Platelet thrombospondin haemagglutinin activity is due to aggregate formation

Abstract

Thrombospondin released from human blood platelets by thrombin activation formed high molecular weight aggregates which co-eluted with haemagglutinin activity on Sepharose 4B gel filtration. Thrombospondin aggregation was mediated by intermolecular disulphide bridges. The aggregates consisted of a series of oligomers ranging from a dimer to polymeric forms with Mr congruent to 40 X 10(6). Native monomeric thrombospondin obtained by a modified procedure was deficient in haemagglutination activity but inhibited haemagglutination induced by aggregated thrombospondin.