Previous studies have shown that oxidized low-density lipoprotein (LDL) induces platelet activation more effectively than native LDL. To achieve a better understanding of the mechanism underlying the activation of human platelets by oxidized LDL, the present study relates the effect of oxidized LDL to changes of binding characteristics for glycoprotein (GP) IIb-IIIa. Washed human platelets were treated by monoclonal antibody against GP IIb-IIIa, and the ligand-receptor complexes were revealed by immunocytochemical techniques on the ultrastructural level. The localization of the antiglycoprotein IIb-IIIa was time-dependent. After binding to the platelet surface membrane and open canalicular system, the surface-membrane labeling decreased during longer incubation periods. Preincubation with oxidized LDL inhibited the binding of antiglycoprotein IIb-IIIa. Our findings suggest that GP IIb-IIIa acts as a receptor for oxidized LDL. The binding of oxidized LDL to the GP IIb-IIIa might be the first step in platelet activation by plasma lipoproteins.
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