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Preferential inactivation of tissue inhibitor of metalloproteinases-1 that is bound to the precursor of matrix metalloproteinase 9 (progelatinase B) by human neutrophil elastase.

Abstract:

The precursor of matrix metalloproteinase 9 (pro-MMP-9) forms a complex with the tissue inhibitor of metalloproteinases (TIMP)-1 through the C-terminal domain of each molecule, and the N-terminal domain of TIMP-1 in the complex interacts and inhibits active MMPs. We have reported that a catalytic amount of MMP-3 (stromelysin 1) activates pro-MMP-9 (Ogata, Y., Enghild, J. J., and Nagase, H. (1992) J. Biol. Chem. 267, 3581-3584). To activate pro-MMP-9 in the complex, however, an excess molar am...

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Publisher copy:
10.1074/jbc.270.28.16518

Authors


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Institution:
University of Oxford
Department:
Oxford, MSD, NDORMS
Role:
Author
Journal:
The Journal of biological chemistry
Volume:
270
Issue:
28
Pages:
16518-16521
Publication date:
1995-07-05
DOI:
EISSN:
1083-351X
ISSN:
0021-9258
URN:
uuid:ce1fca0f-f84a-4564-9b30-9548612f6d2b
Source identifiers:
411408
Local pid:
pubs:411408

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