Human complement in thrombin-mediated platelet function: uptake of the C5b-9 complex. Academic Article uri icon

Overview

abstract

  • 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.

publication date

  • September 19, 1979

Research

keywords

  • Blood Platelets
  • Complement C5
  • Complement C9
  • Complement System Proteins
  • Thrombin

Identity

PubMed Central ID

  • PMC2185636

Scopus Document Identifier

  • 0018290947

Digital Object Identifier (DOI)

  • 10.1084/jem.150.3.633

PubMed ID

  • 479764

Additional Document Info

volume

  • 150

issue

  • 3