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The C-terminal domain of 72 kDa gelatinase A is not required for catalysis, but is essential for membrane activation and modulates interactions with tissue inhibitors of metalloproteinases
Open accessAbstract
Recombinant 72 kDa gelatinase A and a truncated form lacking the C-terminal domain were shown to be activated by organomercurials and to possess similar activities towards a number of substrates. The truncated proenzyme differed from the full-length gelatinase in that it could not be activated by a membrane activator and did not bind tissue inhibitor of metalloproteinase (TIMP)-2. Kinetic studies also showed that the inhibition of the activated truncated enzyme, by both TIMP-1 and TIMP-2, was considerably decreased compared with the full-length enzyme. We conclude that the C-terminal domain plays an important role in the regulation of gelatinase A by a potential physiological activator and inhibitors.
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Cited by
Butler, G. S., Butler, M. J., Atkinson, S. J., Will, H., Tamura, T., van Westrum, S. S., Crabbe, T., Clements, J., d'Ortho, M.-P., & Murphy, G. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.2.871 · Cited by 470
Self-citationFernandez‐Catalan, C., Bode, W., Huber, R., Turk, D., Calvete, J. J., Lichte, A., Tschesche, H., & Maskos, K. (1998) · The EMBO Journal · doi:10.1093/emboj/17.17.5238 · Cited by 321
Baker, A. H., George, S. J., Zaltsman, A. B., Murphy, G., & Newby, A. C. (1999) · British Journal of Cancer · doi:10.1038/sj.bjc.6690217 · Cited by 286
Self-citationTam, E. M., Moore, T. R., Butler, G. S., & Overall, C. M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m407186200 · Cited by 142
Advances in animal cell recombinant protein production: GS-NS0 expression system
Barnes, L. M., Bentley, C. M., & Dickson, A. J. (2000) · Cytotechnology · doi:10.1023/a:1008170710003 · Cited by 129
Metadata
- Authors
- Murphy, G., Willenbrock, F., Ward, R. V., Cockett, M. I., Eaton, D., & Docherty, A. J. P.
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 1992-05-01
- Volume
- 283
- Issue
- 3
- Pages
- 637-641
- ISSN
- 0264-6021 (ISSN-L)
- 1470-8728
- OpenAlex
- W1700189391
- Cited by
- 265
- References
- 0
- FWCI
- 15.69
- Type
- journal article
- Language
- en
- Open access
- bronze
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