gelatinase

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gelatinase

[′jel·ə·tə‚nās]
(biochemistry)
An enzyme, found in some yeasts and molds, that liquefies gelatin.
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on MMP-7, -8 and -9 in oral and cutaneous squamous cell cancers showed MMP-7 expression to be elevated at the invasion front and MMP-9 mildly expressed.
The membranes were incubated with primary antibodies (anti-GPNMB 1:2000 dilution, R&D Systems, USA; anti-MMP-2, MMP-9 1:1000 dilution, Abcam; anti-[beta]-catenin 1:1000 dilution, Santa Cruz, USA; mouse anti-[beta]-actin and LaminB1, 1:2000 dilution, Abcam, UK) at 4[degrees]C overnight, followed by treatment with secondary antibodies for 1 h at room temperature.
Research showed that test mice, vaccinated with peptides containing specific sequences from MMP-2 and MMP-9 and subsequently challenged with melanoma cancer cells, had an average reduction in tumour volume by about 76% compared to unvaccinated controls.
MMP-2 and MMP-9 are members of gelatinase group and are able to degrade gelatin and collagen (2).
There is a higher prevalence of studies on MMP-2 and MMP-9. In 1998, Gohji et al.
Several studies have shown that high MMP-9 levels have a significantly deleterious effect on diabetic foot ulcer healing even though the mechanism of the increase is still uncertain [6-10].
Depending on the substrate specificity and structure, MMPs are divided into several subgroups: collagenases (e.g., MMP-1), gelatinases (e.g., MMP-2 and MMP-9), stromelysins (e.g., MMP-3 and MMP-10), matrilysins (e.g., MMP-7 and MMP-26), and membrane-type matrix metalloproteinase-1 (MT1-MMP).
Matrix metalloproteinase-9 (MMP-9), a zinc-dependent proteinase, is released by various inflammatory cells, predominantly neutrophils and macrophages.
As previously demonstrated, cross-linked collagen type I and type IV can resist cleavage by MMP-1, MMP-2, MMP-9, MMP-13, and noncross-linked collagen type I and type IV.
Recently, it was found that the changes of MMP-9 levels in the excitatory synapse and morphology of the dendritic spine could be involved in the pathophysiology of schizophrenia [9].
MMP-9 is a zinc-dependent enzyme involved in tissue remodeling which includes degradation of extracellular matrix components, as well as the processing of non-matrix substrates (4).