Thrombospondin plays a role in platelet-platelet recognition during release-related aggregation.
Fixed platelets, bearing covalently bound fibrinogen, participate passively in aggregation of fresh platelets when the aggregation process is release related (G. Agam and A. Livne, Thromb Haemostasis 51:145-149, 1984). Inhibition of the release by aspirin abolishes the capability of the fresh platelets activated by 10 microM ADP to interact with the fixed platelets. A supernatant fraction from fresh platelets activated by 10 microM ADP (releasate) reconstitutes the interaction. Purified thrombospondin (TSP) replaces the releasate. Moreover, anti-TSP antibodies abolish the reconstituting effect of the releasate. It is concluded that TSP plays a role in the molecular mechanism of platelet-platelet recognition during release-related aggregation.
D000244:Adenosine Diphosphate / Q000494:pharmacology; D000911:Antibodies, Monoclonal; D001241:Aspirin / Q000494:pharmacology; D005340:Fibrinogen / Q000502:physiology; D006023:Glycoproteins / Q000276:immunology / Q000494:pharmacology / Q000502:physiology*; D006801:Humans; D007106:Immune Sera / Q000494:pharmacology; D010974:Platelet Aggregation / Q000187:drug effects; D019699:Thrombospondins
D000911:Antibodies, Monoclonal; D006023:Glycoproteins; D007106:Immune Sera; D019699:Thrombospondins; D000244:Adenosine Diphosphate; D005340:Fibrinogen; D001241:Aspirin