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Proteolysis of human native and oxidised alpha 1-proteinase inhibitor by matrilysin and stromelysin.

作者信息

Zhang Z, Winyard P G, Chidwick K, Murphy G, Wardell M, Carrell R W, Blake D R

机构信息

Inflammation Research Group, London Hospital Medical College, University of London, UK.

出版信息

Biochim Biophys Acta. 1994 Mar 2;1199(2):224-8. doi: 10.1016/0304-4165(94)90119-8.

DOI:10.1016/0304-4165(94)90119-8
PMID:8123672
Abstract

Matrilysin is shown to rapidly inactivate alpha 1PI, an inhibitor of elastase, by cleaving the Pro357-Met358 peptide bond of its reactive centre. The rate of inactivation of alpha 1PI by matrilysin is four times higher than stromelysin. Matrilysin cleaves oxidised alpha 1PI at the Phe352-Leu353 bond, whilst stromelysin cleaves oxidised alpha 1PI at the Met358-Ser359 bond. We conclude that matrilysin is a potent serpinase which could play a role in inflammatory tissue damage by proteolytically inactivating alpha 1PI.

摘要

相似文献

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Proteolysis of human native and oxidised alpha 1-proteinase inhibitor by matrilysin and stromelysin.
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2
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