ASP514 within the A1 domain of bovine von Willebrand factor is required for interaction with platelet glycoprotein Ib.
ASP514 within the A1 domain of bovine von Willebrand factor is required for interaction with platelet glycoprotein Ib.
复制标题
牛血管性血友病因子 A1 结构域内的 ASP514 是与血小板糖蛋白 Ib 相互作用所必需的。
DOI：
10.1006/bbrc.1994.2265
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发表时间：
1994
影响因子：
3.1
通讯作者：
Budzynski,AZ
中科院分区：
文献类型：
--
作者：
Sinha,D;Bakhshi,M;Kunapuli,S;Vora,R;Gabriel,JL;Kirby,EP;Budzynski,AZ
将含有牛血管性血友病因子（vWF）A1区Leu 469-Ser 723 Of的重组片段PAD-1突变体PAD-1（D514→Q），既不抑制[125 I]vWF与血小板的结合，也不抑制VWF诱导的人血小板凝集。另一方面，PAD-1抑制由牛VWF和[125 I]vWF与人血小板结合诱导的人血小板凝集。然而，突变体的胶原结合特性与PAD-1的胶原结合特性没有区别。这些结果表明，vWF A1区的Asp 514是vWF与人血小板GPIb受体相互作用所必需的。
A mutant PAD-1(D514→Q) of the recombinant fragment PAD-1 comprising Leu469-Ser723Of the A1 domain of bovine von Willebrand factor (vWF) neither inhibited the binding of [125I]vWF to platelets nor the agglutination of human platelets induced by bovine VWF. PAD-1, on the other hand, inhibited human platelet agglutination induced by bovine VWF and [125I]vWF binding to human platelets. Collagen binding properties of the mutant, however, were indistinguishable from those of PAD-1. These results suggested that Asp514within the A1 domain of vWF is required for interaction of bovine vWF with GPIb receptor on human platelets.