Human complement in the arachidonic acid transformation pathway in platelets. Academic Article uri icon

Overview

abstract

  • Arachidonate-mediated release of 14C serotonin and thromboxane B2 (TXB2) is significantly enhanced in the presence of complement. Only purified complement components C5, C6, C7, C8, and C9 are required for this reactivity. No known activating mechanism of the classical or alternative pathway is required, nor is C3. In the absence of exogenously added complement, platelet membrane-bound complement components play an essential role in modulating arachidonate-mediated serotonin release. Incubation of platelet membranes with arachidonate and C5--C9 led to the production of dimers of the membrane attack complex (C5b--9) on the platelet surface. These macromolecular complexes were eluted from the platelet membrane and were identified physicochemically and morphologically. The possibility arises that C3 in association with C5--C9 is required for mobilization of the arachidonic acid from the phospholipid of the platelet membrane. Once the arachidonic acid is mobilized, C3 is no longer required, C5--C9 being sufficient to modulate this pathway leading to enhanced production of TXB2.

publication date

  • February 1, 1981

Research

keywords

  • Arachidonic Acids
  • Blood Platelets
  • Complement System Proteins

Identity

PubMed Central ID

  • PMC2186082

Scopus Document Identifier

  • 0019491599

Digital Object Identifier (DOI)

  • 10.1084/jem.153.2.257

PubMed ID

  • 7241047

Additional Document Info

volume

  • 153

issue

  • 2