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.
Article| June 01 1978
The human complement system in thrombin-mediated platelet function.
M J Polley
Online ISSN: 1540-9538
Print ISSN: 0022-1007
J Exp Med (1978) 147 (6): 1713–1726.
M J Polley, R Nachman; The human complement system in thrombin-mediated platelet function.. J Exp Med 1 June 1978; 147 (6): 1713–1726. doi: https://doi.org/10.1084/jem.147.6.1713
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