Proteolysis of human native and oxidised alpha 1-proteinase inhibitor by matrilysin and stromelysin.
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.
Zhang
Z
Z
Inflammation Research Group, London Hospital Medical College, University of London, UK.
Winyard
P G
PG
Chidwick
K
K
Murphy
G
G
Wardell
M
M
Carrell
R W
RW
Blake
D R
DR
D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D019278:Matrix Metalloproteinase 3; D020783:Matrix Metalloproteinase 7; D008666:Metalloendopeptidases / Q000378:metabolism*; D008969:Molecular Sequence Data; D010084:Oxidation-Reduction; D000515:alpha 1-Antitrypsin / Q000378:metabolism*
D000515:alpha 1-Antitrypsin; D008666:Metalloendopeptidases; D019278:Matrix Metalloproteinase 3; D020783:Matrix Metalloproteinase 7