Human platelet surface binding of endogenous secreted factor VIII-von Willebrand factor and platelet factor 4.
Washed human platelets in buffers containing either 2 mM Ca++ or 4 mM EDTA were stimulated by human alpha-thrombin to induce secretion. The binding of two endogenous secreted proteins, factor-VIII-related protein (VIII-R) (von Willebrand factor) and platelet factor 4, was measured by reacting thrombin-treated and control platelets with specific antibodies to these proteins, then quantifying antibody binding with 125I-staphylococcal protein A. Both of these granule proteins were associated with the platelet membrane surface by a calcium-dependent mechanism after thrombin-induced secretion. This ability to bind endogenous secreted proteins to the plasma membrane surface may provide a mechanism by which the platelet can concentrate and organize its secreted proteins for subsequent physiologic reactions.
D001779:Blood Coagulation Factors; D001792:Blood Platelets / Q000378:metabolism*; D002462:Cell Membrane / Q000378:metabolism; D006801:Humans; D010978:Platelet Factor 4; D012711:Serum Albumin, Radio-Iodinated / Q000378:metabolism; D013205:Staphylococcal Protein A / Q000378:metabolism; D014841:von Willebrand Factor
D001779:Blood Coagulation Factors; D012711:Serum Albumin, Radio-Iodinated; D013205:Staphylococcal Protein A; D014841:von Willebrand Factor; D010978:Platelet Factor 4