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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In accordance with previous quantitative studies, we detected for the first time on zymography that fibroblast-derived MMP-2 did not differ in serum and heparin plasma but was lower in EDTA plasma, whereas the activities of all neutrophil-derived MMP-9 isoforms were 2- to 10-fold higher in serum than in heparin and EDTA plasma (Fig.
Therefore, we investigated the expression of MMP-2 (gelatinase A; 72-kDa type IV collagenase), MMP-9 (gelatinase B; 92-kDa type IV collagenase), TIMP-1, and TIMP-2 in circulating peripheral blood cells and compared this expression to the circulating concentrations of protease and inhibitor protein.
We have continued our investigations concerning MMP-2, MMP-9, and TIMP-2 because commercial ELISA assays are only now available.
21) reported expression of MMP-1, MMP-2, MMP-3, MMP-9, TIMP-1 and TIMP-2 on both synovial (lining) and subsynovial (sublining) layers.
We conclude that the most important role that MMP-2 plays in polyp growth may be in terms of perivascular localization and an increase in vascular permeability, which causes inflammatory cell migration and edema in the extracellular matrix.
SalA showed selectivity on gelatinase (MMP-2 and MMP-9) than on collagenase (MMP-8 and MMP-13) in vitro, and specificity on MMP-9 than MMP-2 in vivo.
MMP-9 and MMP-2 are the two most studied MMPs, and the two most frequently expressed MMPs in the nervous system (10).
It is believed that a very important function of MMP-2 and MMP-9 is in cell remodeling processes in the male and female reproductive system (Woessner, 1994; Hulboy et al.
In our study, we aimed to test whether there would be an increase in MMP-2 levels by NB-UVB treatment.
Two MMPs in particular, MMP-2 and MMP-9, are thought to accelerate wrinkling by degrading the outer components of cells.
DIFFERENTIAL LOCALIZATION OF MMP-2 ISOFORMS IN AUTOIMMUNE THYROID TISSUE.