Anticomplementary activity of tuberculin: relationship to platelet aggregation and lytic response.
Experiments were performed to examine the interaction of tuberculin with platelets and complement. Hemolytic complement titrations show that tuberculin consumes complement in human, rabbit, and guinea pig serum. Evidence in support of classical pathway activation was provided by observation of C1 consumption and failure to detect significant conversion of alternative pathway factor B to B by immunoelectrophoresis. Platelets in plasma from guinea pigs deficient in the fourth component of complement were not affected by tuberculin. However, studies on platelet aggregation in plasma chelated with ethyleneglycolbis(beta-aminoethyl ether)-N,N-tetraacetic acid indicated that tuberculin may initiate sluggish activation of the alternative pathway. That the reaction between tuberculin and platelets is a lytic one was evidenced by observing the release of the cytoplasmic enzyme lactic dehydrogenase and efflux of rubidium-86. Studies with C6-deficient rabbits indicated that platelet release of exogenously supplied tritiated serotonin is caused by platelet lysis.
D000818:Animals; D003167:Complement Activation; D003171:Complement Pathway, Classical; D003165:Complement System Proteins / Q000276:immunology*; D004533:Egtazic Acid / Q000494:pharmacology; D006168:Guinea Pigs; D006461:Hemolysis; D007104:Immune Adherence Reaction; D007770:L-Lactate Dehydrogenase / Q000378:metabolism; D010974:Platelet Aggregation; D011817:Rabbits; D012413:Rubidium / Q000378:metabolism; D014373:Tuberculin / Q000276:immunology*
D014373:Tuberculin; D004533:Egtazic Acid; D003165:Complement System Proteins; D007770:L-Lactate Dehydrogenase; D012413:Rubidium