SUPEROXIDE-DISMUTASE TRIGGERS ACTIVATION OF PRIMED PLATELETS

被引：27

作者：

IULIANO, L ^{[1
]}

PRATICO, D ^{[1
]}

GHISELLI, A ^{[1
]}

BONAVITA, MS ^{[1
]}

VIOLI, F ^{[1
]}

机构：

[1] UNIV ROME LA SAPIENZA,INST CLIN MED 1,I-00185 ROME,ITALY

来源：

ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS | 1991年 / 289卷 / 01期

关键词：

D O I：

10.1016/0003-9861(91)90458-U

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Superoxide dismutase (SOD) triggers activation of human platelets exposed to subthreshold concentrations of arachidonic acid and collagen. The subthreshold concentrations used are not able to activate platelets but "prime" platelets to be activated by SOD. The addition of SOD to arachidonic acid- or collagen-primed platelets induced aggregation, thromboxane A2 production, and release of [3H]serotonin. Superoxide dismutase does not have any effect on resting platelets and ADP-, thrombin-, calcium ionophore A23187-, PAF-, or U46619-stimulated platelets. Furthermore, superoxide dismutase-dependent platelet activation is fully prevented by catalase and/or aspirin, suggesting a role for H2O2 and the involvement of the cyclooxygenase pathway of arachidonic acid in such activation. © 1991.

引用

页码：180 / 183

页数：4

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