Inhibition of the metalloproteinase domain of mouse TACE

Amour, Augustin, Hutton, Mike, Knaüper, Vera ORCID: https://orcid.org/0000-0002-3965-9924, Slocombe, Patrick M., Webster, Ailsa, Butler, Michael, C. Graham, Knight, Smith, Bryan J., Docherty, Andrew J.P. and Murphy, Gillian 1999. Inhibition of the metalloproteinase domain of mouse TACE. Annals of the New York Academy of Sciences 878 (1) , pp. 728-731. 10.1111/j.1749-6632.1999.tb07774.x

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Abstract

TNF-α converting enzyme (TACE/ADAM-17) is a type I membrane-bound metalloproteinase that processes the type II membrane-bound cytokine proTNF-α into soluble TNF-α. 1,2 Because TNF-α is a major mediator of diseases such as rheumatoid arthritis and sepsis, TACE may represent an important target for the design of specific inhibitors with pharmacological applications. However, concern remains as to whether TACE is involved in the shedding of membrane proteins other than proTNF-α. 3 Recent studies have shown that hydroxamate MMP inhibitors and TIMP-3, but not TIMP-1 or -2, can modulate cell shedding of proTNF-α, L-selectin, and interleukin-6 receptor. 4,5 This suggests that an enzyme, possibly TACE or very similar enzymes, are required for those shedding events.

Item Type:	Article
Date Type:	Publication
Status:	Published
Schools:	Dentistry
Publisher:	Wiley
ISSN:	1749-6632
Last Modified:	08 Nov 2023 16:45
URI:	https://orca.cardiff.ac.uk/id/eprint/161587

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