MMP-7

Matrix metalloproteinases (MMPs) are a family of zinc and calcium dependent endopeptidases with the combined ability to degrade all the components of the extracellular matrix. MMP7 (matrilysin) is expressed in epithelial cells of normal and diseased tissues, and is capable of digesting a large series of proteins of the extracellular matrix including collagen IV and X, gelatin, casein, laminin, aggrecan, entactin, elastin and versican. MMP7 is implicated in the activation of other proteinases such as plasminogen, MMP1, MMP2, and MMP9. In addition to its roles in connective tissue remodeling and cancer, MMP7 also regulates intestinal α-defensin activation in innate host defense, releases tumor necrosis factorα in a model of herniated disc resorption, and cleaves FasL to generate a soluble form in a model of prostate involution. Structurally, MMP7 is the smallest of the MMPs and consists of two domains: a prodomain that is cleaved upon activation and a catalytic domain containing the zincbinding site.