stromelysin


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stromelysin

(strō′mă-līs-ĭn),

MMP-3

Member of the matrix metalloproteinase family of enzymes that plays a major role in the degradation of proteoglycans, gelatin, and other constituents of the extracellular matrix. Two forms of stromelysin have been described, stromelysin-1 and -2. Stromelysin-1 degrades proteoglycans, gelatin, fibronectin, laminin, collagen types III, IV, IX, and X. Stromelysin-2 degrades proteoglycans, fibronectin, laminin, and collagen type IV.
References in periodicals archive ?
Sites of stromelysin cleavage in collagen types II, IX, X, and XI of cartilage.
In situ hybridization studies of stromelysin and collagenase messenger RNA expression in rheumatoid synovium.
Stromelysin and tissue inhibitor of metalloproteinases gene expression in rheumatoid arthritis synovium.
The complete primary structure of human matrix metalloproteinase-3: identity with stromelysin.
MMPs are divided into subgroups, distinguished by specific structural domains: collagenases, gelatinases, stromelysins, matrilysins, metaloelastases, and membrane type matrix metalloproteinases (MT-MMPs) (Figure 5) [46].
MMPs are a family of zinc- and calcium-dependent endopeptidases, consisting of four subclasses based on substrate, including collagenases, gelatinases, stromelysins and membrane-associated MMPs.
The main enzymes involved in cartilage destruction in rheumatoid arthritis and LA are collagenases (MMP-1, MMP-13) gelatinases (MMP-2, MMP-9) and stromelysins (MMP-3, MMP-10) [6,7].
These MMPs are divided into five subgroups according to their substrate specificity and structural similarities: Collagenases, stromelysins, gelatinases, matrilysins and membrane-type MMPs (Mook et al.
Based on substrate preference and structural homology, MMPs are sub-classified into functional groups: collagenases, gelatinases, stromelysins, matrilysins, membrane type-MMPs (MT-MMPs) and other non-classified MMPs (Visse and Nagase, 2003).