Go Back MMP 15 (MT2-MMP) catalytic domain

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Matrix metalloproteinases (MMPs) are Zn2+- and Ca2+-dependent endopeptidases which function in the turnover of extracellular matrix components [1]. Presently fifteen secreted MMPs and six membrane-type MMPs are known to be expressed in humans. Human MT2-MMP consists of 628 amino acid residues with a calculated Mr of 71 588 Da [2]. The following domains and sequence regions are distinguished in MT2-MMP: Prodomain (Leu1 - Arg90), catalytic domain (Tyr91 - Gly263), junction between catalytic domain and hemopexin domain (Thr264 - Gly325), hemopexin-like domain (Pro326 - Cys518) and C-terminal sequence (Gln519 - V628) with transmembrane segment. MT2-MMP is expressed in adult liver, placenta, testis, colon, intestine, pancreas, kidney, lung, heart and skeletal muscle [2]. MT2-MMP activates progelatinase A (72-kDa type IV procollagenase) [3,4,5]. The recombinant catalytic domain of MT2-MMP hydrolyzes proteins of the extracellular matrix such as fibronectin, tenascin, laminin, and nidogen. It cleaves the proteoglycans aggrecan and perlecan [6]. The activity of MT2-MMP is poorly inhibited by tissue inhibitor of matrix metalloproteinases-1 (TIMP-1), but efficiently inhibited by TIMP-2 and TIMP-3 [4].