Fauvel-Lafève F, Legrand Y J
Unité 150 INSERM, Vaisseaux et Hémostase, URA 334 CNRS, Hôpital Saint-Louis, Paris, France.
Thromb Haemost. 1990 Aug 13;64(1):145-9.
We developed an ELISA test to measure the binding of plasma von Willebrand factor (vWF) to arterial microfibrils and compared this interaction to the binding of vWF to collagen under the same conditions. We found that vWF binds to microfibrils in a similar manner as it binds to collagen: the binding was independent of the presence of cations, and temperature of incubation and was displaced by 1 M NaCl. Using purified 125I-vWF we showed that the binding was saturable and could be displaced by cold vWF in excess. Using immunoblotting we showed that vWF binds to a 97 kDa protein present in the microfibrils different from the 128 kDa thrombospondin-like structure (GP 128) which in microfibrils is known to interact with blood platelets. These results indicate that in the subendothelium, microfibrils bind plasma vWF and this reinforces the thrombogenic role of these structures.
我们开发了一种酶联免疫吸附测定（ELISA）试验来检测血浆血管性血友病因子（vWF）与动脉微纤维的结合，并在相同条件下将这种相互作用与vWF和胶原蛋白的结合进行比较。我们发现，vWF与微纤维的结合方式与其与胶原蛋白的结合方式相似：这种结合不依赖于阳离子的存在、孵育温度，且可被1M氯化钠取代。使用纯化的125I-vWF，我们表明这种结合是可饱和的，并且可以被过量的冷vWF取代。通过免疫印迹法，我们表明vWF与微纤维中存在的一种97kDa蛋白质结合，该蛋白质不同于128kDa血小板反应蛋白样结构（GP 128），已知后者在微纤维中与血小板相互作用。这些结果表明，在内皮下，微纤维结合血浆vWF，这加强了这些结构的血栓形成作用。
