MMP3

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MMP3

A gene on chromosome 11q22.3 that encodes matrix metalloproteinase 3, which degrades fibronectin, laminin, collagens III, IV, IX and X, and cartilage proteoglycans. MMP3 is thought to be involved in wound repair, progression of atherosclerosis, and tumour initiation.
 
Molecular pathology
Defects in MMP3 cause susceptibility to coronary heart disease type 6.
References in periodicals archive ?
To investigate collagen metabolism in keratinocytes and fibroblasts co-culture under pressure, and study the role of IL-1[alpha] and MMP-3 in terms of regulating fibroblasts-keratinocytes collagen metabolism with pressure.
Matrix metalloproteinases (MMPs) are special class of proteases that are categorized in five groups as per their substrate specificity: collagenases (MMP-1, -8 and -13), gelatinases (MMP-2 and -9), stromelysins (MMP-3, -10, and -11), matrilysins (MMP-7) and membrane-type (MMP-14 to -17, -24 and -25).
Glycitein inhibits glioma cell invasion through down-regulation of MMP-3 and MMP-9 gene expression.
Twenty-four MMPs have been identified, including collagenases (MMP-1, 8, 13, and 18), gelatinases (MMP-2 and 9), stromelysins (MMP-3 and 10), matrilisins (MMP-7 and 26), and membrane-type MMPs (MMP-14, 15, 16, 17, 24, and 25), among other types.
Depending on the substrate specificity and structure, MMPs are divided into several subgroups: collagenases (e.g., MMP-1), gelatinases (e.g., MMP-2 and MMP-9), stromelysins (e.g., MMP-3 and MMP-10), matrilysins (e.g., MMP-7 and MMP-26), and membrane-type matrix metalloproteinase-1 (MT1-MMP).
The fourth group comprises stromelysins: MMP-3 (stromelysin 1), MMP-10 (stromelysin 2) and MMP-11 (stromelysin 3).
Celastrol is also an inhibitor of Hsp90[beta] to significantly downregulate the expression of MMP-1, MMP-3, MMP-13, iNOS-2, and COX-2 induced by IL-1[beta] [17].
In order to determine whether a mixture of undefined DAMPs released from mechanically injured cartilage was able to evoke MMP-3 secretion from chondrocytes, culture media containing substance diffused from mechanically impacted cartilage at 24 hr postinjury were collected and then applied to chondrocyte monolayer cultures and the expression of MMP-3 was examined after 24 hrs of incubation.
Levels of dermal expression of MMP-3, MMP-9, and MMP-12 are increased in cutis laxa lesional fibroblasts or lymphocytes and are correlated with the degree of disruption of elastic fibers [22].
Among these, MMP-1 has been shown to degrade fibrillar collagens while MMP-3 has a wide range of ECM substrates such as nonfibrillar collagens and laminin [4].
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.