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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
Visse, R., & Nagase, H. (2003) · Circulation Research · doi:10.1161/01.res.0000070112.80711.3d · Cited by 4,575
Mechanism of inhibition of the human matrix metalloproteinase stromelysin-1 by TIMP-1.
Gomis-R¨th, F.-X., Maskos, K., Betz, M., Bergner, A., Huber, R., Suzuki, K., Yoshida, N., Nagase, H., Brew, K., Bourenkov, G. P., et al. (1997) · Nature · doi:10.1038/37995 · Cited by 619
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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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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- CoChat. (2026). Citation check: The N-terminal domain of tissue inhibitor of metalloproteinases retains metalloproteinase inhibitory activity. https://app.cochat.ai/papers/10.1021/bi00247a001
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- Murphy, G., Houbrechts, A., Cockett, M. I., Williamson, R. A., O'Shea, M., & Docherty, A. J. P. (1991). The N-terminal domain of tissue inhibitor of metalloproteinases retains metalloproteinase inhibitory activity. Biochemistry. https://doi.org/10.1021/bi00247a001
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
