gelatinase

(redirected from Gelatinases)
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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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Cellular localization of gelatinases and tissue inhibitors of metalloproteinases during follicular growth, ovulation, and early luteal formation in the rat.
A quantitative comparison of the activities of 95 kDa and 72 kDa gelatinases, stromelysins-1 and -2 and punctuated metalloproteinase (PUMP).
Gelatinases target the structural components of connective tissues (collagen, fibrinogen and hemoglobin) and have the ability to hydrolyze these tissues, increasing enterococcal invasiveness (Waters et al.
Indeed, the carbamylation-induced destabilization of collagen triple-helix conformation is responsible for an altered sensitivity to proteolysis, because carbamylated collagen exhibits greater resistance to collagenases, but increased sensitivity to gelatinases (43).
Gelatinases, a class of enzymes, have been implicated in a host of human diseases from cancer to cardiovascular conditions and in particular neurological conditions such as stroke, aneurysm and traumatic brain injury.
Upregulation of gelatinases A and B, collagenases 1 and 2, and increased parenchymal cell death in CGPD.
Studies performed in rat balloon injury model (7), hypercholesterolemic rabbits (8) and mouse carotid artery ligation model (9) showed that in particular, gelatinases (MMP-2 and MMP-9) play essential role in intimal hyperplasia.
Also, Oggionni et al [22] reported that gelatinases and their inhibitors are significantly activated during BLM-induced pulmonary fibrosis.
2-4) Secreted-type MMPs can be classified into 6 subgroups according to their substrate specificity and structural differences (2): (1) collagenases, including tissue collagenase (MMP1), neutrophil collagenase (MMP8), and collagenase 3 (MMP13); (2) gelatinases, such as gelatinase A (MMP2) and gelatinase B (MMP9); (3) stromelysins, including stromelysin 1 (MMP3) and stromelysin 2 (MMP-10); (4) matrilysins, such as matrilysin 1 (MMP7) and matrilysin 2 (MMP26); (5) furin-activated MMPs, including stromelysin 3 (MMP-13) and epilysin (MMP 28); and (6) other MMPs such as metalloelastase (MMP12), MMP19, enamelysin (MMP-20), MMP21, and MMP-27.
Some MMPs, such as gelatinases, stromelysins and collagenase-3, are believed to play key roles in the invasion, metastasis and growth of many malignant tumors.