- 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...
Expand abstract - Publisher copy:
- 10.1074/jbc.270.28.16518
-
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- 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
- Copyright date:
- 1995
Journal article
Preferential inactivation of tissue inhibitor of metalloproteinases-1 that is bound to the precursor of matrix metalloproteinase 9 (progelatinase B) by human neutrophil elastase.
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