Authors:
Z Zhang, PG Winyard, K Chidwick, G Murphy, M Wardell, RW Carrell, DR Blake
Journal name: 
Biochim Biophys Acta
Citation info: 
1199(2):224-228
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.
DOI: 
http://doi.org/10.1016/0304-4165(94)90119-8
E-pub date: 
28 Feb 1994
Users with this publication listed: 
Gillian Murphy