The human complement system in thrombin-mediated platelet function

Thrombin-mediated platelet membrane-specific uptake of C3 and C5 was demonstrated by radiolabeled components and was visualized electron microscopically utilizing a ferritin marker conjugated to monospecific antibody to each component. The role of complement in thrombin-induced platelet function was determined. Though complement was not essential for thrombin-induced platelet aggregation and release of serotonin, these activities were significantly increased if complement was present. The release of serotonin was found to be a nonlytic process because under the conditions employed, no lactic dehydrogenase was released. The activation of complement was induced by a mechanism which has not been previously described. Thrombin associated with the platelet membrane presumably formed a C3 convertase that entered the known complement sequence at the C3 stage and proceeded to activate the terminal components through the known sequence to C9.

• Publication year

  1978

• Venue

  Journal of Experimental Medicine

• Publication date

  1978-06-01

• Fields of study

  Biology, Medicine

• Identifiers
  DOI 10.1084/JEM.147.6.1713PMID 681879PMCID 2184322
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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