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      Mechanism Of Cell Surface Activation Of 72-kDa Type IV Collagenase : ISOLATION OF THE ACTIVATED FORM OF THE MEMBRANE METALLOPROTEASE

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          Cancer metastasis and angiogenesis: an imbalance of positive and negative regulation.

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            A matrix metalloproteinase expressed on the surface of invasive tumour cells.

            Gelatinase A (type-IV collagenase; M(r) 72,000) is produced by tumour stroma cells and is believed to be crucial for their invasion and metastasis, acting by degrading extracellular matrix macro-molecules such as type IV collagen. An inactive precursor of gelatinase A (pro-gelatinase A) is secreted and activated in invasive tumour tissue as a result of proteolysis which is mediated by a fraction of tumour cell membrane that is sensitive to metalloproteinase inhibitors. Here we report the cloning of the complementary DNA encoding a new matrix metalloproteinase with a potential transmembrane domain. Expression of the gene product on the cell surface induces specific activation of pro-gelatinase A in vitro and enhances cellular invasion of the reconstituted basement membrane. Tumour cells of invasive lung carcinomas, which contain activated forms of gelatinase A, were found to express the transcript and the gene product. The new metalloproteinase may thus trigger invasion by tumour cells by activating pro-gelatinase A on the tumour cell surface.
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              Matrix Metalloproteinases: A Review

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                Author and article information

                Journal
                Journal of Biological Chemistry
                J. Biol. Chem.
                American Society for Biochemistry & Molecular Biology (ASBMB)
                0021-9258
                1083-351X
                March 10 1995
                March 10 1995
                : 270
                : 10
                : 5331-5338
                Article
                10.1074/jbc.270.10.5331
                © 1995

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