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 ?
MMP-2 and MMP-9 are members of gelatinase group and are able to degrade gelatin and collagen (2).
Net gelatinolytic activity reflects the proteolytic activity of gelatinases in a specific tissue [22].
Our results demonstrate that AREG enhances gelatinase protein expression via engagement with EGFR.
Tetracyclines are a class of antibiotics which inhibit the catalytic activity of human collagenases and gelatinases, especially MMPs.
Degradation of basement membranes by gelatinases that are only metalloproteinases able to degrade basement membrane collagen (type IV) may result in the formation of distant metastases.
Fainardi et al., "Effects of anticoagulants on the activity of gelatinases," Clinical Biochemistry, vol.
MMP-2, MMP-3, MMP-9, MMP-13, and MT1-MMP have all been identified in neuronal nuclei and gelatinases (MMP-2 and MMP-9) and MMP-3 have been implicated in the progression of infarct volume and neuronal death in animal models of stroke and ischemic stroke patients [9,16,18, 23, 29-33].
[9-11] MMP-9 (Gelatinase B) is released by neutrophils, monocytes, macrophages, and eosinophils in the course of inflammatory response.
Collagenases, gelatinases, stromelysin-3, matrilysin, MT1-MMP [99], and stromelysin-1 [100] are considered the most closely associated to the invasive phenotype.