Nieuwenhuis H K, Akkerman J W, Houdijk W P, Sixma J J
Nature. 1985;318(6045):470-2. doi: 10.1038/318470a0.
The interaction of blood platelets with collagen is generally considered to be of primary importance in the arrest of bleeding and to have a role in the pathogenesis of thrombosis and atherosclerosis. Following damage to the vascular endothelium, circulating platelets come into contact with exposed collagen fibrils in the subendothelium and spread along it; this is followed by the secretion of several biologically active substances and by aggregation of platelets. The glycoproteins of the platelet plasma membrane have an important role in the mechanisms underlying these processes. So far, two specific defects of platelet function in patients with a bleeding disorder are known to be associated with a glycoprotein defect and the study of these patients has contributed significantly to present concepts of platelet function. The glycoprotein (GP) IIB-III complex, absent or deleted in the aggregation-defective Glanzmann's thrombasthenia, has been identified as the platelet fibrinogen receptor. GPIb, which is absent in the adhesion-defective Bernard-Soulier syndrome, has been identified as the von Willebrand factor receptor on platelets. We now report a defect of the platelet plasma membrane glycoprotein composition in a patient whose platelets are totally unresponsive to collagen.
血小板与胶原蛋白的相互作用通常被认为在止血过程中至关重要，并且在血栓形成和动脉粥样硬化的发病机制中起作用。血管内皮受损后，循环中的血小板与内皮下暴露的胶原纤维接触并沿其铺展；随后会分泌几种生物活性物质并发生血小板聚集。血小板质膜糖蛋白在这些过程的潜在机制中起重要作用。到目前为止，已知出血性疾病患者的两种特定血小板功能缺陷与糖蛋白缺陷有关，对这些患者的研究为目前的血小板功能概念做出了重大贡献。在聚集缺陷型Glanzmann血小板无力症中缺失或缺失的糖蛋白（GP）IIb-III复合物已被确定为血小板纤维蛋白原受体。在黏附缺陷型Bernard-Soulier综合征中缺失的GPIb已被确定为血小板上的血管性血友病因子受体。我们现在报告一名患者的血小板质膜糖蛋白组成缺陷，该患者的血小板对胶原蛋白完全无反应。
