Information on EC 3.4.24.35 - gelatinase B

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The expected taxonomic range for this enzyme is: Eukaryota

EC NUMBER
COMMENTARY
3.4.24.35
-
RECOMMENDED NAME
GeneOntology No.
gelatinase B
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cleavage of gelatin types I and V and collagen types IV and V
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
92 kDa gelatinase
-
-
-
-
92 kDa gelatinase
-
-
92 kDa type IV collagenase
-
-
92 kDa type IV collagenase proMMP-9
-
-
92-kDa Gelatinase
-
-
-
-
92-kDa gelatinase B
-
-
92-kDa gelatinase B
-
-
92-kDa Type IV collagenase
-
-
-
-
92-kDa Type IV collagenase
-
-
95 kDa type IV collagenase/gelatinase
-
-
-
-
Collagenase IV
-
-
-
-
Collagenase type IV
-
-
-
-
gelatinase
-
-
gelatinase B
P50282
-
Gelatinase MMP 9
-
-
-
-
GELB
-
-
-
-
Macrophage gelatinase
-
-
-
-
matrix metallopeptidase 9
-
-
matrix metallopeptidase 9 gelatinase B
-
-
matrix metalloprotease-9
-
-
Matrix metalloproteinase 9
-
-
-
-
Matrix metalloproteinase 9
Mus musculus FVB/NJ
-
-
-
Matrix metalloproteinase 9
-
-
matrix metalloproteinase-9
-
-
matrix metalloproteinase-9
-
-
matrix metalloproteinase-9
-
-
matrix metalloproteinase-9
P14780
-
matrix metalloproteinase-9
P41245
-
matrix metalloproteinase-9
Q2M4J5
-
matrix metalloproteinase-9
Mus musculus BALB/c, Mus musculus C57BL/6
-
-
-
matrix metalloproteinase-9
-
-
matrix metalloproteinase-9
P50282
-
matrix metalloproteinase-9
-
-
matrix metalloproteinase-9
Trypanosoma cruzi Y
-
-
-
metrix metalloproteinase-9
-
-
MMP 9
-
-
-
-
MMP 9
-
-
MMP-9
-
-
MMP-9
-
-
MMP-9
P14780
-
MMP-9
P41245
-
MMP-9
Q2M4J5
-
MMP-9
Mus musculus BALB/c, Mus musculus C57BL/6, Mus musculus FVB/NJ
-
-
-
MMP-9
P50282
-
MMP-9
Trypanosoma cruzi Y
-
-
-
MMP9
Mus musculus BALB/c
-
-
-
neutrophil collagenase
-
-
pro-matrix metalloproteinase-9
-
-
Type IV collagen metalloproteinase
-
-
-
-
Type IV collagen metalloproteinase
-
-
Type IV collagenase
-
-
-
-
Type IV collagenase
-
-
Type IV collagenase/gelatinase
-
-
-
-
Type IV collagenase/gelatinase
-
-
Type V collagenase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
146480-36-6
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
cattle infected with Echinococcus granulosus
-
-
Manually annotated by BRENDA team
children with aseptic and bacterial meningitis
-
-
Manually annotated by BRENDA team
glaucoma patients with leaking or overhanging blebs
-
-
Manually annotated by BRENDA team
human
SwissProt
Manually annotated by BRENDA team
patients with benign prostate hyperplasia, localized prostate cancer or metastatic disease
-
-
Manually annotated by BRENDA team
patients with bladder cancer
-
-
Manually annotated by BRENDA team
patients with epidermolysis bullosa acquisita and bullous pemphigoid
-
-
Manually annotated by BRENDA team
patients with pleural effusions, such as malignant pleural effusion, breast carcinoma or lung carcinoma
-
-
Manually annotated by BRENDA team
patients with proliferative diabetic retinopathy
-
-
Manually annotated by BRENDA team
patients with sympathetic ophthalmia
-
-
Manually annotated by BRENDA team
patients with vascular dementia and Alzheimer disease
-
-
Manually annotated by BRENDA team
recombinant enzyme
-
-
Manually annotated by BRENDA team
C57BL/6 mice
-
-
Manually annotated by BRENDA team
C57BL/6, FVB/NJ, or MMP-9-/-, with FVB/NJ background, mice
-
-
Manually annotated by BRENDA team
female C57BL/6 mice
-
-
Manually annotated by BRENDA team
FVB/NJ mice
-
-
Manually annotated by BRENDA team
mouse
-
-
Manually annotated by BRENDA team
Mus musculus BALB/c
-
-
-
Manually annotated by BRENDA team
Mus musculus BALB/c
Balb/c mice
-
-
Manually annotated by BRENDA team
Mus musculus C57BL/6
-
-
-
Manually annotated by BRENDA team
Mus musculus C57BL/6
C57BL/6 mice
-
-
Manually annotated by BRENDA team
Mus musculus FVB/NJ
FVB/NJ mice
-
-
Manually annotated by BRENDA team
Fisher344 rats
-
-
Manually annotated by BRENDA team
Long-Evans female rats
-
-
Manually annotated by BRENDA team
male sprague-dawley rats
-
-
Manually annotated by BRENDA team
strain Y
-
-
Manually annotated by BRENDA team
Trypanosoma cruzi Y
strain Y
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
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
-
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
-
matrix metalloprotease-9 inhibition improves amyloid beta-mediated cognitive impairment and neurotoxicity in mice
malfunction
-
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
-
mice that lack matrix metalloproteinase-9 display delayed wound healing associated with delayed reepithelization and disordered collagen fibrillogenesis
malfunction
-
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
-
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
-
MMP-9 knockdown blocks SGC-7901 cells' invasion, migration and proliferation
malfunction
-
MMP-9 knockout mice are resistant to dextran sodium sulfate-, Salmonella typhimurium-, or trinitrobenzene sulfonic acid-induced colitis
malfunction
-
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
-
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
-
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
-
inhibition of MMP activity, especially MMP-9, has the potential to inhibit tumor growth and metastasis
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
malfunction
Mus musculus BALB/c
-
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
Mus musculus C57BL/6
-
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
-
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
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
Q2M4J5
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
Mus musculus C57BL/6
-
neutrophil-derived matrix metalloproteinase-9 is a potent activator of trypsinogen in acinar cells in acute pancreatitis
-
metabolism
Mus musculus BALB/c
-
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
-
additional information
-
specific inhibition of MMP-9 leads to reduced extents of HIV-1 antigen presentation activity
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(7-methoxycoumarin-4-yl)-acetyl-Pro-Leu-Gly-Leu-(3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-Ala-Arg-NH2 + H2O
?
show the reaction diagram
-
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Pro-Leu-Gly-Leu-beta-(2,4-dinitrophenylamino)Ala-Ala-Arg-NH2 + H2O
?
show the reaction diagram
Mus musculus, Mus musculus C57BL/6
-
-
-
-
?
(7-methoxycoumaryl-4yl)acetylPLGLA2pr(2,4-dinitrophenol)-AR-NH2 + H2O
?
show the reaction diagram
P45452
-
-
?
2,4-dinitrophenyl-Pro-beta-cyclohexylalanyl-Gly-Cys(Me)-His-Ala-Lys(N-Me-2-aminobenzoyl)-NH2 + H2O
?
show the reaction diagram
-
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
show the reaction diagram
-
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
?
show the reaction diagram
-
-
-
-
?
Ac-L-Pro-L-Pro(OH)-Gly-L-Gln-Gly-L-Ala-L-Thr-Gly-L-Glu-L-Pro(OH)-Gly-NH2 + H2O
?
show the reaction diagram
-
-
-
-
?
actin + H2O
?
show the reaction diagram
-
-
-
-
?
ADAM 2 + H2O
?
show the reaction diagram
-
putative protein substrate with potential cleavage site
-
?
aggrecan + H2O
?
show the reaction diagram
-
-
-
?
Aggrecan core protein + H2O
?
show the reaction diagram
-
-
-
-
?
alpha 1(I) collagen + H2O
?
show the reaction diagram
-
-
-
?
alpha 1(V) collagen + H2O
?
show the reaction diagram
-
-
-
?
alpha 1(XI) collagen + H2O
?
show the reaction diagram
-
-
-
?
alpha 2(V) collagen + H2O
?
show the reaction diagram
-
-
-
?
alpha-amylase precursor + H2O
?
show the reaction diagram
-
-
-
-
?
alpha-enolase + H2O
?
show the reaction diagram
-
-
-
-
?
alpha-N-acetylglucosaminidase + H2O
?
show the reaction diagram
-
-
-
-
?
amyloid protein precursor + H2O
?
show the reaction diagram
-
-
-
-
?
amyloid-beta A4 protein precursor + H2O
?
show the reaction diagram
-
-
-
-
?
annexin I + H2O
?
show the reaction diagram
-
-
-
-
?
Arp2/3 complex subunit + H2O
?
show the reaction diagram
-
-
-
-
?
arylsulfatase B precursor + H2O
?
show the reaction diagram
-
-
-
-
?
beta-glucuronidase precursor + H2O
?
show the reaction diagram
-
-
-
-
?
beta-hexosaminidase beta chain precursor + H2O
?
show the reaction diagram
-
-
-
-
?
beta1-integrin + H2O
?
show the reaction diagram
-
-
-
-
?
beta2 integrin subunit CD18 + H2O
?
show the reaction diagram
-
-
-
-
?
betaB1 crystallin + H2O
?
show the reaction diagram
-
main enzyme substrate in lens extract
-
-
?
Cartilage link protein + H2O
?
show the reaction diagram
-
-
-
?
cathepsin E precursor + H2O
?
show the reaction diagram
-
-
-
-
?
CB3 alpha 1(IV) collagen + H2O
?
show the reaction diagram
-
-
-
?
CD25 + H2O
?
show the reaction diagram
-
CD25 is proteolytic cleaved to its soluble form by MMP-9
-
-
?
CD316 antigen + H2O
?
show the reaction diagram
-
-
-
-
?
chondroitin sulfate proteoglycan + H2O
?
show the reaction diagram
-
-
-
-
?
citrate synthase + H2O
?
show the reaction diagram
-
-
-
-
?
Collagen + H2O
?
show the reaction diagram
-
-
-
-
?
Collagen + H2O
?
show the reaction diagram
-
-
-
-
?
Collagen + H2O
?
show the reaction diagram
-
-
-
-
?
Collagen + H2O
?
show the reaction diagram
P41245
-
-
-
?
Collagen + H2O
?
show the reaction diagram
-
type IV
-
-
-
Collagen + H2O
?
show the reaction diagram
-
type V
-
-
-
Collagen + H2O
?
show the reaction diagram
-
type I, not native, type I (denatured)
-
-
-
Collagen + H2O
?
show the reaction diagram
-
type IV (native)
-
-
-
Collagen + H2O
?
show the reaction diagram
-
cleavage of the carboxyl-terminal triple helix-containing region
-
-
-
Collagen + H2O
?
show the reaction diagram
-
cleaves between residues Gly439-Val in both alpha1(V) and alpha(XI) and between residues Gly445-Leu in the alpha2(V) chain
-
-
-
Collagen + H2O
?
show the reaction diagram
-
type I, binding, no cleavage
-
-
-
Collagen + H2O
?
show the reaction diagram
-
type V (native)
-
-
-
Collagen + H2O
?
show the reaction diagram
-
type XIV
-
-
-
Collagen + H2O
?
show the reaction diagram
-
MMP-9 inhibits collagen-induced platelet aggregation
-
-
?
collagen I + H2O
?
show the reaction diagram
-
-
-
-
?
Collagen type I + H2O
?
show the reaction diagram
-
-
-
-
?
Collagen type I + H2O
?
show the reaction diagram
-
soluble, native collagen type I, zymography
-
-
?
collagen type II + H2O
?
show the reaction diagram
-
-
-
-
?
Collagen type III + H2O
?
show the reaction diagram
-
MMP-9 cleaves native, triple helical type III collagen to generate a 3/4 fragment, zymography
-
-
?
collagen type IV + H2O
?
show the reaction diagram
-
-
-
-
?
collagen type IV + H2O
?
show the reaction diagram
-
-
-
-
?
collagen type IV + H2O
?
show the reaction diagram
-
collagen zymography
-
-
?
collagen type V + H2O
?
show the reaction diagram
-
-
-
-
?
collagen type V + H2O
?
show the reaction diagram
-
-
-
-
?
collagen type VII + H2O
?
show the reaction diagram
-
-
-
-
?
collagen type XI + H2O
?
show the reaction diagram
-
-
-
-
?
desmoglein 3 + H2O
?
show the reaction diagram
-
putative protein substrate with potential cleavage site
-
?
DGRNIYNIHVEDSLECVKGPNVAA + H2O
?
show the reaction diagram
-
-
-
-
?
ECVKGPNVAAIVGGT + H2O
ECVKGPNVAA + IVGGT
show the reaction diagram
-
-
-
-
?
Elastin + H2O
?
show the reaction diagram
-
-
-
-
?
Elastin + H2O
?
show the reaction diagram
-
-
-
-
?
Elastin + H2O
?
show the reaction diagram
-
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
-
-
?
endoglin + H2O
?
show the reaction diagram
-
putative protein substrate with potential cleavage site
-
?
endothilin receptor + H2O
?
show the reaction diagram
-
putative protein substrate with potential cleavage site
-
?
ephB1 + H2O
?
show the reaction diagram
-
-
-
?
epidermal growth factor + H2O
?
show the reaction diagram
-
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
-
-
?
epididymis-specific alpha-mannosidase precursor + H2O
?
show the reaction diagram
-
-
-
-
?
ezrin + H2O
?
show the reaction diagram
-
-
-
-
?
fibrillar collagen + H2O
?
show the reaction diagram
-
degradation
-
-
?
fibrillar collagen + H2O
?
show the reaction diagram
-
degradation, MMP-9 is involved in development of osteoarthritis, overview, degradation, cleavage within the triple helix
-
-
?
Fibronectin + H2O
?
show the reaction diagram
-
-
-
-
?
Fibronectin + H2O
?
show the reaction diagram
-
-
-
-
?
filamin B + H2O
?
show the reaction diagram
-
-
-
-
?
fragments of human collagen type II + H2O
?
show the reaction diagram
-
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
?
show the reaction diagram
-
-
-
?
Galectin-3 + H2O
?
show the reaction diagram
-
-
-
-
?
Galectin-3 + H2O
?
show the reaction diagram
-
a galactoside-binding protein, major cleavage site is the Ala62-Tyr63 bond
-
-
-
Gelatin + H2O
?
show the reaction diagram
-
-
-
-
-
Gelatin + H2O
?
show the reaction diagram
-
-
-
?
Gelatin + H2O
?
show the reaction diagram
-
-
-
-
?
Gelatin + H2O
?
show the reaction diagram
P14780
-
-
-
?
Gelatin + H2O
?
show the reaction diagram
-
-
-
-
?
Gelatin + H2O
?
show the reaction diagram
-
-
-
-
?
Gelatin + H2O
?
show the reaction diagram
-
-
-
-
?
Gelatin + H2O
?
show the reaction diagram
-
-
-
-
?
Gelatin + H2O
?
show the reaction diagram
-
-
-
-
?
Gelatin + H2O
?
show the reaction diagram
-
-
-
-
?
Gelatin + H2O
?
show the reaction diagram
P41245
-
-
-
?
Gelatin + H2O
?
show the reaction diagram
P50282
-
-
-
?
Gelatin + H2O
?
show the reaction diagram
-
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
?
show the reaction diagram
-
gelatin zymography
-
-
?
Gelatin + H2O
?
show the reaction diagram
-
gelatin zymography
-
-
?
Gelatin + H2O
?
show the reaction diagram
P14780
gelatin zymography
-
-
?
Gelatin + H2O
?
show the reaction diagram
-
gelatin zymography
-
-
?
Gelatin + H2O
?
show the reaction diagram
-
gelatin zymography
-
-
?
Gelatin + H2O
?
show the reaction diagram
-
gelatin zymography using gelatin and fluorescence-conjugated gelatin peptides
-
-
?
Gelatin + H2O
?
show the reaction diagram
-
gelatin zymography, from porcine skin
-
-
?
Gelatin + H2O
?
show the reaction diagram
-
gelatin zymography, gelatin from porcine skin
-
-
?
Gelatin + H2O
?
show the reaction diagram
-
gelatin zymography, mass spectrometrical analysis, overview
-
-
?
Gelatin + H2O
?
show the reaction diagram
-
zymographic analysis
-
-
?
Gelatin + H2O
?
show the reaction diagram
Trypanosoma cruzi Y
-
-
-
-
?
Gelatin + H2O
?
show the reaction diagram
Mus musculus FVB/NJ
-
gelatin zymography
-
-
?
Gelatin + H2O
?
show the reaction diagram
Mus musculus BALB/c
-
-
-
-
?
Gelatin + H2O
?
show the reaction diagram
Mus musculus BALB/c
-
gelatin zymography, gelatin from porcine skin
-
-
?
Gelatin + H2O
?
show the reaction diagram
Mus musculus C57BL/6
-
gelatin zymography
-
-
?
gelsolin + H2O
?
show the reaction diagram
-
-
-
-
?
Golgi apparatus protein 1 precursor + H2O
?
show the reaction diagram
-
-
-
-
?
heat shock protein 27 + H2O
?
show the reaction diagram
-
-
-
-
?
heat shock protein 70 + H2O
?
show the reaction diagram
-
-
-
-
?
heat shock protein 90 + H2O
?
show the reaction diagram
-
-
-
-
?
histidyl-tRNA synthetase + H2O
?
show the reaction diagram
-
-
-
-
?
HMGB1 protein + H2O
?
show the reaction diagram
-
-
-
-
?
integrin beta5 + H2O
?
show the reaction diagram
-
putative protein substrate with potential cleavage site
-
?
interleukin-1beta + H2O
?
show the reaction diagram
-
-
-
-
?
kallikrein + H2O
?
show the reaction diagram
-
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
?
show the reaction diagram
-
-
-
-
?
ladinin 1 + H2O
?
show the reaction diagram
-
putative protein substrate with potential cleavage site
-
?
Laminin + H2O
?
show the reaction diagram
-
-
-
-
?
Laminin + H2O
?
show the reaction diagram
-
-
-
-
-
Laminin + H2O
?
show the reaction diagram
-
-
-
-
?
Laminin + H2O
?
show the reaction diagram
-
-
-
-
?
laminin alpha3 chain + H2O
?
show the reaction diagram
-
putative protein substrate with potential cleavage site
-
?
lipase A + H2O
?
show the reaction diagram
-
-
-
-
?
LS276-THP + H2O
?
show the reaction diagram
-
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
-
-
?
myelin basic protein + H2O
?
show the reaction diagram
-
-
-
?
N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl-7-methoxycoumarin-4-yl acetyl + H2O
?
show the reaction diagram
-
-
-
?
N-acetylglucosamine-6-sulfatase precursor + H2O
?
show the reaction diagram
-
-
-
-
?
N-alpha-benzoyl-arginine p-nitroanilide + H2O
N-alpha-benzoyl-Arg + 4-nitroaniline
show the reaction diagram
-
i.e. BAPNA
-
-
?
N-cadherin + H2O
?
show the reaction diagram
-
-
-
-
?
Neonatal human proteoglycan + H2O
?
show the reaction diagram
-
poor substrate, cleavage of the His16-Ile17 bond
-
-
-
nucleolin + H2O
?
show the reaction diagram
-
-
-
-
?
occludin + H2O
?
show the reaction diagram
-
-
-
-
?
pancreatic alpha-amylase isozyme + H2O
?
show the reaction diagram
-
-
-
-
?
peptide A13 + H2O
?
show the reaction diagram
-
-
-
?
peptide A13R + H2O
?
show the reaction diagram
-
-
-
?
peptide A3 + H2O
?
show the reaction diagram
-
-
-
?
peptide A34 + H2O
?
show the reaction diagram
-
-
-
?
peptide B74 + H2O
?
show the reaction diagram
-
-
-
?
peptide C15 + H2O
?
show the reaction diagram
-
non-selective peptide substrate
-
?
peptide C9 + H2O
?
show the reaction diagram
-
-
-
?
peptide m1A11 + H2O
?
show the reaction diagram
-
non-selective peptide substrate
-
?
peroxiredoxin 4 + H2O
?
show the reaction diagram
-
-
-
-
?
phosphate regulating neutral endopeptidase + H2O
?
show the reaction diagram
-
putative protein substrate with potential cleavage site
-
?
platelet factor 4 precursor + H2O
?
show the reaction diagram
-
-
-
-
?
pro-urokinase + H2O
active urokinase + prosequence of urokinase
show the reaction diagram
Mus musculus, Mus musculus C57BL/6
-
-
-
-
?
Proteoglycan + H2O
?
show the reaction diagram
-
-
-
-
?
retinoic acid early inducible protein 1 alpha-precursor + H2O
?
show the reaction diagram
-
-
-
-
?
retinoid-inducible serine carboxypeptidase precursor + H2O
?
show the reaction diagram
-
-
-
-
?
SGFGSRYLTA + H2O
?
show the reaction diagram
-
-
-
?
SGKGPRQITA + H2O
?
show the reaction diagram
-
-
-
?
SGKIPRRLTA + H2O
?
show the reaction diagram
-
-
-
?
SGKIPRTATA + H2O
?
show the reaction diagram
-
-
-
?
SGKIPRTLTA + H2O
?
show the reaction diagram
-
-
-
?
SGLKAMITA + H2O
?
show the reaction diagram
-
-
-
?
SGLPAKSTA + H2O
?
show the reaction diagram
-
-
-
?
SGPLFYSVTA + H2O
?
show the reaction diagram
-
-
-
?
SGPRAVSTTA + H2O
?
show the reaction diagram
-
-
-
?
SGQPHYLTTA + H2O
?
show the reaction diagram
-
-
-
?
snRNP D3 + H2O
?
show the reaction diagram
-
-
-
-
?
stathmin + H2O
?
show the reaction diagram
-
-
-
-
?
stromelysin 1 + H2O
?
show the reaction diagram
P45452
-
-
?
succinylated gelatin + H2O
?
show the reaction diagram
-
-
-
-
?
tissue factor pathway inhibitor + H2O
?
show the reaction diagram
-
-
-
?
transforming growth factor-beta + H2O
?
show the reaction diagram
-
MMP9 mediates activation of latent transforming growth factor-beta
-
-
?
tubulin + H2O
?
show the reaction diagram
-
-
-
-
?
Type IV collagen + H2O
?
show the reaction diagram
-
-
-
-
?
type V collagen + H2O
?
show the reaction diagram
-
-
-
-
?
type XI collagen + H2O
?
show the reaction diagram
-
-
-
-
?
vascular endothelial-cadherin + H2O
?
show the reaction diagram
P41245
-
-
-
?
Vitronectin + H2O
?
show the reaction diagram
-
65000 MW and 75000 MW form of vitronectin
-
-
-
moesin + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
specificity overview, 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
?
-
-
peptide A16 SGRR LLSRTA and peptide C11 SGRR LIHHTA are no substrates
-
?
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
?
-
-
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
?
-
P45452
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
?
-
-
independent of its proteolytic function, enzyme has a biphasic effect on smooth muscle cell-mediated collagen gel contraction
-
-
-
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
?
-
-
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
?
-
-
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
?
-
-
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
?
-
-
astrocyte-released MMP-9 is involved in interleukin-1beta induced neurotoxicity, probably via urokinase plasminogen activator, overview
-
-
-
additional information
?
-
-
gastric gelatinase B is rapidly increased in Helicobacter felis-infected mice and is involved in induction of gastritis
-
-
-
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
?
-
-
inhibition of MMP-9 prevents neutrophilic inflammation in ventilator-induced lung injury, VILI, and pulmonary hemorrhage, 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 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 expression is increased in cancers, inhibition of MMP-9 has a therapeutic benefit to cancer
-
-
-
additional information
?
-
-
MMP-9 inhibitor completely inhibits PAF-induced B16F10 metastasis
-
-
-
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 essential for neutrophil infiltration during zymosan peritonitis
-
-
-
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 involved in murine peritonitis by participating in cellular migration, molecular mechanism, 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
?
-
-
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
?
-
-
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
-
-
-
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
?
-
-
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
?
-
Mus musculus FVB/NJ
-
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
?
-
Mus musculus BALB/c
-
MMP-9 is involved in murine peritonitis by participating in cellular migration, molecular mechanism, overview
-
-
-
additional information
?
-
Mus musculus BALB/c
-
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
?
-
Mus musculus C57BL/6
-
gastric gelatinase B is rapidly increased in Helicobacter felis-infected mice and is involved in induction of gastritis
-
-
-
additional information
?
-
Mus musculus C57BL/6
-
MMP-9 is essential for neutrophil infiltration during zymosan peritonitis
-
-
-
additional information
?
-
Mus musculus C57BL/6
-
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
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
Aggrecan core protein + H2O
?
show the reaction diagram
-
-
-
-
?
chondroitin sulfate proteoglycan + H2O
?
show the reaction diagram
-
-
-
-
?
Collagen + H2O
?
show the reaction diagram
-
-
-
-
?
Collagen + H2O
?
show the reaction diagram
-
MMP-9 inhibits collagen-induced platelet aggregation
-
-
?
collagen I + H2O
?
show the reaction diagram
-
-
-
-
?
Collagen type I + H2O
?
show the reaction diagram
-
-
-
-
?
Collagen type III + H2O
?
show the reaction diagram
-
-
-
-
?
collagen type IV + H2O
?
show the reaction diagram
-
-
-
-
?
collagen type IV + H2O
?
show the reaction diagram
-
-
-
-
?
collagen type V + H2O
?
show the reaction diagram
-
-
-
-
?
collagen type V + H2O
?
show the reaction diagram
-
-
-
-
?
collagen type XI + H2O
?
show the reaction diagram
-
-
-
-
?
Elastin + H2O
?
show the reaction diagram
-
-
-
-
?
Elastin + H2O
?
show the reaction diagram
-
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
?
show the reaction diagram
-
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
?
show the reaction diagram
-
degradation
-
-
?
fibrillar collagen + H2O
?
show the reaction diagram
-
degradation, MMP-9 is involved in development of osteoarthritis, overview
-
-
?
Fibronectin + H2O
?
show the reaction diagram
-
-
-
-
?
Fibronectin + H2O
?
show the reaction diagram
-
-
-
-
?
Gelatin + H2O
?
show the reaction diagram
-
-
-
-
?
Gelatin + H2O
?
show the reaction diagram
P14780
-
-
-
?
Gelatin + H2O
?
show the reaction diagram
-
-
-
-
?
Gelatin + H2O
?
show the reaction diagram
-
-
-
-
?
Gelatin + H2O
?
show the reaction diagram
-
-
-
-
?
Gelatin + H2O
?
show the reaction diagram
-
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
?
show the reaction diagram
Mus musculus FVB/NJ
-
-
-
-
?
Gelatin + H2O
?
show the reaction diagram
Mus musculus BALB/c
-
-
-
-
?
Gelatin + H2O
?
show the reaction diagram
Mus musculus C57BL/6
-
-
-
-
?
Laminin + H2O
?
show the reaction diagram
-
-
-
-
?
Laminin + H2O
?
show the reaction diagram
-
-
-
-
?
pro-urokinase + H2O
active urokinase + prosequence of urokinase
show the reaction diagram
Mus musculus, Mus musculus C57BL/6
-
-
-
-
?
transforming growth factor-beta + H2O
?
show the reaction diagram
-
MMP9 mediates activation of latent transforming growth factor-beta
-
-
?
Laminin + H2O
?
show the reaction diagram
-
-
-
-
?
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
?
-
-
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
?
-
P45452
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
?
-
-
independent of its proteolytic function, enzyme has a biphasic effect on smooth muscle cell-mediated collagen gel contraction
-
-
-
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
?
-
-
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
?
-
-
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
?
-
-
astrocyte-released MMP-9 is involved in interleukin-1beta induced neurotoxicity, probably via urokinase plasminogen activator, overview
-
-
-
additional information
?
-
-
gastric gelatinase B is rapidly increased in Helicobacter felis-infected mice and is involved in induction of gastritis
-
-
-
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
?
-
-
inhibition of MMP-9 prevents neutrophilic inflammation in ventilator-induced lung injury, VILI, and pulmonary hemorrhage, 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 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 expression is increased in cancers, inhibition of MMP-9 has a therapeutic benefit to cancer
-
-
-
additional information
?
-
-
MMP-9 inhibitor completely inhibits PAF-induced B16F10 metastasis
-
-
-
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 essential for neutrophil infiltration during zymosan peritonitis
-
-
-
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 involved in murine peritonitis by participating in cellular migration, molecular mechanism, 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
?
-
-
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
?
-
-
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
-
-
-
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
?
-
-
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
?
-
Mus musculus FVB/NJ
-
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
?
-
Mus musculus BALB/c
-
MMP-9 is involved in murine peritonitis by participating in cellular migration, molecular mechanism, overview
-
-
-
additional information
?
-
Mus musculus BALB/c
-
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
?
-
Mus musculus C57BL/6
-
gastric gelatinase B is rapidly increased in Helicobacter felis-infected mice and is involved in induction of gastritis
-
-
-
additional information
?
-
Mus musculus C57BL/6
-
MMP-9 is essential for neutrophil infiltration during zymosan peritonitis
-
-
-
additional information
?
-
Mus musculus C57BL/6
-
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
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
-
dependent on
Ca2+
-
dependent on
Ca2+
-
-
Ca2+
-
required
Ca2+
-
required
Calcium
-
required
Zinc
-
required
Zn2+
-
zinc-dependent proteinase
Zn2+
-
active-site zinc-binding domain
Zn2+
-
a zinc metalloproteinase, contains one Zn2+ per enzyme molecule
Zn2+
-
a zinc metalloproteinase
Zn2+
-
dependent on
Zn2+
-
dependent on, one Zn2+ ion at the active site
Zn2+
-
dependent on
Zn2+
-
-
Zn2+
-
a zinc endopeptidase
Zn2+
-
MMP-9 is a Zn2+-dependent endopeptidase
Zn2+
-
zinc metalloprotease
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2E)-3-(N-hydroxycarbamoyl)-2-(3-phenylpropylidene)propionyl-L-tryptophan-N-methylamide
-
-
(2E)-3-(N-hydroxycarbamoyl)-2-heptylidenepropionyl-L-tryptophan-N-methylamide
-
-
(2E)-3-(N-hydroxycarbamoyl)-2-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
-
-
1,10-phenanthroline
-
10 mM, 100% inhibition
1,10-phenanthroline
-
-
1,10-phenanthroline
-
-
1,10-phenanthroline
-
totally inhibited by 10 mM 1,10-phenanthroline
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
-
AZD-6140
-
-
BB-94
-
broad-spectrum MMP inhibitor
BB1101
-
MMP inhibitor
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
-
CGS 27023A
-
-
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
doxycycline
-
doxyxycline inhibits directlyMMP-9 enzymatic activity derived from tumor necrosis factor-alpha-stimulated vascular smooth muscle cells
doxycycline
-
totally inhibited by 10 mM doyxycline
doxycycline
-
-
doxycycline
-
-
doxycycline
-
inhibitory mechanism and effect on osteoclastogenesis signaling induced by RANKL, both in vitro and in vivo, overview. Although Dox inhibits RANKL-induced osteoclastogenesis and down-modulates the mRNA expression of functional osteoclast markers, it neither affects RANKL-induced MAPKs phosphorylation nor NFATc1 gene expression in RAW264.7 monocytic cells
EDTA
-
10 mM, 74% inhibition
EDTA
-
complete inhibition at 10 mM
GM6001
-
MMP-9-specific inhibitor
GM6001
-
MMP inhibitor, complete inhibition at 0.025 mM
ilomastat
-
-
ilomastat
-
a pan-MMP inhibitor, strong inhibition
Immunoglobulins purified from antisera raised against gelatinase
-
-
-
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-9 inhibitor I
-
highly specific inhibition of MMP-9
MMP-9 inhibitor I
-
-
N,N'-[(2S)-6-[[(2,3-dihydroxyphenyl)carbonyl]amino]hexane-1,2-diyl]bis(2,3-dihydroxybenzamide)
-
-
N-hydroxy-2-(isobutyl[(4-methoxyphenyl)sulfonyl]amino)acetamide
-
50% inhibition at 2.9 nM, comparison with inhibitory effect on matrix metalloproteinases MMP-3, MMp-7, MMP-2
N-[(5R)-5-[[(2,3-dihydroxyphenyl)carbonyl]amino]-6-hydroxyhexyl]-2,3-dihydroxybenzamide
-
-
N-[(5S)-5-[[(2,3-dihydroxyphenyl)carbonyl]amino]-6-hydroxyhexyl]-2,3-dihydroxybenzamide
-
-
N-[(5S)-6-amino-5-[[(2,3-dihydroxyphenyl)carbonyl]amino]hexyl]-2,3-dihydroxybenzamide
-
-
norcantharidin
-
i.e. exo-7-oxabicylo-[2.2.1] heptane-2,3-dicarboxylic anhydride, norcantharidin inhibits gelatinase activity of MM-9 in a concentration- and time-dependent manner
o-phenanthroline
-
-
Phenanthroline
-
-
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
-
-
-
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
-
i.e. tissue inhibitor of metalloproteinase 1, a natural inhibitor
-
TIMP-1
-
formation of proMMP-9/TIMP-1 complexes
-
TIMP-1
-
major inhibitor of MMP-9
-
TIMP-1/2
-
-
-
TIMP-2
-
specific inhibitor for MMP9
-
TIMP-2
-
a MMP inhibitor
-
TIMP-4
-
-
-
TIMP1
-
interaction analysis and structure modeling, overview
-
TIMP2
-
interaction analysis and structure modeling, overview
-
Tissue inhibitor
-
of metalloproteinase-2
-
Tissue inhibitor
-
of metalloproteinase-1; of metalloproteinase-2
-
Tissue inhibitor
-
of metalloproteinases, recombinant
-
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
P45452
-
-
tissue inhibitor of metalloproteinase TIMP-2
P45452
-
-
Tissue inhibitor of metalloproteinase-1
-
1 nM, 88% inhibition
-
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 metalloproteinase-1
-
-
-
Tissue inhibitor of metalloproteinase-2
-
-
-
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
-
MMP-9i
-
MMP-9 inhibitor, an anthranilate hydroxamic acid derivative
-
additional information
-
inhibitor synthesis and molecular docking, overview
-
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
-
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
-
no inhibition by amiloride or plasminogen activator/plasmin inhibitor D-Phe-Pro-Arg-chloromethylketone dihydrochloride
-
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
-
NK4 intervention suppresses MMP9 mRNA expression
-
additional information
-
Notch1 knockdown decreases MMP9 expression
-
additional information
-
gene expression of MMP-9 is significantly suppressed in the hearts of eplerenone-treated mice compared with controls
-
additional information
-
MMP-9 is decreased 12 months after natalizumab treatment in patients with relapsing-remitting multiple sclerosis
-
additional information
-
integrin-linked kinase gene knockdown leads to reduced MMP9 expression
-
additional information
-
doublecortin synthesis suppresses the expression and activation of MMP9
-
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
-
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
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2,3,7,8-tetrachlorodibenzo-p-dioxin
-
both MMP-9 mRNA expression and enzymatic activity are gradually increased with the concentration increase of 2,3,7,8-tetrachlorodibenzo-p-dioxin in media and these changes can be reversed by resveratrol treatment in a dose-dependent manner, c-Jun mediates 2,3,7,8-tetrachlorodibenzo-p-dioxin-induced MMP-9 expression and activity
4-amino phenylmercuric acetate
-
pro-MMP-9 is activated with 1 mM 4-amino phenylmercuric acetate in assay buffer at 37C for 1.5 h
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
-
1 mM
4-aminophenylmercuric acetate
-
after treatment with 4-aminophenylmercuric acetate, affinity-purified W-256 cell gelatinase is converted to a final processed form of 66000 Da
4-aminophenylmercuric acetate
-
1 mM 4-aminophenylmercuric acetate-mediated activation of MMP-9 provokes autocatalytic cleavage of recombinant MMP-9
4-aminophenylmercuric acetate
-
-
4-aminophenylmercuric acetate
-
activation of pro-MMP-9 constructs at pH 7.0
4-aminophenylmercuric acetate
-
artificial activation of the inactive zymogen
acrolein
-
activates MMP-9 via EGFR/MAPK signaling and stimulation of pro-MMP-9 cleavage
APMA
-
-
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
interleukin-1
-
-
-
Interleukin-1beta
-
-
-
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
-
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
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
-
-
-
tumor necrosis factor-alpha
-
-
-
matrix metalloproteinase-7
P41245
MMP-9 is activated by matrix metalloproteinase-7
-
additional information
-
tissue kallikrein is a potent activator of latent proenzyme
-
additional information
-
binding of the zymogen to fetuin or asialofetuin results in activation
-
additional information
-
MMP-9 is upregulated by tumor necrosis factor alpha, TNFalpha
-
additional information
-
beta-hematin, and not hemin, accelerates the activation of MMP-9, activation of MMP-9 by hemin and MMP-3, overview
-
additional information
-
activation of pro-MMP-9 by 4-aminophenylmercuric acetate
-
additional information
-
MMP-9 is induced in small renal arteries by recombinant human relaxin, up-regulation of 70%
-
additional information
-
implantation of 9L glioma cells into brain increases the expression of MMP-9, overview
-
additional information
-
gastric gelatinase B is rapidly increased in Helicobacter felis-induced gastritis
-
additional information
-
activation by trypsin, MMP3, and MMP10, computational model of MMP9 activation and inhibition, overview
-
additional information
-
pulmonary infection with the Gram-negative intracellular bacterium Francisella tularensis, a category A biological threat agent, induces MMP-9 expression
-
additional information
-
relaxin induces enzyme expression in THP-1 cells, while it reduces expression of NF-kappaB inhibitor protein, IkappaB-alpha, overview
-
additional information
-
interleukin-1beta induces MMP-9 activity
-
additional information
-
8-bromo-cGMP yields increases in active MMP-9
-
additional information
-
human arteries subjected to ex vivo angioplasty and stent implantation display increased in-stent intimal hyperplasia and higher MMP-9 activity in the presence of leukotriene B4
-
additional information
-
treatment with tissue necrosis factor increases MMP9 release while pre-treatment with alpha-lipoic acid (6,8-dithio-octanoic acid) inhibits this tissue necrosis factor-induced effect
-
additional information
-
dermal fibroblasts and hepatic stellate cells require type-I collagen which boosts Jun N-terminal kinase activity to maximally induce MMP-9
-
additional information
P50282
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
-
Notch1 may be involved in MMP9 activation either by enhancing its expression or by stabilizing the protein
-
additional information
-
high glucose (25 mM) induces expression of MMP-9
-
additional information
-
activator protein-4 expression may play an important role in the induction of synthesis of MMP-9
-
additional information
-
ectopic Fra-1 markedly stimulates MMP-9 mRNA expression
-
additional information
-
MMP-9 is activated by a whole-cell extract from Prevotella nigrescens ATCC 33563
-
additional information
-
several members of the vascular endothelial growth factor family and the three vascular endothelial growth factor receptors are responsible for secretion of MMP-9 via an autocrine loop
-
additional information
-
0.001-0.04 mM arachidonic acid increases matrix metalloproteinase 9 secretion and expression at the mRNA level; eicosapentaenoic acid, docosapentaenoic acid or docosahexaenoic acid by themselves have no effect on MMP-9 secretion
-
additional information
-
the MMP-9 mRNA expression is inducible by vascular endothelial growth factor
-
additional information
-
treatment with phorbol 12-myristate 13-acetate (100 ng/ml) induces MMP-9 expression in glandular epithelia, supportive connective tissue, and muscle tissue cell lines
-
additional information
-
cells treated with more than 1 ng/ml of tissue growth factor-beta1 secrete pro-MMP-9 in a dose dependant manner, addition of 20 ng/ml of tissue necrosis factor-alpha further upregulates pro-MMP-9 expression
-
additional information
-
MMP-9 expression is increased after a 16 h acetaldehyde treatment (0.1 mM)
-
additional information
-
benzo[a]pyrene increases the mRNA level of matrix metalloproteinase 9
-
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
-
the presence of an intact active site and hemopexin domain are required for full angiogenesis-inducing activity of the MMP-9 enzyme
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00422
N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl-7-methoxycoumarin-4-yl acetyl
-
pH 7.6, 25C, wild type
0.00496
N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl-7-methoxycoumarin-4-yl acetyl
-
pH 7.6, 25C, recombinant enzyme
0.8
SGFGSRYLTA
-
pH 7.5, 37C, peptide A19
3.7
SGKGPRQITA
-
pH 7.5, 37C, peptide C15
1.4
SGKIPRRLTA
-
pH 7.5, 37C, peptide A11m1
4.7
SGKIPRTATA
-
pH 7.5, 37C, peptide A11m2
1.3
SGKIPRTLTA
-
pH 7.5, 37C, peptide A11
2.4
SGLKALMITA
-
pH 7.5, 37C, peptide A7
13.5
SGLRPAKSTA
-
pH 7.5, 37C, peptide A18
0.5
SGPLFYSVTA
-
pH 7.5, 37C, peptide A10
2.9
SGPRAVSTTA
-
pH 7.5, 37C, peptide A6
1
SGQPHYLTTA
-
pH 7.5, 37C, peptide B1
0.000013
stromelysin1
P45452
pH 7.5, 37C, monomeric form
-
0.000025
stromelysin1
P45452
pH 7.5, 37C, dimeric form
-
0.0013
vitronectin
-
75000 MW form
-
0.0015
65000 MW form of vitronectin
-
-
-
additional information
additional information
-
detailed binding kinetics
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.04 - 1.97
(7-methoxycoumaryl-4yl)acetylPLGLA2pr(2,4-dinitrophenol)-AR-NH2
P45452
pH 7.5, 37C, dimeric form
2.72
(7-methoxycoumaryl-4yl)acetylPLGLA2pr(2,4-dinitrophenol)-AR-NH2
P45452
pH 7.5, 37C, monomeric form
3 - 6
(7-methoxycoumaryl-4yl)acetylPLGLA2pr(2,4-dinitrophenol)-AR-NH2
P45452
pH 7.5, 37C, monomeric form
8.67
(7-methoxycoumaryl-4yl)acetylPLGLA2pr(2,4-dinitrophenol)-AR-NH2
P45452
pH 7.5, 37C, dimeric form
0.0005
65000 MW form of vitronectin
-
-
-
0.000333
75000 MW form of vitronectin
-
-
-
11
SGFGSRYLTA
-
pH 7.5, 37C, peptide A19
703
SGKGPRQITA
-
pH 7.5, 37C, peptide C15
224
SGKIPRRLTA
-
pH 7.5, 37C, peptide A11m1
9.4
SGKIPRTATA
-
pH 7.5, 37C, peptide A11m2
86.4
SGKIPRTLTA
-
pH 7.5, 37C, peptide A11
30
SGLKALMITA
-
pH 7.5, 37C, peptide A7
78
SGLRPAKSTA
-
pH 7.5, 37C, peptide A18
20
SGPLFYSVTA
-
pH 7.5, 37C, peptide A10
178
SGPRAVSTTA
-
pH 7.5, 37C, peptide A6
9
SGQPHYLTTA
-
pH 7.5, 37C, peptide B1
0.00041
stromelysin 1
P45452
pH 7.5, 37C, dimeric form
-
0.0019
stromelysin 1
P45452
pH 7.5, 37C, monomeric form
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00000713
TIMP-1
P45452
pH 7.5, 37C, dimeric form
-
0.00000817
TIMP-1
P45452
pH 7.5, 37C, monomeric form
-
0.0000259
TIMP-2
P45452
pH 7.5, 37C, monomeric form
-
0.0000361
TIMP-2
P45452
pH 7.5, 37C, dimeric form
-
additional information
additional information
-
detailed binding kinetics
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000045
(2E)-3-(N-hydroxycarbamoyl)-2-(3-phenylpropylidene)propionyl-L-tryptophan-N-methylamide
-
-
0.01
(2E)-3-(N-hydroxycarbamoyl)-2-heptylidenepropionyl-L-tryptophan-N-methylamide
-
above
0.000017
(2E)-3-(N-hydroxycarbamoyl)-2-isopropionyl-L-tryptophan-N-methylamide
-
-
0.000038
(2E)-3-(N-hydroxycarbamoyl)-2-[(2E)-3-phenylprop-2-en-1-ylidene]propionyl-L-tryptophan-N-methylamide
-
-
0.000974
(2E)-3-(N-hydroxycarbamoyl)-2-[(2E)-but-2-en-1-ylidene]propionyl-L-tryptophan-N-methylamide
-
-
0.0000005
(R)-2-(N-((6-fluoropyridin-3-yl)methyl)-4-methoxyphenyl-sulfonamido)-N-hydroxy-3-methylbutanamide
-
-
0.017
3',4',5,6,7,8-hexamethoxyflavone
-
TNF-alpha-treated cells, pH and temperature not specified in the publication
0.0209
3',4',5,6,7,8-hexamethoxyflavone
-
PMA-treated cells, pH and temperature not specified in the publication
0.0108
3',4'-dihydroxy-5,6,7,8-tetramethoxyflavone
-
TNF-alpha-treated cells, pH and temperature not specified in the publication
0.0123
3',4'-dihydroxy-5,6,7,8-tetramethoxyflavone
-
PMA-treated cells, pH and temperature not specified in the publication
0.0164
3'-hydroxy-4',5,6,7,8-pentamethoxyflavone
-
TNF-alpha-treated cells, pH and temperature not specified in the publication
0.0169
3'-hydroxy-4',5,6,7,8-pentamethoxyflavone
-
PMA-treated cells, pH and temperature not specified in the publication
0.0037
4'-hydroxy-3',5,6,7,8-pentamethoxyflavone
-
PMA-treated cells, pH and temperature not specified in the publication
0.0055
4'-hydroxy-3',5,6,7,8-pentamethoxyflavone
-
TNF-alpha-treated cells, pH and temperature not specified in the publication
0.000026
5-(1,5-dihydroxypentan-3-yl)-5-(4-phenoxyphenyl)pyrimidine-2,4,6(1H,3H,5H)-trione
-
pH 7.5, 37C
0.000145
5-(4-hydroxybutan-2-yl)-5-(4-phenoxyphenyl)pyrimidine-2,4,6(1H,3H,5H)-trione
-
pH 7.5, 37C
0.000104
5-(4-phenoxyphenyl)-5-(3-(1-nitrooxy-methyl)piperidin-1-yl)-pyrimidine-2,4,6(1H,3H,5H)-trione
-
pH 7.5, 37C
0.000152
5-(4-phenoxyphenyl)-5-(4-(1-nitrooxy-ethyl)piperidin-1-yl)-pyrimidine-2,4,6(1H,3H,5H)-trione
-
pH 7.5, 37C
0.000092
5-(4-phenoxyphenyl)-5-(4-(2-nitrooxy-ethyl)piperazin-1-yl)-pyrimidine-2,4,6(1H,3H,5H)-trione
-
pH 7.5, 37C
0.000202
5-(4-phenoxyphenyl)-5-(4-(2-nitrooxy-ethyl)piperidin-1-yl)-pyrimidine-2,4,6(1H,3H,5H)-trione
-
pH 7.5, 37C
0.000091
5-(4-phenoxyphenyl)-5-(bis-(2-nitrooxy-ethyl)-amino)pyrimidine-2,4,6(1H,3H,5H)-trione
-
pH 7.5, 37C
0.000048
5-(4-phenoxyphenyl)-5-(methyl-(2-nitrooxy-ethyl)-amino)-pyrimidine-2,4,6(1H,3H,5H)-trione
-
pH 7.5, 37C
0.0000062
5-[3-(hydroxymethyl)piperidin-1-yl]-5-(4-phenoxyphenyl)pyrimidine-2,4,6(1H,3H,5H)-trione
-
pH 7.5, 37C
0.0000081
5-[4-(2-hydroxyethyl)piperazin-1-yl]-5-(4-phenoxyphenyl)pyrimidine-2,4,6(1H,3H,5H)-trione
-
pH 7.5, 37C
0.000012
5-[4-(2-hydroxyethyl)piperidin-1-yl]-5-(4-phenoxyphenyl)pyrimidine-2,4,6(1H,3H,5H)-trione
-
pH 7.5, 37C
0.000097
5-[4-(hydroxymethyl)piperidin-1-yl]-5-(4-phenoxyphenyl)pyrimidine-2,4,6(1H,3H,5H)-trione
-
pH 7.5, 37C
0.000006
CGS 27023A
-
-
0.0000002
ilomastat
-
pH 7.4, 37C
0.0000005
ilomastat
-
-
additional information
additional information
-
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
-
additional information
-
MMP-9 activity in relaxin-treated and untreated renal artery, overview
additional information
-
coupled assay method using MMP-9 catalyzes activation of urokinase and susequent reaction of urokinase with the fluorogenic substrate S-2444 for spectrophotometric quantification, overview
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.8
-
assay at
7.4
-
assay at
7.4
-
assay at
7.5
-
assay at
7.6
-
assay at
8
-
assay at
8.3
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 37
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
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
Manually annotated by BRENDA team
Mus musculus C57BL/6
-
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
-
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
secretion, induced by interleukin-1beta
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
MMP-9 secretion
Manually annotated by BRENDA team
-
bone marrow-derived cells are the major source of MMP-9 in the ischemic brain
Manually annotated by BRENDA team
-
primary breast tumor cell
Manually annotated by BRENDA team
-
laryngeal in situ carcinoma
Manually annotated by BRENDA team
-
from femoral condyles in the knee
Manually annotated by BRENDA team
-
glial-neuronal coculture
Manually annotated by BRENDA team
-
articular chondrocyte of the late-stage osteoarthritis cartilage with surface fibrillation and chondrocyte clusters, not in healthy chondrocytes, overview
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
stage II/III rectal carcinoma, expression analysis, the MMP-9 expression is related to tumor growth, overview
Manually annotated by BRENDA team
-
purified from neutrophil granulocytes
Manually annotated by BRENDA team
-
recombinant pro-MMP-9
Manually annotated by BRENDA team
Mus musculus BALB/c
-
-
-
Manually annotated by BRENDA team
-
coronary arteritis is induced by Lactobacillus casei cell wall extract injection
Manually annotated by BRENDA team
-
contitioned culture medium
Manually annotated by BRENDA team
-
contitioned culture medium
Manually annotated by BRENDA team
-
from SC40-transformed cells, normal alveolar macrophages, phorbol ester-differentiated monocytic leukemia U937 cells, fibrosarcoma HT1080 cells, cultured keratinocytes
Manually annotated by BRENDA team
-
of rabbit synovial cell line HIG-82
Manually annotated by BRENDA team
-
demineralized dentin matrix, extraction is best at acidic conditions of pH 2-3 compared to pH 7.4-EDTA-containing extracts
Manually annotated by BRENDA team
-
colon adenocarcinoma cell line
Manually annotated by BRENDA team
-
MMP-9 is expressed at very low levels in endometrioid adenocarcinoma cells
Manually annotated by BRENDA team
-
increased MMP-9 levels
Manually annotated by BRENDA team
-
MMP-9 protein is localized at the leading-edge keratinocytes in front of the migrating epidermal layer
Manually annotated by BRENDA team
Trypanosoma cruzi Y
-
-
-
Manually annotated by BRENDA team
-
bleb tissue and fluid of glaucoma patients
Manually annotated by BRENDA team
-
enzyme protein is present in cells within granulomas and in scattered epitheloid cells
Manually annotated by BRENDA team
-
proteolytic activity and expression of gelatinase B in serum of gastric cancer patients and their correlation with the stage of the tumor
Manually annotated by BRENDA team
-
induced by ethanol
Manually annotated by BRENDA team
Mus musculus BALB/c
-
induced by ethanol
-
Manually annotated by BRENDA team
-
high expression level of MMP-9 increasing during growth
Manually annotated by BRENDA team
-
neutrophil, commercial preparation
Manually annotated by BRENDA team
-
colon adenocarcinoma cell line
Manually annotated by BRENDA team
-
enzyme activity and expression analysis, overview
Manually annotated by BRENDA team
-
leukemia cell line, secretion of MMP-9
Manually annotated by BRENDA team
-
a fibrosarcoma cell line
Manually annotated by BRENDA team
-
tumour cells developed in mice, high expression level
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
the level of MMP-9 activity in lens epithelial cells is highest in eyes with cortical cataract
Manually annotated by BRENDA team
-
unstimulated/resident and inflammatory, peritoneal leukocytes, constitutive expression
Manually annotated by BRENDA team
Mus musculus C57BL/6
-
unstimulated/resident and inflammatory, peritoneal leukocytes, constitutive expression
-
Manually annotated by BRENDA team
-
cirrhotic liver
Manually annotated by BRENDA team
Mus musculus BALB/c
-
-
-
Manually annotated by BRENDA team
-
increased MMP-9 activity and expression during ventilator-induced lung injury, overview
Manually annotated by BRENDA team
-
from surgical lobectomy for lung cancer
Manually annotated by BRENDA team
-
polymorphonuclear lymphocytes
Manually annotated by BRENDA team
-
activated, MMP-9 secretion
Manually annotated by BRENDA team
-
secretion of MMP-9 in the early phase of peritonitis, no MMP-9 production in unstimulated macrophages
Manually annotated by BRENDA team
-
secretion of MMP-9, transcription factor NF-kappaB is important in MMP gene regulation in macrophage cells
Manually annotated by BRENDA team
-
polymorphonuclear macrophages
Manually annotated by BRENDA team
-
macrophages contribute significantly to the elevated levels of MMP-9 in dystrophic muscle
Manually annotated by BRENDA team
-
macrophages derived from THP-1 cells
Manually annotated by BRENDA team
-
located within the granulation tissue
Manually annotated by BRENDA team
Mus musculus FVB/NJ
-
activated, MMP-9 secretion
-
Manually annotated by BRENDA team
Mus musculus C57BL/6
-
secretion of MMP-9 in the early phase of peritonitis, no MMP-9 production in unstimulated macrophages
-
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
secretion of MMP-9
Manually annotated by BRENDA team
Mus musculus C57BL/6
-
secretion of MMP-9
-
Manually annotated by BRENDA team
Mus musculus BALB/c
-
-
-
Manually annotated by BRENDA team
-
cell expression system
Manually annotated by BRENDA team
-
polymorphonuclear neutrophils
Manually annotated by BRENDA team
-
MMP-9 secretion
Manually annotated by BRENDA team
-
secretion of MMP-9, high MMP-9 expression in the early phase and especially in the late phase of peritonitis
Manually annotated by BRENDA team
Mus musculus FVB/NJ
-
MMP-9 secretion
-
Manually annotated by BRENDA team
Mus musculus C57BL/6
-
secretion of MMP-9, high MMP-9 expression in the early phase and especially in the late phase of peritonitis
-
Manually annotated by BRENDA team
-
atrophic acnd nonatrophic oral lichen planus
Manually annotated by BRENDA team
Mus musculus C57BL/6
-
-
-
Manually annotated by BRENDA team
Mus musculus C57BL/6
-
-
-
Manually annotated by BRENDA team
-
periapical ligament
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
Mus musculus BALB/c
-
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
-
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
no association between plasma MMP-9 activity and the concentrations of lead in whole blood or plasma, overview
Manually annotated by BRENDA team
Mus musculus BALB/c
-
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
-
Manually annotated by BRENDA team
-
primary bronchial epithelial cell
Manually annotated by BRENDA team
Mus musculus BALB/c
-
-
-
Manually annotated by BRENDA team
-
immunohistochemic analysis
Manually annotated by BRENDA team
-
MMP-9 is expressed at very low levels in serous cystoadenocarcinoma cells
Manually annotated by BRENDA team
-
transfected with a construct expressing enzyme. Enzyme overexpressing cells show a significantly reduced collagen gel contraction
Manually annotated by BRENDA team
-
gastric mucosa
Manually annotated by BRENDA team
Mus musculus BALB/c
-
gastric mucosa
-
Manually annotated by BRENDA team
Mus musculus C57BL/6
-
-
-
Manually annotated by BRENDA team
-
stromal cells are the major source of MMP-9
Manually annotated by BRENDA team
-
colon adenocarcinoma cell line
Manually annotated by BRENDA team
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, 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
Manually annotated by BRENDA team
additional information
-
MMP-9 co-localizes with macrophages and neutrophils in gastritic stomach, overview
Manually annotated by BRENDA team
additional information
-
MMP-9 expression analysis in peritonitis, overview
Manually annotated by BRENDA team
additional information
-
MMP-9 is increased in tumor cells, no expression in healthy/untreated brain tissue, brain expression analysis after implantation of 9L glioma cells, overview
Manually annotated by BRENDA team
additional information
-
MMP-9 is not expressed in mucinous and clear cell adenocarcinoma cells
Manually annotated by BRENDA team
additional information
-
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
Manually annotated by BRENDA team
additional information
-
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
Manually annotated by BRENDA team
additional information
-
MMP-9 levels are increased in acute pancreatitis
Manually annotated by BRENDA team
additional information
Mus musculus C57BL/6
-
MMP-9 levels are increased in acute pancreatitis, MMP-9 co-localizes with macrophages and neutrophils in gastritic stomach, overview, MMP-9 expression analysis in peritonitis, overview
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Trypanosoma cruzi Y
-
-
-
Manually annotated by BRENDA team
-
the enzyme is secreted
-
Manually annotated by BRENDA team
-
the enzyme is secreted
-
Manually annotated by BRENDA team
-
the enzyme is secreted
-
Manually annotated by BRENDA team
-
MMP-9 is secreted
-
Manually annotated by BRENDA team
-
secreted enzyme
-
Manually annotated by BRENDA team
-
secreted enzyme
-
Manually annotated by BRENDA team
-
secretion of MMP-9
-
Manually annotated by BRENDA team
-
blood plasma
-
Manually annotated by BRENDA team
Mus musculus BALB/c
-
MMP-9 is secreted
-
-
Manually annotated by BRENDA team
Mus musculus C57BL/6
-
secreted enzyme, secretion
-
-
Manually annotated by BRENDA team
additional information
-
secretion of proMMP-9 from the amniochorion after application of lipopolysacchride to either sidesof the membrane is increased, overview
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
707123
66000
-
active form of MMP-9, SDS-PAGE
709920
67000
-
active form of MMP-9, SDS-PAGE
698353
72000
-
active form of MMP-9, SDS-PAGE
709413
78000
-
active form of MMP-9, SDS-PAGE
707452
82000
-
active enzyme, gelatin zymography
701422
82000
-
active enzyme
707123
82000
-
activated form of MMP-9, SDS-PAGE
707953
84000
-
MMP-9 active enzyme, SDS-PAGE
699222
85000
-
85000 Da polypeptide in both cellular and secreted parasite extracts, activated form of MMP-9, SDS-PAGE
708445
87000
-
active form of MMP-9
700477
88000
-
activated enzyme
708245
88000
-
active form of MMP-9, SDS-PAGE
710067
92000
-
human SC40-transformed lung cells, gel filtration, glycosylated proenzyme can be activated by organomercurials by removal of 73 amino acids
31212
92000
-
-
651499
92000
P45452
monomeric form, SDS-PAGE
652033
92000
-
SDS-PAGE
653711, 696965
92000
-
-
696980
92000
-
MMP-9 proenzyme, SDS-PAGE
699222
92000
-
SDS-PAGE
699345
92000
-
SDS-PAGE
699716
92000
-
SDS-PAGE
699939
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
700477
92000
-
proenzyme MMP-9
700530
92000
-
proenzyme, gelatin zymography
701422
92000
-
SDS-PAGE
702513
92000
-
pro-form of MMP-9, SDS-PAGE
707452
92000
-
SDS-PAGE
707631
92000
-
inactive form of MMP-9, SDS-PAGE
707953
92000
-
inactive pro-MMP-9, SDS-PAGE
707964
92000
-
inactive enzyme form
708245
92000
-
SDS-PAGE
708775, 709301
92000
-
inactive form of MMP-9, SDS-PAGE
709413
92000
-
activated MMP-9, SDS-PAGE
710575
92000
-
pro-MMP-9, SDS-PAGE
710602
92000
-
SDS-PAGE
710695
94000
-
-
700527
94000
-
pro-MMP9, SDS-PAGE
709920
95000
-
proMMP-9, SDS-PAGE
710575
96000
-
proMMP-9, SDS-PAGE
710067
97000
-
active enzyme form, gelatin gel zymography
696037
97000
-
97000 Da protein band in cellular extract, SDS-PAGE
708445
97000
-
active form of MMP-9, SDS-PAGE
709650
97000
-
SDS-PAGE
710065
100000
-
SDS-PAGE
707928
104000
-
gel filtration
707062
105000
-
the molecular mass of recombinant MMP-9 is approximately 105000 Da, SDS-PAGE
709680
130000
-
-
651499
135000
-
neutrophil gelatinase-associated lipocalin-MMP-9 complex, SDS-PAGE
710575
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
700477
200000
-
the molecular weight of proMMP-9 is about 200000 Da, SDS-PAGE
709051
210000
P45452
dimeric form, SDS-PAGE
652033
220000
-
native PAGE
684107
225000
-
-
651499
225000
P45452
Western blot
652033
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 70795, calculated, enzyme mutant E402A, x * 20947, calculated, isolated enzyme collagen-binding domain
?
-
x * 103000, about, pro-MMP9, SDS-PAGE, x * 86000, about, activated MMP-9, SDS-PAGE
?
-
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 * 92000, pro-MMP-9, SDS-PAGE, x * 84000, activated MMP-9, SDS-PAGE
?
-
x * 92000, pro-MMP-9, SDS-PAGE, x * 86000, activated 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, 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 * 92000
dimer
P45452
-
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, 2 * 92000, proMMP-9, SDS-PAGE
monomer
P45452
-
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
-
molecular modeling of the three-dimensional structure of the MMP-9/TIMP-1 complex, 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
-
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
Mus musculus BALB/c
-
molecular modeling of the three-dimensional structure of the MMP-9/TIMP-1 complex, overview
-
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
-
-
glycoprotein
-
MMP-9 contains a heavily O-glycosylated OG domain
proteolytic modification
-
4-aminophenylmercuric acetate proteolytically activates the enzyme
proteolytic modification
-
activation by trypsin, MMP3, and MMP10, kinetics, overview
proteolytic modification
-
MMP-3 and hemin activate MMP-9 cleaving at Glu40-Met41 and Arg87-Phe88, and at Glu40-Met41 and Leu52-Leu53, respectively, overview
proteolytic modification
-
the inactive zymogen is cleaved at the pro-peptide and activated to the mature MMP-9
proteolytic modification
-
acrolein stimulates pro-MMP-9 cleavage and activation
proteolytic modification
-
activation
proteolytic modification
-
activation of MMP-9
glycoprotein
-
the enzyme is O-glycosylated at Trp116-Lys214 sequence of the C-terminal part
additional information
-
activation of pro-MMP-2 by 4-aminophenylmercuric acetate
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, stored in 50% glycerol, complete retention of activity forat least 1 month
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
catalytic domain of mutated enzyme
-
gelatin Sepharose 4B bead chromatography
-
gelatin-Sepharose column chromatography
-
native MMP-9 from dentin inculding serial dilutions, method development
-
recombinant enzyme
-
recombinant full-length pro-MMP-9 from Spodoptera frugiperda Sf9 cells
-
recombinant full-length proMMP-9 and mutant enzymes from Spodoptera frugiperda Sf9 insect cells
-
recombinant MMP-9 from Spodoptera frugiperda Sf9 cells
-
SC40-transformed cells
-
native MMP-9 from gastric mucosa
-
recombinant activated MMP-9 dimers by gelatin affnity chromatography
-
recombinant enzyme
-
recombinant secreted mutant enzymes from Hep-G2 cells by gelatin affinity chromatography to homogeneity
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cDNA of the mutated enzyme used to transfect HEK 293 cells
-
expressed in baculovirus-infected Spodoptera frugiperda IPLB-Sf21 AE cells
-
expressed in CT-26 cells
-
expressed in immortalized keratinocytes, transduced by lentivrus
-
expression in H9C2 cell
-
expression of full-length pro-MMP-9 in Spodoptera frugiperda Sf9 cells
-
expression of full-length proMMP-9 and of mutant enzymes in Spodoptera frugiperda Sf9 insect cells using the baculovirus infection system
-
expression of MMP-9 in Spodoptera frugiperda Sf9 cells
-
expresssion of wild-type MMP-9 and truncated versions in insect cells
-
cDNA encoding the catalytic domain cloned into pCDNA3 and used to transfect HEK 293 cells
-
expressed in A549-C and A549-FI cells
-
expression of mutant enzymes in Hep-G2 cells using recombinant adenoviral vectors adenovirus-2 or adenovirus-5, secretion of the recombinant enzymes, overview
-
expression of wild-type full-length MMP-9 and of a mutant version lacking the O-glycosylated linker region and hemopexin domains in Drosophila melanogaster S2 cells using the Drosophila metallothionein promoter, the native MMP-9 signal peptide is utilized for secretion contained in the beginning of the sequences
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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
-
MMP-9 protein activity is decreased in the media samples of cells from large-healthy follicles compared with those from medium-healthy follicles
-
there is no difference in expression of MMP-9 for any follicle size or health status class
-
0.025 mM panduratin A markedly down-regulates MMP-9 expression
-
12-O-tetradecanoyl phorbol-13-acetate-induced MMP-9 expression is decreased by 324.8% by 0.1 mM silibinin
-
20 mg doxycycline decreases MMP-9 levels after 1 month, 20 mg doxycycline decreases endometrial MMP-9 at 1 and 6 months compared to baseline
-
active treatment with uric acid (0.5 or 1.0 mg) is associated with reduced levels of active MMP-9 at the end of infusion
-
after 24 h incubation, 0.05 mg/ml aspirin inhibits MMP-9 mRNA expression by 50%. MMP-9 mRNA expression and release are inhibited by fenofibrate (0.1 mM) and 15d-prostaglandin J2 (0.005 mM)
-
aqueous extract isolated from Prunella vulgaris suppresses 12-phorbol 13-myristate acetate-enhanced expression of MMP-9 protein, mRNA and transcription activity levels through suppression of nuclear factor-kappaB activation
-
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
-
diet-induced long-term weight loss decreases MMP-9
-
immune cell secretion of MMP-9 decreases by 58% after 3 months of omega-3 fatty acid supplementation when compared with baseline levels in patients with relapsing-remitting multiple sclerosis
-
in sections of ectopic tumors treated with Dz13, MMP-9 is downregulated
-
in the human vascular endothelium, simvastatin and atorvastatin (0.0001-0.01 mM) reduce MMP-9 expression and activity
-
induction of MMP-9 expression and activity is significantly inhibited by 0.001 mM of the specific cPLA2alpha inhibitor
-
interferon-gamma suppresses MMP-9 expression
-
leucine-zipper and sterile-alpha motif kinase reduces MMP-9 activity by increasing TIMP-1/2 expression in H9c2 cardiomyoblast cells
-
MMP-9 protein and mRNA levels are decreased up to 43% after treatment with 0.025 mM panduratin A
-
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
-
non-surgical periodontal therapy decreases blood plasma MMP-9 concentration by 39%
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
treatment with 0.05 mM glycitein downregulates MMP-9 gene expression and inhibits the phorbol myristate acetate-induced MMP-9 secretion in U87MGcells
-
TX-1877 significantly inhibits expression of MMP-9
-
vitamin D3 significantly reduces the MMP-9 level in antigen stimulated and unstimulated cultures of pulmonary tuberculosis as compared to healthy controls
-
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
-
there is no MMP-9 mRNA elevation in mononuclear cells
-
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
-
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
-
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
-
10% (v/v) Porphyromonas gingivalis supernatant induces about 2.5fold increased MMP-9 expression in human oral epidermoid cells
-
a significant increase in MMP-9 is observed in pulmonary tuberculosis patients as compared to healthy controls
-
A3 receptor stimulation induces an increase of MMP-9 protein levels in cellular extracts of U87MG cells by phosphorylation of extracellular signal-regulated protein kinases, c-Jun N-terminal kinase/stress-activated protein kinase, protein kinase B, and activator protein 1. A3 receptor activation stimulates also an increase of extracellular MMP-9 in the supernatants from U87MG glioblastoma cells
-
C-reactive protein increases the expression and activity of MMP-9 in a dose-dependent manner in human THP-1 cells
-
circulating MMP-9 concentrations are higher in patients with abdominal aortic aneurysm than those in subjects without abdominal aortic aneurysm
-
Dz13 upregulates the matrix metalloproteinase-9 in cultured tumor cells
-
epidermal growth factor contributes to prostate cancer metastasis through stimulating MMP-9 secretion from prostate cancer cells
-
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
-
heregulin-beta1 stimulates MMP-9 secretion and activation via a transcriptional regulation in human breast cancer cells
-
higher plasma MMP-9 concentrations are found in periodontal disease patients compared with healthy controls
-
homocysteine increases mRNA expression of MMP-9
-
interleukin 1beta, interleukin-6, and tumor necrosis factor -alpha stimulate MMP-9 expression
-
levonorgestrel subcutaneous implant increases serum MMP-9 levels after 1 month
-
matrix metalloproteinase-9 is significantly increased after 8 weeks of very low energy diet-induced weight loss
-
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
-
MMP-9 is significantly increased in the infarcted tissue compared to the contralateral hemisphere after ischemic stroke
-
MMP-9 mRNA expression and release are induced by 0.002 mM prostaglandin E2
-
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
-
obese individuals show increased activity of MMP-9/LCN2 complex, while a positive correlation between MMP-9 activity and body mass index is observed
-
serum MMP-9 concentrations are significantly higher in patients with non-herpetic acute limbic encephalitis in acute and convalescent stages than in control patients
-
Skp2 overexpression increases the expression of MMP-9, Sp1 is involved in the induction of MMP-9 by Skp2
-
tear MMP-9 activity is significantly higher in patients with dysfunctional tear syndrome, this activity is associated with increased mRNA expression of MMP-9
-
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
-
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
-
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
-
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
-
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
-
the serum MMP-9 level is significantly higher in moyamoya disease than in healthy controls
-
there is a highly significant relationship between the expression of MMP-9 and macrophage count in eosinophilic granulomas
-
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
-
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
-
50 mg/kg (-)-epigallocatechin gallate administration significantly inhibits the induction of the active form of MMP-9
-
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
-
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)
-
in vivo administration of a nuclear factor-kappa B inhibitory peptide blocks the expression of MMP-9 in dystrophic muscle of mdx mice
-
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
-
myricetin, i.e. 3,3',4',5,5',7-hexahydroxyflavone, suppresses UVB-induced MMP-9 expression through the suppression of Raf kinase activity
-
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
-
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
-
total Panax notoginsenosides downregulate expression of MMP-9 apolipoprotein E-knockout mice
-
peroxisome proliferators-activated receptor gamma antagonist GW9662 has little effect on MMP-9 expression
-
acrolein exposure induces MMP-9 expression at both protein and mRNA levels in the lung tissue
-
activation of phosphatidylinositol 3-kinase is required for tumor necrosis factor-alpha-induced upregulation of matrix metalloproteinase-9. Red wine extrac and quercetin inhibit significantly the tumor necrosis factor-alpha-induced upregulation of MMP-9 whereas resveratrol does not have significant inhibitory effects
-
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
-
mild nonischemic cerebral venous hypertension results in increased MMP-9 activity. MMP-9 activity increases 10fold 1 day after surgery, gradually decreases afterwards, and returns to baseline 2 weeks after surgery
-
MMP-9 expression and activity significantly increase on day 3 after status epilepticus after pilocarpine injection
-
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
-
MMP-9 mRNA expression is induced by interleukin 17, at 200 ng/ml the mRNA level increases about 17times compared with the untreated group
-
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
-
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
Q2M4J5
the gelatinolytic activity of MMP-9 is constitutively activated in Lewis lung carcinoma cells
-
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
-
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
-
there is an increase in the active form of MMP-9 after ischemia
-
auto-amplified NFATc1 plays a key role in upregulating MMP-9
-
auto-amplified NFATc1 plays a key role in upregulating MMP-9
Mus musculus BALB/c
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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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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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normobaric hyperoxia inhibits MMP-9-mediated occludin degradation in the ischemic hemispheric microvessels
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the broad-spectrum matrix metalloproteinase inhibitor doxycycline reduces pulmonary expression of active MMP-9
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F(ab')2 fragments or stimulation with lipopolysaccharide have no effect on MMP-9 production
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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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expression of MMP9 protein and mRNA increases in rat brain tissue after cardiopulmonary resuscitation
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ischemia and reperfusion induce an upregulation of MMP-9 in the ischemic hemispheric microvessels
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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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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 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 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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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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orthodontic pressure induces gene transcription MMP-9 in pressure gingival soft tissue
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polyclonal immunoglobulins (IVIg) induce expression of MMP-9 in microglia
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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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there are significant increases in MMP-9 protein expression and enzyme activity 7 h after thermal injury
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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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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E402A
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no enzymic activity, competition with isolated collagen-binding domain and with matrix metalloproteinase MMP-2 binding to native and denatured type I collagen
E402A
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site-directed mutagenesis of the catalytic Glu402 results in an inactive enzyme
P574R
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the mutant is associated with a non-significant decreased risk of coronary artery disease when compared with the wild type genotype
R279Q
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the mutant is associated with a non-significant decreased risk of coronary artery disease when compared with the wild type genotype
R279Q
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there is no relationship between R279Q polymorphism and atrial fibrillation hypertensive heart disease patients of Chinese Han population
R668Q
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the mutant is associated with a non-significant decreased risk of coronary artery disease when compared with the wild type genotype
E402H/H411E
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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
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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
Mus musculus BALB/c
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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
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E402Q
Mus musculus BALB/c
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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
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E402A
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inactive
E412D
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site-directed mutagenesis
additional information
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recombinant enzyme collagen-binding domain, competition with binding to gelatin of either enzyme mutant E402A or matrix metalloproteinase MMP-2 mutant E404A
additional information
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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
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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
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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
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the -1562CNT polymorphism of MMP-9 gene is significantly associated with atrial fibrillation risk in Chinese Han patients with hypertensive heart disease
additional information
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the functional-1562C/T polymorphism is associated with schizophrenia
additional information
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variant genotypes -1562 CT/TT, 279 RQ/QQ, 574 PR/RR and 668 RQ/QQ have a 51% decreased risk of coronary artery disease
H401A
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site-directed mutagenesis, proteolytic inactive MMP-9 mutant, application of the MMP-9 mutant decreases portal and periportal accumulation of collagen and inhibits fibrogenesis induced by CCl4 in mice, the MMP-9 mutant suppresses transdifferentiation of hepatic stellate cells to the myofibroblast-like phenotype in vitro and in vivo. Adenoviral application of the mutant leads to increased apoptosis of activated hepatic stellate cells
additional information
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enzyme-deficient MPP-9-/- mice show impaired neutrophil infiltration during zymosan peritonitis, overview
additional information
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MMP-9 deprived mice show impaired polymorphonuclear leukocyte infiltration at infalmmation sites, overview
additional information
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MMP-9 knockout mice show delayed inflammatory response and macrophage infiltration in gastritis
additional information
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MMP-9 mutants reduce type I collagen protein, TIMP-1, and MMP-2 expression in vivo, overview
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
additional information
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MMP-9-deficient mice show eliminated elastin breakdown in coronary artery in the Kawasaki disease
additional information
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generation of a mutant version lacking the O-glycosylated linker region and hemopexin domains and containing only the protease domain, residues 1-447
H401A
Mus musculus BALB/c
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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
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additional information
Mus musculus BALB/c
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MMP-9 mutants reduce type I collagen protein, TIMP-1, and MMP-2 expression in vivo, overview, MMP-9 deprived mice show impaired polymorphonuclear leukocyte infiltration at infalmmation sites, overview
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additional information
Mus musculus C57BL/6
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MMP-9 knockout mice show delayed inflammatory response and macrophage infiltration in gastritis, enzyme-deficient MPP-9-/- mice show impaired neutrophil infiltration during zymosan peritonitis, overview
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additional information
Mus musculus FVB/NJ
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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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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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circulating concentrations of MMP-9 may be a marker helping in the diagnosis and prognosis of cardiovascular and neoplastic diseases
diagnostics
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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
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MMP-9 levels are useful in endometriosis diagnostics
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
medicine
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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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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
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enzyme is present in extracts from leaking bleb tissue of glaucoma patients, but not in bleb leak fluid or aqueous humor samples
medicine
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enzyme levels are significantly elevated in cerebrospinal fluid of patients with vascular dementia compared to those with Alzheimer disease and to control
medicine
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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
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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
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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
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incubation of lenses with enzyme leads immediately to cataract
medicine
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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
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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
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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
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a positive correlation between MMP-9 values and gestational age is observed in normal pregnant women
medicine
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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
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higher levels of MMP-9 mRNA expression in the apical periodontitis when compared to healthy periapical ligaments, suggest that MMP-9 can be directly involved in tissue remodeling/destruction during lesion development
medicine
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matrix metalloproteinase is an independent predictor of the reduced nitrate-mediated dilatation in the type 1 diabetes mellitus
medicine
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matrix metalloproteinase-9 is an independent prognostic marker in laryngeal and hypopharyngeal cancer
medicine
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MMP-9 expression positively correlates with prognosis of oral squamous cell carcinoma
medicine
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MMP-9 genotype polymorphisms are primary predictors for oral squamous cell carcinoma risk
medicine
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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
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serum MMP-9 level is related to FEV1 decline
medicine
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the expression of the mRNA of MMP-9 is not significantly elevated with the progression of biliary-associated liver fibrosis
medicine
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the functional polymorphism C1562T in the promoter of matrix metalloproteinase-9 gene is associated with susceptibility to knee osteoarthritis in the Turkish population
medicine
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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
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controlling MMP-9 expression has therapeutic potential in Parkinson's disease
medicine
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down-regulation of the expression and activity of MMP-9 is a treatment alternative for plaque stabilization by inhibiting the nuclear factor-kappaB activation
medicine
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higher circulating MMP-9 concentrations are associated with abdominal aortic aneurysm presence
medicine
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imbalance between total MMP-9 and TIMP-1 may contribute to the pathogenesis of lupus nephritis
medicine
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MMP-9 is a nontraditional cardiovascular risk factor
medicine
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MMP-9 is a potential target for cerebral ischemic treatment in human stroke therapy
medicine
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MMP-9 is a potential therapeutic target for gastric adenocarcinomas
medicine
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MMP-9 is a potentially useful biomarker for diagnosing, classifying, and monitoring dysfunctional tear syndrome
medicine
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MMP-9 overexpression is an early marker of breast carcinogenesis preceding tumor invasion
medicine
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MMP-9 plasma levels are predictive of cognitive performance following carotid endarterectomy
medicine
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pretreatment serum levels of MMP-9 are powerful prognostic markers in patients with oral squamous cell carcinoma, patients with MMP-9 serum levels higher than median have significantly shorter overall survival than those with levels lower than median
medicine
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the serum levels of MMP-9 significantly correlate with the occurrence and severity of acute graft-versus-host disease
medicine
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MMP-9 induces TGF-beta1 production in the airway epithelium through the cleavage of EGF and EGF-like ligands and activating EGFR, suggesting potential targets of therapeutic intervention in airway fibrotic disorders
drug development
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MMP-9 is an attractive target for therapeutic intervention studies in mouse models
medicine
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MMP-9 is suggested as a regulator of the angiogenic switch in tumor development
medicine
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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
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MMP-9 is a marker of endothelial activation and dysfunction
medicine
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the reduction of MMP-9 activity may have a possible therapeutic effect for the management of brain injury after focal ischemia
medicine
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MMP-9 is a promising target for a neuroprotective approach to preventing seizure-induced hippocampal damage
medicine
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pharmacological inhibition of MMP-9 activity ameliorates skeletal muscle pathogenesis and enhanced myofiber regeneration in mdx mice. MMP-9 represents as one of the most promising therapeutic targets for the prevention of disease progression in Duchenne muscular dystrophy
medicine
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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