Endenburg S C, Hantgan R R, Sixma J J, de Groot P G, Zwaginga J J
Department of Haematology, University Hospital Utrecht, The Netherlands.
Blood Coagul Fibrinolysis. 1993 Feb;4(1):139-42.
We have found that glycoprotein IIb:IIIa (GPIIb:IIIa) expressed on nonstimulated platelets is the primary receptor for platelet adhesion to immobilized fibrinogen or fibrin. At low shear rates of the blood the interaction between GPIIb:IIIa and fibrin(ogen) is strong enough to resist the shear forces exerted on the platelet as was shown with experiments with antibodies against platelet membrane glycoproteins and perfusion studies with blood from patients lacking platelet membrane receptors. Impaired platelet adhesion to fibrin(ogen) was found with blood from a patient with Glanzmann's thrombasthenia (lacking GPIIb:IIIa), blood from patients with the Bernard-Soulier syndrome (lacking GPIb) and blood from patients with severe von Willebrand's disease. This indicates that at higher shear rates additional interactions via GPIb on the platelet and von Willebrand factor originating from plasma or platelets are necessary to increase the affinity of the platelet for fibrin(ogen).
我们发现，未受刺激的血小板上表达的糖蛋白IIb:IIIa（GPIIb:IIIa）是血小板黏附于固定化纤维蛋白原或纤维蛋白的主要受体。在血液的低剪切速率下，GPIIb:IIIa与纤维蛋白（原）之间的相互作用足够强，能够抵抗施加在血小板上的剪切力，这已通过针对血小板膜糖蛋白的抗体实验以及对缺乏血小板膜受体患者的血液进行灌注研究得到证实。在患有Glanzmann血小板无力症（缺乏GPIIb:IIIa）的患者血液、患有Bernard-Soulier综合征（缺乏GPIb）的患者血液以及患有严重血管性血友病的患者血液中，均发现血小板对纤维蛋白（原）的黏附受损。这表明，在较高剪切速率下，血小板上的GPIb与源自血浆或血小板的血管性血友病因子之间的额外相互作用对于增加血小板对纤维蛋白（原）的亲和力是必要的。
