Thromb Haemost 1984; 52(03): 354-357
DOI: 10.1055/s-0038-1661213
Original Article
Schattauer GmbH Stuttgart

Effect of Anti-Thrombospondin Antibodies on the Hemagglutination Activities of the Endogenous Platelet Lectin and Thrombospondin

T Kent Gartner
The Department of Biology, Memphis State University Memphis, TN, USA, and the Department of Medicine, University of Wisconsin-Madison, Madison, WI, USA
,
Mary Jean Doyle
The Department of Biology, Memphis State University Memphis, TN, USA, and the Department of Medicine, University of Wisconsin-Madison, Madison, WI, USA
,
Deane F Mosher
The Department of Biology, Memphis State University Memphis, TN, USA, and the Department of Medicine, University of Wisconsin-Madison, Madison, WI, USA
› Author Affiliations
Further Information

Publication History

Received 22 August 1984

Accepted 25 September 1984

Publication Date:
19 July 2018 (online)

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Summary

The proposal that thrombospondin is the endogenous platelet lectin was evaluated using antisera and monoclonal antibodies to thrombospondin. The platelet-bound hemagglutinin activity of human platelets stimulated with A23187 was inhibited by rabbit anti-thrombospondin sera and by a monoclonal anti-thrombospondin IgG. A second monoclonal IgG did not inhibit platelet- bound agglutinin activity. Preparations of purified platelet thrombospondin differed in their hemagglutination activities. The hemagglutination activity of an active preparation of thrombospondin was inhibited by the monoclonal antibody that inhibited platelet-bound lectin activity. The hemagglutination activity of an almost inactive preparation of thrombospondin was enhanced by the anti-thrombospondin monoclonal antibody that did not block platelet-bound lectin activity. The results demonstrate that expression of the platelet-bound form of the endogenous lectin is thrombospondin-dependent and suggest that thrombospondin must become part of a larger complex, either by binding to the platelet surface or by becoming aggregated in solution, before hemagglutination activity can be expressed.