PROTEOLYSIS OF HUMAN NATIVE AND OXIDIZED ALPHA-1-PROTEINASE INHIBITORBY MATRILYSIN AND STROMELYSIN

Authors
ZHANG Z WINYARD PG CHIDWICK K MURPHY G WARDELL M CARRELL RW BLAKE DR
Citation
Z. Zhang et al., PROTEOLYSIS OF HUMAN NATIVE AND OXIDIZED ALPHA-1-PROTEINASE INHIBITORBY MATRILYSIN AND STROMELYSIN, Biochimica et biophysica acta (G). General subjects, 1199(2), 1994, pp. 224-228
Citations number
34
Categorie Soggetti
Biology,Biophysics
Journal title
Biochimica et biophysica acta (G). General subjects → ACNP
ISSN journal
03044165
Volume
1199
Issue
2
Year of publication
1994
Pages
224 - 228
Database
ISI
SICI code
0304-4165(1994)1199:2<224:POHNAO>2.0.ZU;2-A
Abstract
Matrilysin is shown to rapidly inactivate alpha(1)PI, an inhibitor of elastase, by cleaving the Pro(357)-Met(358) peptide bond of its reacti ve centre. The rate of inactivation of alpha(1)PI by matrilysin is fou r times higher than stromelysin. Matrilysin cleaves oxidised alpha(1)P I at the Phe(352)-Leu(353) bond, whilst stromelysin cleaves oxidised a lpha(1)PI at the Met(358)-Ser(359) bond. We conclude that matrilysin i s a potent serpinase which could play a role in inflammatory tissue da mage by proteolytically inactivating alpha(1)PI.