Monoclonal Antibody to Human Platelet Glycoprotein I II. EFFECTS ON HUMAN PLATELET FUNCTION

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Abstract
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. 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. Platelet membrane glycoprotein I apparently 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 presence of the antibody. Platelet membrane glycoprotein I could, thus, be a binding site for factor VIII/von Willebrand factor to allow platelet adhesion to subendothelium.