The human complement system in thrombin-mediated platelet function. Academic Article uri icon

Overview

abstract

  • 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 date

  • June 1, 1978

Research

keywords

  • Blood Platelets
  • Complement System Proteins
  • Thrombin

Identity

PubMed Central ID

  • PMC2184322

Scopus Document Identifier

  • 0018101590

Digital Object Identifier (DOI)

  • 10.1084/jem.147.6.1713

PubMed ID

  • 681879

Additional Document Info

volume

  • 147

issue

  • 6