Paper| Volume 26, ISSUE 6, P431-441, June 15, 1982

Effects of galactose-binding lectins on human blood platelets: Identity of the peanut agglutinin receptor with the von Willebrand factor receptor

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      Platelets washed in the presence of EDTA were treated with neuraminidase and resuspended in platelet-poor plasma, source of human von Willebrand factor (vWF) [denoted desialo-platelets]. Peanut agglutinin (PNA), soybean agglutinin (SBA) and Math Eq agglutinin (RCAI) induced agglutination of desialo-platelets down to concentrations of 25 μg/ml. Agglutination of platelets by ristocetin/vWF was not affected by removal of the terminal sialic acid. In subagglutinating concentrations, PNA inhibited the ristocetin-induced agglutination of desialo-platelets whereas SBA and RCAI were without effect. When platelets incubated in Ca2+-containing medium were desialylated and resuspended in platelet-poor plasma [denoted desialo-platelets preincubated with Ca2+], their agglutination with PNA and ristocetin was greatly impaired, SBA and RCAI reacted normally. These results indicate that PNA and ristocetin/vWF compete in binding to the same receptor. Since asialoglycoprotein Ib was shown earlier to be the only glycoprotein on desialo-platelets to bind to a PNA-Sepharose affinity column these results provide further evidence that glycoprotein Ib is the vWF receptor on human platelets and that the carbohydrate-rich outer part of glycoprotein Ib is an essential part of the receptor structure. Lectin-induced platelet agglutination can be mediated by structures other than glycoprotein Ib but lectins which interact with glycoprotein Ib induce strong platelet responses including secretion.


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