
specific inhibitor for MMP9
-
TIMP-2
-
a MMP inhibitor
-
Tissue inhibitor
-
of metalloproteinase-2
-
Tissue inhibitor
-
of metalloproteinase-1; of metalloproteinase-2
-
Tissue inhibitor
-
of metalloproteinases, recombinant
-
Tissue inhibitor of metalloproteinase-1
-
-
-
Tissue inhibitor of metalloproteinase-1
-
1 nM, 88% inhibition
-
Tissue inhibitor of metalloproteinase-1
-
-
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 metalloproteinase-1
-
-
-
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
-
tissue inhibitor of metalloproteinases 1
TIMP-1
-
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
-
inhibitor synthesis and molecular docking, overview
-
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
-
Notch1 knockdown decreases MMP9 expression
-
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
-
epitope tagging of MMP-9 with monoclonal antibodies, overview
-
additional information
-
both NF-jB and AP-1 inhibitors inhibit MMP-9 expression
-
additional information
-
NK4 intervention suppresses MMP9 mRNA 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
-
borneol has no influence on MMP-9 activity
-
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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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
4-aminophenylmercuric acetate
acrolein
-
activates MMP-9 via EGFR/MAPK signaling and stimulation of pro-MMP-9 cleavage
aminophenylmercuric acetate
-
-
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 3
-
converts inactive pro-MMP-9 to active MMP-9
-
matrix metalloproteinase-7
MMP-9 is activated by matrix metalloproteinase-7
-
phorbol 12-myristate 13-acetate
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
tumor necrosis factor-alpha
-
4-aminophenylmercuric acetate
-
-
4-aminophenylmercuric acetate
-
proteolytically activates the enzyme
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
-
artificial activation of the inactive zymogen
4-aminophenylmercuric acetate
-
1 mM
4-aminophenylmercuric acetate
-
activation of pro-MMP-9 constructs at pH 7.0
4-aminophenylmercuric acetate
-
1 mM 4-aminophenylmercuric acetate-mediated activation of MMP-9 provokes autocatalytic cleavage of recombinant MMP-9
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
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
tumor necrosis factor-alpha
-
-
-
tumor necrosis factor-alpha
-
-
-
additional information
-
binding of the zymogen to fetuin or asialofetuin results in activation
-
additional information
-
activation by trypsin, MMP3, and MMP10, computational model of MMP9 activation and inhibition, overview
-
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
-
relaxin induces enzyme expression in THP-1 cells, while it reduces expression of NF-kappaB inhibitor protein, IkappaB-alpha, overview
-
additional information
-
0.001-0.04 mM arachidonic acid increases matrix metalloproteinase 9 secretion and expression at the mRNA level
-
additional information
-
activator protein-4 expression may play an important role in the induction of synthesis of MMP-9
-
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
-
dermal fibroblasts and hepatic stellate cells require type-I collagen which boosts Jun N-terminal kinase activity to maximally induce MMP-9
-
additional information
-
eicosapentaenoic acid, docosapentaenoic acid or docosahexaenoic acid by themselves have no effect on MMP-9 secretion
-
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
-
MMP-9 expression is increased after a 16 h acetaldehyde treatment (0.1 mM)
-
additional information
-
MMP-9 is activated by a whole-cell extract from Prevotella nigrescens ATCC 33563
-
additional information
-
Notch1 may be involved in MMP9 activation either by enhancing its expression or by stabilizing the protein
-
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
-
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
-
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
-
8-bromo-cGMP yields increases in active MMP-9
-
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
-
implantation of 9L glioma cells into brain increases the expression of MMP-9, overview
-
additional information
-
interleukin-1beta induces MMP-9 activity
-
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
-
benzo[a]pyrene increases the mRNA level of matrix metalloproteinase 9
-
additional information
-
high glucose (25 mM) induces expression of MMP-9
-
additional information
-
tissue kallikrein is a potent activator of latent proenzyme
-
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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
-
-
0.017 - 0.0209
3',4',5,6,7,8-hexamethoxyflavone
0.0108 - 0.0123
3',4'-dihydroxy-5,6,7,8-tetramethoxyflavone
0.0164 - 0.0169
3'-hydroxy-4',5,6,7,8-pentamethoxyflavone
0.0037 - 0.0055
4'-hydroxy-3',5,6,7,8-pentamethoxyflavone
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
0.000006
CGS 27023A
Mus musculus
-
-
0.0000002 - 0.0000005
ilomastat
additional information
additional information
Homo sapiens
-
-
-
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
0.0000002
ilomastat
Homo sapiens
-
pH 7.4, 37°C
0.0000005
ilomastat
Homo sapiens
-
-
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-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
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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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MMP-9 secretion
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in the walls
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bone marrow-derived cells are the major source of MMP-9 in the ischemic brain
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glial-neuronal coculture
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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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primary
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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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colon adenocarcinoma cell line
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MMP-9 is expressed at very low levels in endometrioid adenocarcinoma cells
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increased MMP-9 levels
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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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airway
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tumor periphery
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high expression level of MMP-9 increasing during growth
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neutrophil, commercial preparation
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colon adenocarcinoma cell line
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leukemia cell line, secretion of MMP-9
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from ileus
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fibroblast
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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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from surgical lobectomy for lung cancer
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cell expression system
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atrophic acnd nonatrophic oral lichen planus
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periapical ligament
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immunohistochemic analysis
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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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of larynx
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stromal cells are the major source of MMP-9
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colon adenocarcinoma cell line
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MMP9 is expressed in teeth from early embryonic to adult stage
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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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secretion, induced by interleukin-1beta
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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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primary breast tumor cell
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primary cell
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laryngeal in situ carcinoma
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embryonic
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from femoral condyles in the knee
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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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primary tumors
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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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purified from neutrophil granulocytes
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recombinant pro-MMP-9
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contitioned culture medium
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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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contitioned culture medium
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of rabbit synovial cell line HIG-82
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in the lumen of the cranial and cervical neural tubes
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in the lumen of the cranial and cervical neural tubes
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bleb tissue and fluid of glaucoma patients
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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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induced by ethanol
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induced by ethanol
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the enzyme is upregulated compared to control brain
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enzyme activity and expression analysis, overview
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a fibrosarcoma cell line
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tumour cells developed in mice, high expression level
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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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cirrhotic liver
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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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polymorphonuclear lymphocytes
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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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polymorphonuclear macrophages
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macrophages derived from THP-1 cells
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activated, MMP-9 secretion
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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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located within the granulation tissue
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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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activated, MMP-9 secretion
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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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secretion of MMP-9
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secretion of MMP-9
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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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polymorphonuclear neutrophils
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MMP-9 secretion
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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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MMP-9 secretion
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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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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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secretion of MMP-9
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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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primary bronchial epithelial cell
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668514, 668996, 670741, 684107, 697548, 701178, 708232, 708245, 708784, 708814, 709619, 709819, 710177, 710452, 710542, 710584 brenda
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gastric mucosa
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gastric mucosa
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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
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
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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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
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
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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 expression analysis in peritonitis, 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 levels are increased in acute pancreatitis
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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 expression analysis in peritonitis, overview
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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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additional information
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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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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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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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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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matrix metalloprotease-9 inhibition improves amyloid beta-mediated cognitive impairment and neurotoxicity in mice
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
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 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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MMP-9 knockdown blocks SGC-7901 cells' invasion, migration and proliferation
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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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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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
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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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inhibition of MMP activity, especially MMP-9, has the potential to inhibit tumor growth and metastasis
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
malfunction
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
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
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
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
malfunction
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
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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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malfunction
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enzyme inhibition prevents neural crest cells delamination and migration
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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
-
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
-
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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metabolism
-
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
-
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
-
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
-
activated MMP-9 degrades components of the neurovascular unit, mediates blood-brain barrier leakage, and facilitates brain edema and hemorrhage
physiological function
-
changes in MMP-9 activity may be essential to the tissue reorganization necessary for ovulation in the equine ovary
physiological function
-
epithelial-derived MMP-9 is an important mediator of tissue injury in colitis
physiological function
expression of MMP-9 mRNA is associated with abnormal apparent diffusion coefficient after global cerebral ischemia
physiological function
-
lipocalin-2 is associated with MMP-9 activity
physiological function
-
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
-
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
-
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
-
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
-
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
-
MMP-9 is a key enzyme in neutrophil biology
physiological function
-
MMP-9 is essential for ischemia-induced neovascularization by modulating bone marrow-derived endothelial progenitor cells
physiological function
-
MMP-9 is essential for osteoclastogenesis
physiological function
-
MMP-9 is involved in both bacterial translocation and polymorphonuclear neutrophil granulocytes transmigration in rat severe acute pancreatitis
physiological function
-
MMP-9 is involved in cardiomyocytes contractility dysfunction, MMP-9 treatment attenuates the voltage-induced contraction of primary cardiomyocytes
physiological function
-
MMP-9 is required for tissue remodeling in response to natural hydroxyapatite
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
-
MMP-9 plays a causal role in amyloid beta-induced cognitive impairment and neurotoxicity
physiological function
-
MMP-9 plays a causative role in blood-brain barrier disruption after peripheral thermal injury
physiological function
-
MMP-9 plays a pivotal role in vascular remodeling and development of atherosclerotic lesion
physiological function
-
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
-
MMP-9 plays an important role in the pathogenesis of acute graft-versus-host disease
physiological function
-
MMP-9 plays an important role in wound healing, angiogenesis, inflammation, tumor invasion, and metastasis
physiological function
-
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- mediated occludin degradation represents an important mechanism for blood brain barrier disruption in ischemic stroke
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
-
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
-
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
-
the recruitment of mesoangioblasts requires the secretion of MMP-9 by M2 cells
physiological function
-
MMP-9 has a role as essential mediator in degradation/damage of the extracellular matrix of fetal membranes
physiological function
-
MMP-9 is involved in the mechanism of cell-to-cell HIV-1 endocytosis in dendritic cells
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 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
-
MMPs can promote cancer cell invasion by degradation of various extracellular matrix components resulting in release of growth factor and cytokines
physiological function
-
neutrophil-derived matrix metalloproteinase-9 is a potent activator of trypsinogen in acinar cells in acute pancreatitis
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
-
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
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
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 reduces islet amyloid formation by degrading islet amyloid polypeptide, the constituent of amyloid deposits in Alzheimer's disease
-
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
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
-
physiological function
-
neutrophil-derived matrix metalloproteinase-9 is a potent activator of trypsinogen in acinar cells in acute pancreatitis
-
additional information
-
specific inhibition of MMP-9 leads to reduced extents of HIV-1 antigen presentation activity
additional information
-
digestion of the intact enzyme with chondroitinase decreases the size of the molecule to 80 kDa
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
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
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
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
-
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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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
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
200000
-
the molecular weight of proMMP-9 is about 200000 Da, SDS-PAGE
20947
-
x * 70795, calculated, enzyme mutant E402A, x * 20947, calculated, isolated enzyme collagen-binding domain
210000
dimeric form, SDS-PAGE
228300
enzyme multimer/trimer, PAGE, structure analysis by AFM
230000
-
x * 80000, deglycosylated enzyme, SDS-PAGE, x * 230000, glycosylated enzyme, SDS-PAGE
65000 - 82000
major circulating MMP-9 enzyme forms: 92 kDa proMMP-9, and active 82 kDa and 65 kDa enzyme forms
66000
-
active form of MMP-9, SDS-PAGE
67000
-
active form of MMP-9, SDS-PAGE
70795
-
x * 70795, calculated, enzyme mutant E402A, x * 20947, calculated, isolated enzyme collagen-binding domain
72000
-
active form of MMP-9, SDS-PAGE
78000
-
active form of MMP-9, SDS-PAGE
80000
-
x * 80000, deglycosylated enzyme, SDS-PAGE, x * 230000, glycosylated enzyme, SDS-PAGE
85000
-
85000 Da polypeptide in both cellular and secreted parasite extracts, activated form of MMP-9, SDS-PAGE
87000
-
active form of MMP-9
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
95000
-
proMMP-9, SDS-PAGE
96000
-
proMMP-9, SDS-PAGE
130000
-
-
130000
-
x * 92000,enzyme form 1, SDS-PAGE, x * 130000, enzyme form 2, SDS-PAGE, x * 225000, enzyme form 3, SDS-PAGE
225000
-
-
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
-
active enzyme, gelatin zymography
82000
-
activated form of MMP-9, SDS-PAGE
82000
-
x * 92000, full-length pro-MMP-9, SDS-PAGE, x * 82000, processed active MMP-9, SDS-PAGE
82000
-
2 * 82000, 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
-
MMP-9 active 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
84000
-
x * 92000, pro-MMP-9, SDS-PAGE, x * 84000, activated MMP-9, 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-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
86000
-
x * 92000, pro-MMP9, SDS-PAGE, x * 86000, activated MMP-9, SDS-PAGE
88000
-
active form of MMP-9, SDS-PAGE
92000
-
-
92000
-
human SC40-transformed lung cells, gel filtration, glycosylated proenzyme can be activated by organomercurials by removal of 73 amino acids
92000
monomeric form, SDS-PAGE
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
-
MMP-9 proenzyme, SDS-PAGE
92000
-
proenzyme, gelatin zymography
92000
-
activated MMP-9, SDS-PAGE
92000
-
inactive enzyme form
92000
-
inactive form of MMP-9, SDS-PAGE
92000
-
inactive pro-MMP-9, SDS-PAGE
92000
-
pro-form of MMP-9, SDS-PAGE
92000
-
pro-MMP-9, SDS-PAGE
92000
-
2 * 92000, pro-MMP-9, SDS-PAGE
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
92000
-
x * 92000, pro-MMP-9, SDS-PAGE, x * 84000, activated MMP-9, SDS-PAGE
92000
-
x * 92000, pro-MMP-9, SDS-PAGE, x * 86000, activated 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
-
x * 92000, pro-MMP9, SDS-PAGE, x * 86000, activated MMP-9, SDS-PAGE
92000
-
2 * 92000, proMMP-9, SDS-PAGE
92000
-
1 * 92000, pro-enzyme, SDS-PAGE, 1 * 82000, recombinant truncated mutant MMP-9, SDS-PAGE
94000
-
-
94000
-
pro-MMP9, SDS-PAGE
97000
-
SDS-PAGE
97000
-
active enzyme form, gelatin gel zymography
97000
-
active form of MMP-9, SDS-PAGE
97000
-
97000 Da protein band in cellular extract, SDS-PAGE
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?
-
x * 92000, pro-MMP-9, SDS-PAGE, x * 84000, activated MMP-9, SDS-PAGE
?
-
x * 80000, deglycosylated enzyme, SDS-PAGE, x * 230000, glycosylated enzyme, SDS-PAGE
?
x * 82000, mature active 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, pro-MMP-9, SDS-PAGE, x * 86000, activated MMP-9, SDS-PAGE
?
-
x * 92000, pro-MMP9, SDS-PAGE, x * 86000, activated 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 * 65000, active matured, truncated enzyme form lacking both the N- and C-terminal domains, SDS-PAGE, x * 82000, activated mature enzyme, 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 * 103000, about, pro-MMP9, SDS-PAGE, x * 86000, about, activated MMP-9, SDS-PAGE
?
-
x * 92000, pro-MMP-9, SDS-PAGE
?
-
x * 92000, pro-MMP-9, SDS-PAGE, x * 86000, activated MMP-9, SDS-PAGE
?
-
x * 92000, pro-MMP9, SDS-PAGE, x * 86000, activated MMP-9, SDS-PAGE
dimer
-
dimer
-
2 * 92000, pro-MMP-9, SDS-PAGE
dimer
-
dimers of MMP-9 are detected under physiological conditions
dimer
-
2 * 60000-65000, extracellular proteolytically active disulfide-linked MMP-9 dimers, SDS-PAGE
homodimer
-
2 * 82000, active MMP-9, SDS-PAGE
homodimer
-
2 * 92000, proMMP-9, SDS-PAGE
monomer
-
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
epitope mapping, structure modeling, overview
additional information
-
epitope mapping, structure modeling, overview
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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E412D
-
site-directed mutagenesis
P574R
-
the mutant is associated with a non-significant decreased risk of coronary artery disease when compared with the wild type genotype
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
-
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
-
the mutant is associated with a non-significant decreased risk of coronary artery disease when compared with the wild type genotype
R279Q
-
there is no relationship between R279Q polymorphism and atrial fibrillation hypertensive heart disease patients of Chinese Han population
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
-
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
-
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
-
the -1562CNT polymorphism of MMP-9 gene is significantly associated with atrial fibrillation risk in Chinese Han patients with hypertensive heart disease
additional information
-
the functional-1562C/T polymorphism is associated with schizophrenia
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
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
-
enzyme-deficient MPP-9-/- mice show impaired neutrophil infiltration during zymosan peritonitis, overview
additional information
-
MMP-9 deprived mice show impaired polymorphonuclear leukocyte infiltration at infalmmation sites, 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-/- 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-deficient mice show eliminated elastin breakdown in coronary artery in the Kawasaki disease
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
-
MMP-9 knockout mice show delayed inflammatory response and macrophage infiltration in gastritis
-
additional information
-
enzyme-deficient MPP-9-/- mice show impaired neutrophil infiltration during zymosan peritonitis, overview
-
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
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additional information
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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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0.025 mM panduratin A markedly down-regulates MMP-9 expression
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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
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12-O-tetradecanoyl phorbol-13-acetate-induced MMP-9 expression is decreased by 324.8% by 0.1 mM silibinin
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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
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50 mg/kg (-)-epigallocatechin gallate administration significantly inhibits the induction of the active form of MMP-9
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a significant increase in MMP-9 is observed in pulmonary tuberculosis patients as compared to healthy controls
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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
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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
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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
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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
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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)
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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
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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
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circulating MMP-9 concentrations are higher in patients with abdominal aortic aneurysm than those in subjects without abdominal aortic aneurysm
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diet-induced long-term weight loss decreases MMP-9
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Dz13 upregulates the matrix metalloproteinase-9 in cultured tumor cells
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elevated plasma levels of MMP-9 are correlated with brain levels within 24 h of acute cerebral ischemia in rats
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epidermal growth factor contributes to prostate cancer metastasis through stimulating MMP-9 secretion from prostate cancer cells
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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)
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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
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expression of MMP9 protein and mRNA increases in rat brain tissue after cardiopulmonary resuscitation
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F(ab')2 fragments or stimulation with lipopolysaccharide have no effect on MMP-9 production
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heregulin-beta1 stimulates MMP-9 secretion and activation via a transcriptional regulation in human breast cancer cells
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higher plasma MMP-9 concentrations are found in periodontal disease patients compared with healthy controls
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homocysteine increases mRNA expression of MMP-9
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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
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in sections of ectopic tumors treated with Dz13, MMP-9 is downregulated
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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
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in vivo administration of a nuclear factor-kappa B inhibitory peptide blocks the expression of MMP-9 in dystrophic muscle of mdx mice
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induction of MMP-9 expression and activity is significantly inhibited by 0.001 mM of the specific cPLA2alpha inhibitor
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interferon-gamma suppresses MMP-9 expression
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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
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islet MMP-9 mRNA levels are decreased in type 2 diabetic subjects
leucine-zipper and sterile-alpha motif kinase reduces MMP-9 activity by increasing TIMP-1/2 expression in H9c2 cardiomyoblast cells
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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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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
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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
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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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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 are induced by 0.002 mM prostaglandin E2
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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 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
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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
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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
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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 an increase in the active form of MMP-9 after ischemia
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there is no difference in expression of MMP-9 for any follicle size or health status class
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there is no MMP-9 mRNA elevation in mononuclear cells
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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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TX-1877 significantly inhibits expression of MMP-9
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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
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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
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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
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auto-amplified NFATc1 plays a key role in upregulating MMP-9
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auto-amplified NFATc1 plays a key role in upregulating MMP-9
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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 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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diagnostics
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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
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MMP-9 expression is an independent and significant factor for prediction of a poor prognosis in colorectal cancer
diagnostics
-
MMP-9 levels are useful in endometriosis diagnostics
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
drug development
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MMP-9 is a target for therapeutic treatment
drug development
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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
-
abundant expression of enzyme by synovial tissue mast cells in patients with rheumatoid arthritis but not in normal control
medicine
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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
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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
-
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
-
enzyme is present in extracts from leaking bleb tissue of glaucoma patients, but not in bleb leak fluid or aqueous humor samples
medicine
-
enzyme levels are significantly elevated in cerebrospinal fluid of patients with vascular dementia compared to those with Alzheimer disease and to control
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
-
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
-
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
-
incubation of lenses with enzyme leads immediately to cataract
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
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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
-
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
-
a positive correlation between MMP-9 values and gestational age is observed in normal pregnant women
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
-
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
-
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
-
matrix metalloproteinase is an independent predictor of the reduced nitrate-mediated dilatation in the type 1 diabetes mellitus
medicine
-
matrix metalloproteinase-9 is an independent prognostic marker in laryngeal and hypopharyngeal cancer
medicine
-
MMP-9 expression positively correlates with prognosis of oral squamous cell carcinoma
medicine
-
MMP-9 genotype polymorphisms are primary predictors for oral squamous cell carcinoma risk
medicine
-
MMP-9 is a marker of endothelial activation and dysfunction
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
-
serum MMP-9 level is related to FEV1 decline
medicine
-
the expression of the mRNA of MMP-9 is not significantly elevated with the progression of biliary-associated liver fibrosis
medicine
-
the functional polymorphism C1562T in the promoter of matrix metalloproteinase-9 gene is associated with susceptibility to knee osteoarthritis in the Turkish population
medicine
-
the reduction of MMP-9 activity may have a possible therapeutic effect for the management of brain injury after focal ischemia
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
-
controlling MMP-9 expression has therapeutic potential in Parkinson's disease
medicine
-
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
-
higher circulating MMP-9 concentrations are associated with abdominal aortic aneurysm presence
medicine
-
imbalance between total MMP-9 and TIMP-1 may contribute to the pathogenesis of lupus nephritis
medicine
-
MMP-9 is a nontraditional cardiovascular risk factor
medicine
-
MMP-9 is a potential target for cerebral ischemic treatment in human stroke therapy
medicine
-
MMP-9 is a potential therapeutic target for gastric adenocarcinomas
medicine
-
MMP-9 is a potentially useful biomarker for diagnosing, classifying, and monitoring dysfunctional tear syndrome
medicine
-
MMP-9 is a promising target for a neuroprotective approach to preventing seizure-induced hippocampal damage
medicine
-
MMP-9 overexpression is an early marker of breast carcinogenesis preceding tumor invasion
medicine
-
MMP-9 plasma levels are predictive of cognitive performance following carotid endarterectomy
medicine
-
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
-
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
-
the serum levels of MMP-9 significantly correlate with the occurrence and severity of acute graft-versus-host disease
medicine
-
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