Platelet activation by Protease I of Porphyromonas gingivalis W83.

Abstract:

:Porphyromonas gingivalis produces a trypsin-like enzyme, Protease I, which is thought to be an important virulence determinant of the organism in adult periodontal disease. Protease I is transiently inhibited by physiological inhibitors of human thrombin. The aim of the present work was to establish whether Protease I was able to mimic thrombin by activation of the thrombin receptor on human platelets. Protease I caused true platelet activation at concentrations comparable to thrombin as measured by aggregometry, morphology and fluorescence flow cytometric analysis of CD63 expression. The effect was blocked by protease inhibitors but not by anti-thrombin receptor antibodies which, by contrast, blocked platelet activation by thrombin. We conclude that the activation of platelets by P. gingivalis Protease I involves proteolysis, but not scission of the thrombin cleavage site of the thrombin receptor.

journal_name

FEMS Microbiol Lett

authors

Curtis MA,Macey M,Slaney JM,Howells GL

doi

10.1111/j.1574-6968.1993.tb06315.x

subject

Has Abstract

pub_date

1993-06-15 00:00:00

pages

167-73

issue

2

eissn

0378-1097

issn

1574-6968

journal_volume

110

pub_type

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