matrix metalloproteinase

(redirected from Stromelysin)
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matrix metalloproteinase

[¦mā·triks mə‚tal·ō′prō·tē·ə‚nās]
(biochemistry)
Any member of a family of at least 19 structurally related zinc-dependent neutral endopeptidases collectively capable of degrading essentially all components of extracellular matrix.
References in periodicals archive ?
Effects of treatment on gingival crevicular collagenase, stromelysin and tissue inhibitor of metalloproteinases and their ability to predict response to treatment.
Stromelysin 3 expression: a useful marker for the differential diagnosis dermatofibroma versus dermatofibrosarcoma protuberans.
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.
Localization of stromelysin gene expression in atherosclerotic plaques by in situ hybridization.
Four members of this family have been identified, among which TIMP-1 acts against all members of the collagenase, stromelysin, and gelatinase classes of MMPs (9).
Immunoassays for the detection of human collagenase, stromelysin, tissue inhibitor of metal loproteinases (TIMP) and enzyme-inhibitor complexes.
Plaque rupture is mediated by such enzymes as collagenase, gelatinase, and stromelysin, which degrade components of the interstitial matrix.
Collagenases (MMP-1, MMP-8, and MMP-13) and stromelysins (MMP-3, MMP-10, and MMP11) are composed of a catalytic domain and a hemopexin-like domain.