Steps involved in activation of the pro-matrix metalloproteinase 9 (progelatinase B)-tissue inhibitor of metalloproteinases-1 complex by 4-aminophenylmercuric acetate and proteinases.

Journal article

The precursor of matrix metalloproteinase 9 (pro-MMP-9, progelatinase B) noncovalently binds to tissue inhibitor of metalloproteinases (TIMP)-1 through the C-terminal domain of each molecule. We have isolated the proMMP-9.TIMP-1 complex from the medium of human fibrosarcoma HT-1080 cells and investigated the activation processes of the complex by 4-aminophenylmercuric acetate, trypsin, and matrix metalloproteinase 3 (MMP-3, stromelysin 1). The treatment of the proMMP-9.TIMP-1 complex with 4-a...

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Authors: Ogata, Y; Itoh, Y; Nagase, H

• Journal: Journal of biological chemistry
• Volume: 270
• Issue: 31
• Pages: 18506-18511
• Publication date: 1995-08-01
• DOI: 10.1074/jbc.270.31.18506
• EISSN: 1083-351X
• ISSN: 0021-9258
• Language: English
• Keywords: Tissue Inhibitor of Metalloproteinases; Tumor Cells, Cultured; Metalloendopeptidases; Macromolecular Substances; Collagenases; Glycoproteins; Trypsin; Matrix Metalloproteinase 3; Matrix Metalloproteinase 9; Humans; Protein Binding; Phenylmercuric Acetate; Extracellular Matrix; Enzyme Activation; Enzyme Precursors