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  • Title: Ligand interactions with the RGD recognition site alter binding of GPIIb-IIIa reactive monoclonal antibody to human platelets.
    Author: Marder P.
    Journal: Biochem Biophys Res Commun; 1993 Sep 15; 195(2):799-806. PubMed ID: 8373415.
    Abstract:
    A major component of thrombus formation is the activation of blood platelets and binding of soluble fibrinogen. Glycoprotein IIb-IIIa (GPIIb-IIIa) is the dominant receptor on platelets mediating this activity. This study describes how GPIIb-IIIa is differentially displayed on resting and activated human platelets and how this display is alternatively masked and enhanced by arginine-glycine-aspartic acid (RGD) containing or mimicking compounds. Results indicate that thrombin strongly increases GPIIb-IIIa display on platelet membrane surfaces while other platelet activators enhance GPIIb-IIIa display to lesser degrees. This upregulated display was masked by compounds RGDS, GPenGRGDSPCA and L-367,073. Conversely, membrane GPIIb-IIIa display was markedly enhanced on otherwise resting platelets by incubation with these same compounds. This study indicates that small ligands that bind to RGD recognition sites can modulate GPIIb-IIIa membrane surface display differentially, depending on the nature of their cellular targets.
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