Olsen O H, Persson E
Haemostasis Biochemistry, Novo Nordisk A/S, Novo Nordisk Park, Måløv, Denmark.
Cell Mol Life Sci. 2008 Mar;65(6):953-63. doi: 10.1007/s00018-007-7480-5.
Coagulation factor VIIa (FVIIa) is an atypical member of the trypsin family of serine proteases. It fails to attain spontaneously its catalytically competent conformation and requires its protein cofactor tissue factor (TF) to accomplish this. Over a number of years, this unique behaviour of FVIIa has prompted investigations of the TF-induced activation mechanism and the zymogenicity determinants in factor VIIa. Factor VIIa has gained additional interest in the past decade because of its development into a clinically useful haemostatic agent. Here, we present an overview of the current knowledge about the TF-induced allosteric activation of FVIIa and the various molecular approaches to enhance the intrinsic activity and efficacy of FVIIa.
凝血因子VIIa（FVIIa）是丝氨酸蛋白酶胰蛋白酶家族的一个非典型成员。它不能自发地达到其具有催化活性的构象，需要其蛋白质辅因子组织因子（TF）来完成这一过程。多年来，FVIIa的这种独特行为促使人们对TF诱导的激活机制以及因子VIIa中的酶原性决定因素进行研究。在过去十年中，由于FVIIa发展成为一种临床上有用的止血剂，它引起了更多的关注。在这里，我们概述了目前关于TF诱导的FVIIa变构激活以及增强FVIIa内在活性和功效的各种分子方法的知识。
