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Title: Proteolysis of human native and oxidised alpha 1-proteinase inhibitor by matrilysin and stromelysin. Author: Zhang Z, Winyard PG, Chidwick K, Murphy G, Wardell M, Carrell RW, Blake DR. Journal: Biochim Biophys Acta; 1994 Mar 02; 1199(2):224-8. PubMed ID: 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.[Abstract] [Full Text] [Related] [New Search]