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TNF‐α converting enzyme (TACE) is inhibited by TIMP‐3
Abstract
TNF‐α converting enzyme (TACE; ADAM‐17) is a membrane‐bound disintegrin metalloproteinase that processes the membrane‐associated cytokine proTNF‐α to a soluble form. Because of its putative involvement in inflammatory diseases, TACE represents a significant target for the design of specific synthetic inhibitors as therapeutic agents. In order to study its inhibition by tissue inhibitors of metalloproteinases (TIMPs) and synthetic inhibitors of metalloproteinases, the catalytic domain of mouse TACE (rTACE) was overexpressed as a soluble Ig fusion protein from NS0 cells. rTACE was found to be well inhibited by peptide hydroxamate inhibitors as well as by TIMP‐3 but not by TIMP‐1, ‐2 and ‐4. These results suggest that TIMP‐3, unlike the other TIMPs, may be important in the modulation of pathological events in which TNF‐α secretion is involved.
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Cites
A metalloproteinase disintegrin that releases tumour-necrosis factor-α from cells
Black, R. A., Rauch, C. T., Kozlosky, C. J., Peschon, J. J., Slack, J. L., Wolfson, M. F., Castner, B. J., Stocking, K. L., Reddy, P., Srinivasan, S., et al. (1997) · Nature · doi:10.1038/385729a0 · Cited by 3,149
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
Cited by
Visse, R., & Nagase, H. (2003) · Circulation Research · doi:10.1161/01.res.0000070112.80711.3d · Cited by 4,575
Newby, A. C. (2005) · Physiological Reviews · doi:10.1152/physrev.00048.2003 · Cited by 817
Hypercholesterolemia Accelerates the Alzheimer's Amyloid Pathology in a Transgenic Mouse Model
Refolo, L. M., Pappolla, M. A., Malester, B., LaFrancois, J., Bryant-Thomas, T., Wang, R., Tint, G. S., Sambamurti, K., & Duff, K. (2000) · Neurobiology of Disease · doi:10.1006/nbdi.2000.0304 · Cited by 783
Metalloproteinases and their inhibitors: Regulators of wound healing
Gill, S. E., & Parks, W. C. (2008) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2007.10.024 · Cited by 742
ADAM-17: the enzyme that does it all
Gooz, M. (2010) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409231003628015 · Cited by 377
Metadata
- Authors
- Amour, A., Slocombe, P. M., Webster, A., Butler, M., Knight, C. G., Smith, B. J., Stephens, P. E., Shelley, C., Hutton, M., Knäuper, V., Docherty, A. J. P., & Murphy, G.
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 1998-09-11
- Volume
- 435
- Issue
- 1
- Pages
- 39-44
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W1997522892
- Cited by
- 609
- References
- 2
- FWCI
- 10.72
- Type
- journal article
- Language
- en
- Open access
- closed
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- Amour, A., Slocombe, P. M., Webster, A., Butler, M., Knight, C. G., Smith, B. J., Stephens, P. E., Shelley, C., Hutton, M., Knäuper, V., Docherty, A. J. P., & Murphy, G. (1998). TNF‐α converting enzyme (TACE) is inhibited by TIMP‐3. FEBS Letters. https://doi.org/10.1016/s0014-5793(98)01031-x
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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