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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We investigated the differences of MMP-2 expression between LV and RV in response to nandrolone decanoate (ND), swimming training (ST), and combined ND and ST (NS) in mice, based on their structural, functional, and biochemical characteristics.
Second group comprises gelatinases: MMP-2 (gelatinase A) and MMP-9 (gelatinase B).
The levels of latent and active MMP-2 did not show significant change until 12 weeks after Ovx.
Among all MMPs, MMP-9 and MMP-2 have been extensively studied in MS given their ability to degrade the components of the basal lamina and to mediate BBB damage [6-8].
MMP-2 and MT1-MMP (MMP-14) are present in normal condition in latent or proforms in both human and experimental animals [7].
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.
Findings showed that full length soluble CD147 was found in the culture medium of HCC cells and serum of patients with HCC, as well as that the extracellular domain of soluble CD147 stimulated the expression of CD147 and MMP-2 from HCC cells.
Se incluyen en ese grupo la MMP-2 (gelatinasa A) y la MMP-9 (gelatinasa B) (30).
MMP-9 and MMP-2 are the two most studied MMPs, and the two most frequently expressed MMPs in the nervous system (10).
The matrix metalloproteinases (MMP) are proteolytic enzymes involved in tumor invasion (QUARANTA, 2000) and the expression of MMP-2 (gelatinase A) and MMP-9 (gelatinase B) has been studied in benign and malignant human prostatic tumors (WILSON et al.