Phosphatidylethanolamine incorporation into vesicles selectively enhances factor Va inactivation by activated protein C.
Phosphatidylethanolamine incorporation into vesicles selectively enhances factor Va inactivation by activated protein C.
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DOI：
10.1016/s0021-9258(17)42183-1
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发表时间：
1994-01
期刊：
影响因子：
--
通讯作者：
M. Smirnov;C. Esmon
中科院分区：
文献类型：
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作者：
M. Smirnov;C. Esmon
膜表面通过活化的蛋白C加速因子Va的蛋白水解失活。在大多数凝血复合物中，最具活性的膜磷脂被认为是磷脂酰丝氨酸。在这项研究中，我们表明，与磷脂酰丝氨酸含有囊泡，磷脂酰乙醇胺的掺入增加了约10倍的因子Va的灭活率在所有浓度的因子Va研究和在所有囊泡浓度或低于凝血酶原激活的最佳。相比之下，磷脂酰乙醇胺对凝血酶原激活的影响很小。磷脂酰乙醇胺是囊泡的关键成分，使囊泡在血浆中最佳地支持活化的蛋白C抗凝活性。这些结果表明，不同的凝血/抗凝复合物的膜要求的差异比以前认识到的更多。
Membrane surfaces accelerate the proteolytic inactivation of factor Va by activated protein C. In most coagulation complexes, the most active membrane phospholipid is believed to be phosphatidylserine. In this study, we demonstrate that with phosphatidylserine-containing vesicles, incorporation of phosphatidylethanolamine increased the rate of factor Va inactivation approximately 10-fold at all concentrations of factor Va studied and at all vesicle concentrations at or below the optimum for prothrombin activation. In contrast, phosphatidylethanolamine had very little influence on prothrombin activation. Phosphatidylethanolamine was a critical component of vesicles for the vesicles to support activated protein C anticoagulant activity optimally in plasma. These results demonstrate that the membrane requirements for the different coagulation/anticoagulation complexes differ much more than previously appreciated.