Key result
Purified thrombospondin reconstituted the interaction of fresh platelets with fixed platelets, and anti-TSP antibodies abolished this effect, indicating TSP's role in platelet-platelet recognition.
Thrombospondin is identified as a key molecule in the mechanism of platelet-platelet recognition during release-related aggregation.
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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.
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TSP may mediate platelet aggregation in experimental models; leaves open human therapeutic relevance pending clinical studies.
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Agam et al. (1984) studied Platelet aggregation. Purified thrombospondin (TSP) and anti-TSP antibodies was evaluated on Platelet-platelet recognition during release-related aggregation. Purified thrombospondin reconstituted the interaction of fresh platelets with fixed platelets, and anti-TSP antibodies abolished this effect, indicating TSP's role in platelet-platelet recognition.
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