Secreted platelet thrombospondin binds monovalently to platelets and erythrocytes in the absence of free Ca2+.

Washed human platelets suspended in Ca2+-free buffer bind thrombospondin secreted in response to stimulation by the calcium ionophore A23187. Under these conditions, the secreted thrombospondin binds to the surface of the platelets monovalently, that is, the thrombospondin does not agglutinate the platelets. In addition, the secreted thrombospondin can bind monovalently to the surface of the erythrocytes used to assay the endogenous lectin of human platelets. These findings resolve the contradictions resulting from the apparent requirement for free Ca2+ in the binding of secreted thrombospondin to the plasma membranes of platelets, the behavior of purified thrombospondin in hemagglutination assays and the characteristics of the endogenous lectin (thrombospondin) expressed by platelets stimulated with A23187 or gamma-thrombin.