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Cited by 609

The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.

TNF‐α converting enzyme (TACE) is inhibited by TIMP‐3

Amour, Augustin, Slocombe, Patrick M, Webster, Ailsa, Butler, Michael, Knight, C.Graham, Smith, Bryan J, Stephens, Paul E, Shelley, Chris, Hutton, Mike, Knäuper, Vera, Docherty, Andrew J.P, Murphy, Gillian·1998·FEBS Letters
DOI 10.1016/s0014-5793(98)01031-x
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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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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
DOI
10.1016/s0014-5793(98)01031-x
OpenAlex
W1997522892
Cited by
609
References
2
FWCI
10.72
Type
journal article
Language
en
Open access
closed

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