Interaction of thrombin with mammalian platelets.
In this study we have explored the interaction of thrombin with platelets from human and rat. Compared to human platelets, rat platelets suspended in plasma required a higher concentration of thrombin for aggregation. This difference in sensitivity to thrombin was maintained when platelets were washed and suspended in buffer. Platelets from both mammals bound thrombin and showed a similar number of binding sites. However, the apparent dissociation constant of thrombin binding for rat platelets was approximately 15-fold higher than that for human. Thus, the decreased aggregation response of rat platelets may be due to a reduced binding of thrombin to its receptor. It is known that the thrombin receptor is located on the platelet surface. Gel electrophoresis of platelets followed by specific staining as well as fluorography showed significant differences in the surface glycoproteins of human and rat platelets. Human platelets showed labeled components corresponding to 210,000 and 160,000 daltons, whereas rat platelets showed glycoproteins with molecular weights of 240,000 and 190,000. A 135,000-dalton component was present in platelets from both sources. These results suggest that either or both glycoproteins of 210,000 and 160,000 daltons may be involved in the interaction of thrombin with human platelets.
D000818:Animals; D001792:Blood Platelets / Q000378:metabolism* / Q000502:physiology; D004305:Dose-Response Relationship, Drug; D006023:Glycoproteins / Q000378:metabolism; D006801:Humans; D008565:Membrane Proteins / Q000378:metabolism; D010974:Platelet Aggregation / Q000187:drug effects; D051381:Rats; D013045:Species Specificity; D013917:Thrombin / Q000378:metabolism* / Q000494:pharmacology
D006023:Glycoproteins; D008565:Membrane Proteins; D013917:Thrombin