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The effect on platelet function of a monoclonal platelet antibody to platelet membrane glycoprotein I was tested. This antibody, AN51, inhibited ristocetin or bovine factor VIII-induced aggregation but did not modify ADP, collagen type I or type III, thrombin or arachidonic acid induced aggregations. Furthermore, the adhesion-aggregation of platelets induced by microfibrils was also inhibited by the antibody. Platelet adhesion to rabbit aorta subendothelium was impaired by the antibody. The persistent adhesion of platelets to collagenase-treated subendothelium was also inhibited. These findings strongly suggested that platelet membrane glycoprotein I could interact with a non-collagenic microfibrillar component of subendothelium. The binding of factor VIII/von Willebrand factor to platelet membrane in the presence of ristocetin was decreased in the binding site for factor VIII/von Willebrand factor to allow platelet adhesion to subendothelium.


Journal article


Br J Haematol

Publication Date





511 - 519


Antibodies, Monoclonal, Antigen-Antibody Reactions, Blood Platelets, Cytoskeleton, Factor VIII, Glycoproteins, Humans, Immunoglobulin G, In Vitro Techniques, Platelet Adhesiveness, Platelet Aggregation, Ristocetin, von Willebrand Factor