Kobayashi I, Lamme S, Nilsson I M
Thromb Res. 1984 Jul 1;35(1):65-75. doi: 10.1016/0049-3848(84)90313-x.
The interaction of factor VIII with phospholipids was investigated in 11 patients with mild and moderate hemophilia A, 7 patients with von Willebrand's disease and in 10 healthy people as controls. The addition of phospholipid vesicles containing phosphatidylserine and phosphatidylethanolamine to normal plasma and that of patients with von Willebrand's disease resulted in the loss of almost two thirds of the factor VIII clotting antigen (VIII:CAg) measurable by IRMA. Defective interaction of phospholipids with VIII:CAg was noted in some genetic variants of mild and moderate hemophilia A. Thus four of the five families tested showed decreased binding of VIII:CAg to phospholipids. One of the families tested belonged to a genetic variant with much more VIII:CAg than VIII:C, and it was in members of this family that the binding capacity was most reduced. The most probable explanations for the defective interaction with phospholipids is that molecular defects of VIII:CAg result in either decreased binding to phospholipids or might lead to a stronger binding between VIII:CAg and the von Willebrand factor (VIIIR:Ag) in the factor VIII complex and thereby preventing the normal separation of the complex.
在11例轻度和中度甲型血友病患者、7例血管性血友病患者以及10名健康对照者中研究了因子VIII与磷脂的相互作用。向正常血浆以及血管性血友病患者的血浆中添加含有磷脂酰丝氨酸和磷脂酰乙醇胺的磷脂囊泡,导致通过免疫放射分析(IRMA)检测到的因子VIII凝血抗原(VIII:CAg)几乎损失三分之二。在轻度和中度甲型血友病的一些遗传变异型中,发现磷脂与VIII:CAg的相互作用存在缺陷。因此,所检测的5个家族中有4个家族显示VIII:CAg与磷脂的结合减少。所检测的一个家族属于一种遗传变异型,其VIII:CAg比VIII:C多得多,正是在这个家族的成员中,结合能力降低最为明显。与磷脂相互作用存在缺陷的最可能解释是,VIII:CAg的分子缺陷导致与磷脂的结合减少,或者可能导致因子VIII复合物中VIII:CAg与血管性血友病因子(VIIIR:Ag)之间的结合更强,从而阻止复合物的正常分离。