Human complement in thrombin-mediated platelet function: uptake of the C5b-9 complex

Thrombin-mediated platelet aggregation and release is enhanced by the presence of C3, C5, C6, C7, C8, and C9 of human complement. The interaction of thrombin with its receptor on the platelet membrane initiates activation of complement on the platelet surface. Trypsin-mediated platelet function is n...

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Bibliographic Details
Published in:The Journal of experimental medicine 1979-09, Vol.150 (3), p.633-645
Main Authors: Polley, M J, Nachman, R L
Format: Article
Language:English
Subjects:
Antithrombin III - physiology
Aspirin - pharmacology
Blood Platelets - physiology
Complement C5 - metabolism
Complement C9 - metabolism
Complement System Proteins - physiology
Humans
In Vitro Techniques
Platelet Aggregation - drug effects
Serotonin - metabolism
Thrombin - pharmacology
Trypsin - pharmacology
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Summary:Thrombin-mediated platelet aggregation and release is enhanced by the presence of C3, C5, C6, C7, C8, and C9 of human complement. The interaction of thrombin with its receptor on the platelet membrane initiates activation of complement on the platelet surface. Trypsin-mediated platelet function is not enhanced by the addition of complement, probably because trypsin has no receptor on the platelet surface so activation of complement is triggered in the fluid phase and not on the platelet surface. Activation of complement by thrombin led to production of dimers of the C5b-9 complex on the platelet surface. These complexes were eluted from the platelet membrane and were identified physicochemically and morphologically. The mechanism of complement-induced enhancement of platelet function is not clear, however, it probably is mediated via the arachidonic acid transormation pathway because this activity was blocked by known inhibitors of cyclo-oxygenase, namely, aspirin and indomethacin.
ISSN:0022-1007
1540-9538
DOI:10.1084/jem.150.3.633