PLATELET ACTIVATION BY PROTEASE-I OF PORPHYROMONAS-GINGIVALIS W83
PLATELET ACTIVATION BY PROTEASE-I OF PORPHYROMONAS-GINGIVALIS W83
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DOI：
10.1016/0378-1097(93)90461-a
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发表时间：
1993-06-15
影响因子：
2.1
通讯作者：
HOWELLS, GL
中科院分区：
文献类型：
--
作者：
CURTIS, MA;MACEY, M;HOWELLS, GL
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.
