Preparation of monoclonal antibodies against glycoprotein IIIa of human platelets

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Abstract
Monoclonal antibodies against purified glycoprotein IIIa (GPIIIa) of human platelet membranes were obtained. These antibodies, except 1, are able to bind to intact platelets; the exception is M108/p98 antibody which recognizes a new epitope, unmasked after proteolysis of GPIIIa in vitro. Several antigenic areas can be delineated on the molecule by testing the ability of differnet antibodies to compete in their simultaneous binding to GPIIIa. One of the monoclonal antibodies inhibits ADP-induced platelet aggregation while others do not have an effect or induce agglutination of platelets independent of ADP. Conventional antiserum raised against purified GPIIIa also blocks the aggregation induced by ADP. GPIIIa apparently plays a direct role in the mechanism of platelet aggregation.