VONWILLEBRAND PROTEIN FACILITATES PLATELET INCORPORATION IN POLYMERIZING FIBRIN
VONWILLEBRAND PROTEIN FACILITATES PLATELET INCORPORATION IN POLYMERIZING FIBRIN
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DOI：
10.1172/jci112668
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发表时间：
1986-10-01
影响因子：
15.9
通讯作者：
HANDIN, RI
中科院分区：
文献类型：
--
作者：
LOSCALZO, J;INBAL, A;HANDIN, RI
发现vonWillebrand蛋白促进血小板结合到形成的纤维蛋白血栓中。使用福尔马林处理的或新鲜的血小板，血小板掺入聚合纤维蛋白的初始速率和程度都依赖于血管性血友病蛋白。vonWillebrand蛋白与血小板平行地掺入到形成的纤维蛋白血栓中。与丙烯腈珠（Matrex 102）共价连接的可溶性纤维蛋白单体以15 μ g/ml的表观近似解离常数（KD）特异性且饱和地结合von Willebrand蛋白。在该系统中，糖蛋白Ib的水溶性蛋白水解片段Glycocalicin也特异性地和饱和地与纤维蛋白单体结合，表观KD约为5 μ g/ml，但仅在饱和浓度的von Willebrand蛋白存在下。这些数据表明：（a）血小板掺入形成的纤维蛋白血栓的初始速率和程度依赖于血管性血友病蛋白;（B）血管性血友病蛋白作为聚合纤维蛋白和血小板表面糖蛋白Ib之间的连接物;和（c）血管性血友病蛋白与纤维蛋白单体结合，从而能够在没有利托那肽的情况下与血小板表面糖蛋白Ib结合。
von Willebrand protein was found to promote the incorporation of platelets into evolving fibrin thrombi. Using formalin-treated or fresh platelets, both the initial rate and extent of platelet incorporation into polymerizing fibrin were dependent on von Willebrand protein. von Willebrand protein was incorporated into evolving fibrin thrombi in parallel with platelets. Soluble fibrin monomer covalently linked to acrylonitrile beads (Matrex 102) bound von Willebrand protein specifically and saturably with an apparent approximate dissociation constant (KD) of 15 .mu.g/ml. Glycocalicin, the water-soluble proteolytic fragment of glycoprotein Ib, bound to fibrin monomer in this system specifically and saturably, as well, with an apparent approximate KD of 5 .mu.g/ml, but only in the presence of saturating concentrations of von Willebrand protein. These data demonstrate that (a) the initial rate and extent of platelet incorporation into evolving fibrin thrombi are dependent on von Willebrand protein; (b) von Willebrand protein serves as a link between polymerizing fibrin and platelet surface glycoprotein Ib; and (c) von Willebrand protein binds to fibrin monomer and is thereby able to bind to platelet surface glycoprotein Ib in the absence of ristocetin.