作者: G. TOBELEM , S. LEVY-TOLEDANO , R. BREDOUX , H. MICHEL , A. NURDEN
DOI: 10.1038/263427A0
关键词: Cell biology 、 Platelet adhesiveness 、 Adenosine diphosphate 、 In vitro 、 Adhesion 、 Endothelium 、 Chemistry 、 Ristocetin 、 Platelet 、 Glycoprotein
摘要: IT has been suggested that the layer of bound carbohydrate on surface a platelet contains groupings vital to haemostatic function platelet1. This role is largely dependent ability adhere exposed subendothelial components in event vessel damage2. Platelet aggregation, induced by bovine factor VIII and ristocetin, adhesion subendothelium are impaired Bernard–Soulier syndrome, while aggregation ADP apparently normal3,4. A gross abnormality 155,000-molecular weight glycoprotein seen membrane fractions prepared from platelets this syndrome5 suggests acts as an acceptor–receptor during interation with macromolecular aggregation-inducing agents. Here we report further evidence specific site required for ristocetin induce when inhibited acquired antiplatelet antibody found polytransfused patient. vitro, normal human platelets, Bernard–Soulier-like defect, so was defective, ADP-mediated unaffected.