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.
| Original language | English |
|---|---|
| Pages (from-to) | 482-486 |
| Number of pages | 5 |
| Journal | Experimental Biology and Medicine |
| Volume | 177 |
| Issue number | 3 |
| DOIs | |
| State | Published - 1 Jan 1984 |
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology (all)