Thrombospondin Plays a Role in Platelet–Platelet Recognition during Release-Related Aggregation

G. Agam, O. Shohat, A. Livne

Research output: Contribution to journalArticlepeer-review

5 Scopus citations

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 languageEnglish
Pages (from-to)482-486
Number of pages5
JournalExperimental Biology and Medicine
Volume177
Issue number3
DOIs
StatePublished - 1 Jan 1984

ASJC Scopus subject areas

  • General Biochemistry, Genetics and Molecular Biology

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