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2,3,7,8-tetrachlorodibenzo-p-dioxin
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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
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pro-MMP-9 is activated with 1 mM 4-amino phenylmercuric acetate in assay buffer at 37°C for 1.5 h
4-aminophenylmercuric acetate
acrolein
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activates MMP-9 via EGFR/MAPK signaling and stimulation of pro-MMP-9 cleavage
aminophenylmercuric acetate
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cathepsin G
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MMP9 is released in an inactive form and requires proteolytic activation, cathepsin G mediates activation of pro-matrix metalloproteinase 9
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chymase
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chymase converts promatrix metalloproteinase-9 to matrix metalloproteinase-9
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fibronectin
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fibronectin enhances, in a PKC-dependent manner, the net activity of MMP-9, but not its expression
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homocysteine
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homocysteine activates matrix metalloproteinase-9, muscimol ameliorates the homocysteine-mediated MMP-9 activation
lipopolysaccharide
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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
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converts inactive pro-MMP-9 to active MMP-9
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matrix metalloproteinase-7
MMP-9 is activated by matrix metalloproteinase-7
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phorbol 12-myristate 13-acetate
platelet-activating factor
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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
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4-aminophenylmercuric acetate
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4-aminophenylmercuric acetate
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proteolytically activates the enzyme
4-aminophenylmercuric acetate
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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
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artificial activation of the inactive zymogen
4-aminophenylmercuric acetate
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1 mM
4-aminophenylmercuric acetate
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activation of pro-MMP-9 constructs at pH 7.0
4-aminophenylmercuric acetate
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1 mM 4-aminophenylmercuric acetate-mediated activation of MMP-9 provokes autocatalytic cleavage of recombinant MMP-9
4-aminophenylmercuric acetate
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after treatment with 4-aminophenylmercuric acetate, affinity-purified W-256 cell gelatinase is converted to a final processed form of 66000 Da
phorbol 12-myristate 13-acetate
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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
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30 nM 12-phorbol 13-myristate acetate is used to activate MMP-9, aqueous extract isolated from Prunella vulgaris reduces 12-phorbol 13-myristate acetate-induced activation of MMP-9
phorbol 12-myristate 13-acetate
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30 nM 12-phorbol 13-myristate acetate is used to activate MMP-9, aqueous extract isolated from Prunella vulgaris reduces 12-phorbol 13-myristate acetate-induced activation of MMP-9
tumor necrosis factor-alpha
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tumor necrosis factor-alpha
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additional information
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binding of the zymogen to fetuin or asialofetuin results in activation
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additional information
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activation by trypsin, MMP3, and MMP10, computational model of MMP9 activation and inhibition, overview
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additional information
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activation of pro-MMP-9 by 4-aminophenylmercuric acetate
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additional information
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beta-hematin, and not hemin, accelerates the activation of MMP-9, activation of MMP-9 by hemin and MMP-3, overview
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additional information
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relaxin induces enzyme expression in THP-1 cells, while it reduces expression of NF-kappaB inhibitor protein, IkappaB-alpha, overview
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additional information
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0.001-0.04 mM arachidonic acid increases matrix metalloproteinase 9 secretion and expression at the mRNA level
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additional information
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activator protein-4 expression may play an important role in the induction of synthesis of MMP-9
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additional information
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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
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additional information
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dermal fibroblasts and hepatic stellate cells require type-I collagen which boosts Jun N-terminal kinase activity to maximally induce MMP-9
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additional information
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eicosapentaenoic acid, docosapentaenoic acid or docosahexaenoic acid by themselves have no effect on MMP-9 secretion
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additional information
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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
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additional information
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MMP-9 expression is increased after a 16 h acetaldehyde treatment (0.1 mM)
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additional information
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MMP-9 is activated by a whole-cell extract from Prevotella nigrescens ATCC 33563
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additional information
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Notch1 may be involved in MMP9 activation either by enhancing its expression or by stabilizing the protein
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additional information
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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
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additional information
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the MMP-9 mRNA expression is inducible by vascular endothelial growth factor
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additional information
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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
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additional information
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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
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additional information
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the presence of an intact active site and hemopexin domain are required for full angiogenesis-inducing activity of the MMP-9 enzyme
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additional information
enzyme MMP-9 is released in the inactive form as proenzyme and can be secreted in physical association with its specific tissue inhibitor (TIMP-1) as proMMP-9/TIMP-1 complex or as TIMP-1 free protein. Activation of MMP-9 requires a complex network of mechanisms involving other matrix metalloproteases
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additional information
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8-bromo-cGMP yields increases in active MMP-9
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additional information
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gastric gelatinase B is rapidly increased in Helicobacter felis-induced gastritis
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additional information
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MMP-9 is upregulated by tumor necrosis factor alpha, TNFalpha
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additional information
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pulmonary infection with the Gram-negative intracellular bacterium Francisella tularensis, a category A biological threat agent, induces MMP-9 expression
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additional information
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ectopic Fra-1 markedly stimulates MMP-9 mRNA expression
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additional information
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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
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additional information
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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
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additional information
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implantation of 9L glioma cells into brain increases the expression of MMP-9, overview
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additional information
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interleukin-1beta induces MMP-9 activity
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additional information
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MMP-9 is induced in small renal arteries by recombinant human relaxin, up-regulation of 70%
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additional information
an increase in hypoxia-inducible factor-1alpha is followed by a significant increase in MMP-9 gene expression at 4 h at 24 h post-traumatic brain injury, traumatic brain injury increases MMP-9 mRNA and protein levels in cortical and hippocampal regions early at 4 h post-traumatic brain injury, persisting for 5 days
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additional information
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benzo[a]pyrene increases the mRNA level of matrix metalloproteinase 9
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additional information
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high glucose (25 mM) induces expression of MMP-9
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additional information
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tissue kallikrein is a potent activator of latent proenzyme
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