重组因子 VIIa 与血小板糖蛋白 Ib 的相互作用。

The interaction of recombinant factor VIIa with platelet glycoprotein Ib.

机构信息

Surgical Research Laboratory, Department of Surgery, University Medical Center Groningen, University of Groningen, Groningen, The Netherlands.

出版信息

Thromb Res. 2010 Apr;125 Suppl 1:S13-5. doi: 10.1016/j.thromres.2010.01.024. Epub 2010 Feb 11.

DOI:10.1016/j.thromres.2010.01.024

PMID:20153024

Abstract

Recombinant factor VIIa (rFVIIa) exerts potent prohemostatic activities via both tissue factor-dependent and -independent mechanisms. Tissue factor-independent enhancement of hemostasis involves a direct interaction of rFVIIa with the activated platelet membrane resulting in factor X activation. We have recently shown that rFVIIa binds to the platelet glycoprotein Ib/IX/V complex in addition to the negatively charged membrane surface. This interaction appears to slightly enhance tissue factor-independent thrombin generation. These findings add to our understanding of the mechanism of action of rFVIIa and may lead to improved therapeutic use of the drug.

摘要

重组凝血因子 VIIa（rFVIIa）通过组织因子依赖和非依赖机制发挥强大的促止血作用。非依赖组织因子的止血增强作用涉及 rFVIIa 与激活的血小板膜的直接相互作用，导致因子 X 的激活。我们最近表明，rFVIIa 除了带负电荷的膜表面之外，还与血小板糖蛋白 Ib/IX/V 复合物结合。这种相互作用似乎略微增强了非依赖组织因子的凝血酶生成。这些发现增加了我们对 rFVIIa 作用机制的理解，并可能导致该药物的治疗用途得到改善。