Co-culture of human breast adenocarcinoma MCF-7 cells and human dermal fibroblasts enhances the production of matrix metalloproteinases 1, 2 and 3 in fibroblasts
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Matrix metalloproteinases(MMPs)that plays an important role in neutral pH value are a family of zinc-containing endopeptidases.MMPs cleave the whole component of the extracellular matrix,containing approximately 20 subunits and requiring calcium to maintain normal functions.The expression and activation of MMPs are under the precise control.Gelatinase is the most important class in MMPs.Recent years,the expression and activation of MMPs are increased in pediatric cardiovascular diseases.Gelatinase has also been found to play a significant role in the development of myocardial remodelling and congestive heart failure in children.This article aims to review the relationship between gelatinase and cardiovascular diseases in children in recent years.
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Article Enzyme Linked Immunosorbent Assays (ELISA) for the Quantitative Determination of Human Leukocyte Collagenase and Gelatinase was published on January 1, 1989 in the journal Clinical Chemistry and Laboratory Medicine (CCLM) (volume 27, issue 6).
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Activated gelatinase A is reportedly associated with tumor spread. We identified novel matrix metalloproteinases that localize on the cell surface and mediate the activation of progelatinase A. Thus, these progelatinase A activators were named membrane-type matrix metalloproteinase-1 and -2 (MT-MMP-1 and -2, respectively). MT-MMP-1 is overexpressed in malignant tumor tissues, including lung and stomach carcinomas that contain activated gelatinase A. This suggests that MT-MMP-1 is associated with the activation of progelatinase A in these tumor tissues. The expression of MT-MMP-1 also induced binding of gelatinase A to the cell surface by functioning as a receptor. The cell surface localization of proteinases has advantages over pericellular proteolysis. MT-MMP-1 and its family may play a central role in the cell surface localization and activation of progelatinase A and via this mechanism, tumor cell use exogenous progelatinase A to mediate the proteolysis associated with invasion and metastasis.
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Abstract BACKGROUND In the current study, the authors investigated the effects of synthetic low molecular weight inhibitors of matrix metalloproteinases (MMPs) on the expression and activation of MMP‐2 in a three‐dimensional tissue system. METHODS Rabbit periosteal explants were cultured with or without various concentrations of the MMP inhibitors CT1166, CT1399, or CT1746, and conditioned media and tissue extracts were analyzed for the expression and activity of MMP‐2. RESULTS The data showed that blocking the activity of all MMPs with relatively high inhibitor concentrations completely prevented the conversion of pro‐MMP‐2 into its active form and that the level of protein was decreased. Selective inhibition of the activity of gelatinases (MMP‐2 and MMP‐9) by using low inhibitor concentrations, however, induced a higher level of active MMP‐2 and increased its expression significantly. CONCLUSIONS The current observations indicate that selective inhibitors of MMPs affect the expression and activity of MMP‐2, thus providing clues regarding the differing effects such inhibitors appear to have when applied in vivo. Cancer 2003;97:1582–88. © 2003 American Cancer Society. DOI 10.1002/cncr.11193
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