Plasma membrane-bound tissue inhibitor of metalloproteinases (TIMP)-2 specifically inhibits matrix metalloproteinase 2 (gelatinase A) activated on the cell surface.

Journal article

The cell-surface activation of pro-matrix metalloproteinase 2 (pro-MMP-2) is considered to be critical for cell migration and invasion. Treatment of human uterine cervical fibroblasts with concanavalin A activates pro-MMP-2 on the cell surface by converting it to the 65-kDa form with a minor form of 45 kDa. However, the 65-kDa MMP-2 was inactivated by tissue inhibitor of metalloproteinases (TIMP)-2 that was bound to the plasma membrane upon concanavalin A treatment. TIMP-2 binds to the plasma...

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Authors: Itoh, Y; Ito, A; Iwata, K; Tanzawa, K; Mori, Y

• Journal: Journal of biological chemistry
• Volume: 273
• Issue: 38
• Pages: 24360-24367
• Publication date: 1998-09-01
• DOI: 10.1074/jbc.273.38.24360
• EISSN: 1083-351X
• ISSN: 0021-9258
• Language: English
• Keywords: Concanavalin A; Uterus; Kinetics; Cells, Cultured; CHO Cells; Recombinant Proteins; Cricetinae; Gelatinases; Fibroblasts; Cell Membrane; Female; Enzyme Activation; Matrix Metalloproteinase 3; Hydroxamic Acids; Transfection; Humans; Tissue Inhibitor of Metalloproteinase-2; Molecular Weight; Matrix Metalloproteinase 2; Collagenases; Animals; Metalloendopeptidases; Matrix Metalloproteinase 9