MMP (matrix metalloproteinase) are proteolytic enzymes capable of degrading connective tissue components. MMP have a common mode of activation, a conserved amino acid sequence in the putative metal binding-active site region, and are inhibited by specific tissue inhibitors of metalloproteinases (TIMPs). MMPa and TIMPs play a significant role in regulating angiogenesis. MMP2 is synthesized as a 631 amino acid proenzyme which is activated by cleavage of the first 80 amino acids, and contains the basic structure of propeptide, catalytic, and hemopexin domains. The matrix metalloproteinases (MMPs) are a family of at least eighteen secreted and membrane-bound zincendopeptidases. Collectively, these enzymes can degrade all the components of the extracellular matrix, including fibrillar and non-fibrillar collagens, fibronectin, laminin and basement membrane glycoproteins. In general, a signal peptide, a propeptide, and a catalytic domain containing the highly conserved zinc-binding site characterizes the structure of the MMPs. Functionally, MMP2 is involved in tissue remodeling. Mutations in MMP-2 gene have been associated with Winchester syndrome and Nodulosis-Arthropathy-Osteolysis (NAO) syndrome. Two transcript variants encoding different isoforms of MMP-2 have been found.
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Protein Aliases: 72 kDa gelatinase; 72 kDa type IV collagenase; 72kD gelatinase; 72kD type IV collagenase; 72kDa gelatinase; 72kDa type IV collagenase; CLG 4A; Collagenase; collagenase type IV-A; Gelatinase A; Gelatinase alpha; Mat; matrix metallo protease; matrix metallopeptidase 2 (gelatinase A, 72kDa gelatinase, 72kDa type IV collagenase); matrix metalloproteinase 2; Matrix metalloproteinase-2; matrix metalloproteinase-II; MMP; MMP-2; MMPs; neutrophil gelatinase; PEX; Progelatinase A; TBE-1; TBE1
Gene Aliases: CLG4; CLG4A; GelA; MMP-2; MMP-II; MMP2; MONA; TBE-1; wu:fa99h12; wu:fk89d01