Abstract
Abstract
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 μM ADP to interact with the fixed platelets. A supernatant fraction from fresh platelets activated by 10 μM 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.
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