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 ?
Grupo Colagenases MMP Nome enzimatico MMP-1 Colagenase intersticial MMP-8 Neutrofilo colagenase MMP-13 Colagenase-3 Gelatinases MMP-2 Gelatinase A MMP-9 Gelatinase B Estromalisinas MMP-3 Estromalisina-1 MMP-10 Estromalisina-2 MMP-11 Estromalisina-3 MMPs tipo MMP-14 MT1-MMP membrana MMP-16 MT3-MMP MMP-17 MT4-MMP MMP-24 MT5-MMP MMP-25 MT6-MMP Outras MMP-7 Matrilisina MMP-26 Matrilisina-2 MMP-12 Macrofago metaloelastase
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.
Punches (3 mm) were obtained from the posterior sclera of chick eyes and immediately placed in multiwell plates containing Dulbecco's Modified Eagle's Medium (DMEM) alone (controls) or DMEM containing Tissue Inhibitor of Metalloproteinase CRIMP)--2, a natural inhibitor of gelatinase A, Nobiletin, a citrus flavonoid, or Captopril, an inhibitor of angiotensin converting enzyme, which also blocks activity of [Zn.sup.2+]-dependent metalloproteinases.
When placed in organ culture, scleral punches from chick eyes released clearly detectable levels of both the latent and active forms of gelatinase A into the medium.
NAFs from BBD patients who subsequently developed BC showed additional gelatinolytic bands (activated forms of both gelatinase A and B; Fig.
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).
Zymographic analysis of circulating and tissue forms of colon carcinoma gelatinase A (MMP-2) and B (MMP-9) separated by mono- and two-dimensional electrophoresis.
Western blotting and biochemical analyses identified the gelatinase as latent activatable proMMP-2 (Fig.