gelatinase

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gel·a·tin·ase

(jĕ-lat'i-nās),
Pepsin B; a metalloproteinase that hydrolyzes gelatin and a number of types of collagen. See: pepsin.

gelatinase

(jĕl′ă-tĭn-ās),

MMP-2; MMP-9

Metalloproteinases that cleave gelatin, or nondenatured collagen. Two forms of gelatinase, A and B, have been identified. Gelatinase A (MMP-2) has a molecular weight of about 72,000, and gelatinase B (MMP-9) has a molecular weight of about 92,000. Both are involved in cancer angiogenesis and metastasis and are blocked by a variety of naturally occurring and synthetic inhibitors.
References in periodicals archive ?
Our results (higher concentrations of gelatinase A in type I NAFs from healthy and BBD tissue) are in agreement with findings of MMP production/ secretion in healthy breast tissue (3, 4, 6, 20, 22).
Western blot results indicated that both latent and active forms of gelatinase A accumulate in the cervix during pregnancy and are maximal at term (Figure 2).
Due to the parallel changes in proteoglycan synthesis and levels of gelatinase A activity, we believe that changes in gelatinase A levels in the uterine cervix play a role in proteoglycan turnover and remodeling in the cervix during parturition.
The significant inhibitory effects of Captopril on scleral gelatinase A activity in vitro suggest that tins agent may prove useful in therapies designed to slow or prevent myopia progression.
Zymograms were digitized using a flatbed scanner and relative amounts of active and latent gelatinase A were measured on zymograms using NIH Image 1.
Western blotting and biochemical analyses identified the gelatinase as latent activatable proMMP-2 (Fig.