MMP 2 ( matrix metallopeptidase 2 ( gelatinase A , 72 kDa gelatinase , 72 kDa type IV collagenase ) .
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چکیده
Description MMP2 is a Zn dependent endopeptidase, synthesized and secreted in zymogen form. The nascent form of the protein shows an N-terminal signal sequence ('pre' domain) that directs the protein to the endoplasmic reticulum. The pre domain is followed by a propeptide'pro' domain that maintains enzyme-latency until cleaved or disrupted, and a catalytic domain that contains the conserved zinc-binding region.
منابع مشابه
Secretion of 72 kDa type IV collagenase/gelatinase by cultured human lipocytes. Analysis of gene expression, protein synthesis and proteinase activity.
The matrix metalloproteinases play an important role in matrix degradation, but there is limited information about this family of enzymes in either normal or diseased human liver. In this study, we have examined the synthesis of a 72 kDa type IV collagenase/gelatinase by human hepatic lipocytes in primary culture. Hepatic lipocytes were isolated from wedges of normal human donor liver by Pronas...
متن کاملDomain structure of human 72-kDa gelatinase/type IV collagenase. Characterization of proteolytic activity and identification of the tissue inhibitor of metalloproteinase-2 (TIMP-2) binding regions.
The 72-kDa gelatinase/type IV collagenase, a metalloproteinase thought to play a role in metastasis and in angiogenesis, forms a noncovalent stoichiometric complex with the tissue inhibitor of metalloproteinase-2 (TIMP-2), a potent inhibitor of enzyme activity. To define the regions of the 72-kDa gelatinase responsible for TIMP-2 binding, a series of NH2- and COOH-terminal deletions of the enzy...
متن کاملGelatinase Expression of Interstitial Collagenase, Stromelysin, and 72-kDa Tumor Cell-derived Collagenase-stimulatory Factor Increases
The tumor cell-derived collagenase-stimulatory factor (TCSF) was pre viously purified from human lung carcinoma cells (S. M. Ellis, K. Nabeshima, and C. Biswas, Cancer Res., 49: 3385-3391, 1989). This protein is present on the surface of several types of human tumor cells in vitro and in vivo and stimulates production of interstitial collagenase in human fibroblasts. In this study it is shown t...
متن کاملIntracellular activation of gelatinase A (72-kDa type IV collagenase) by normal fibroblasts.
Normal fibroblasts cultured as monolayers secrete matrix metalloproteinases (MMP), including gelatinase A (72-kDa type IV collagenase) as inactive zymogens. Previously we found that normal fibroblasts cultured in a type I collagen lattice (dermal equivalent) secrete active gelatinase A. Here we show that the activation of progelatinase A occurs within the cell and that the activator copurifies ...
متن کاملMatrix metalloproteinase 9 (92-kDa gelatinase/type IV collagenase) from HT 1080 human fibrosarcoma cells. Purification and activation of the precursor and enzymic properties.
Matrix metalloproteinase 9 (MMP-9) has been purified as an inactive zymogen of M(r) 92,000 (proMMP-9) from the culture medium of HT 1080 human fibrosarcoma cells. The NH2-terminal sequence of proMMP-9 is Ala-Pro-Arg-Gln-Arg-Gln-Ser-Thr-Leu-Val-Leu-Phe-Pro, which is identical to that of the 92-kDa type IV collagenase/gelatinase. The zymogen can be activated by 4-aminophenylmercuric acetate, yiel...
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تاریخ انتشار 2011