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The N-terminal domain of tissue inhibitor of metalloproteinases retains metalloproteinase inhibitory activity
Abstract
Recombinant tissue inhibitor of metalloproteinases (TIMP-1) and a truncated version containing only the three N-terminal loops, delta 127-184TIMP, have been expressed in myeloma cells and purified by affinity chromatography and gel filtration. delta 127-184TIMP was found to exist as two main glycosylation variants of molecular mass 24 kD and 19.5 kDa and an unglycosylated form of 13 kDa. All forms of the truncated inhibitor were able to inhibit and form complexes with active forms of the matrix metalloproteinases, indicating that the major structural features for specific interaction with these enzymes resides in these three loops. Stable binding of delta 127-184TIMP to pro 95-kDa gelatinase was not demonstrable under the conditions for binding of full-length TIMP-1.
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Cited by
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Novel functions of TIMPs in cell signaling
Chirco, R., Liu, X.-W., Jung, K.-K., & Kim, H.-R. C. (2006) · Cancer and Metastasis Reviews · doi:10.1007/s10555-006-7893-x · Cited by 401
TIMP-3 Binds to Sulfated Glycosaminoglycans of the Extracellular Matrix
Yu, W.-H., Yu, S.-S. C., Meng, Q., Brew, K., & Woessner, J. F. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m000907200 · Cited by 328
Iredale, J. P., Benyon, R. C., Arthur, M. J., Ferris, W. F., Alcolado, R., Winwood, P. J., Clark, N., & Murphy, G. (1996) · Hepatology · doi:10.1002/hep.510240129 · Cited by 324
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Advances in animal cell recombinant protein production: GS-NS0 expression system
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Grossman, M., Tworowski, D., Dym, O., Lee, M.-H., Levy, Y., Murphy, G., & Sagi, I. (2010) · Biochemistry · doi:10.1021/bi902141x · Cited by 68
Self-citationSorsby fundus dystrophy—A review of pathology and disease mechanisms
Christensen, D. R. G., Brown, F. E., Cree, A. J., Ratnayaka, J. A., & Lotery, A. J. (2017) · Experimental Eye Research · doi:10.1016/j.exer.2017.08.014 · Cited by 60
Mercuri, F. A., Maciewicz, R. A., Tart, J., Last, K., & Fosang, A. J. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.42.33038 · Cited by 52
The isolated N-terminal domains of TIMP-1 and TIMP-3 are insufficient for ADAM10 inhibition.
Rapti, M., Atkinson, S. J., Lee, M.-H., Trim, A., Moss, M., & Murphy, G. (2008) · Biochemical Journal · doi:10.1042/bj20071430 · Cited by 43
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Metadata
- Authors
- Murphy, G., Houbrechts, A., Cockett, M. I., Williamson, R. A., O'Shea, M., & Docherty, A. J. P.
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 1991-08-01
- Volume
- 30
- Issue
- 33
- Pages
- 8097-8102
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W2000212022
- Cited by
- 324
- References
- 0
- FWCI
- 9.09
- Type
- journal article
- Language
- en
- Open access
- closed
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