Atsumi Tatsuya, Amengual Olga, Yasuda Shinsuke, Matsuura Eiji, Koike Takao
Department of Medicine II, Hokkaido University Graduate School of Medicine, Sapporo, Japan.
Autoimmunity. 2005 Aug;38(5):377-81. doi: 10.1080/08916930500124312.
Beta2-glycoprotein I (beta2GPI), a phospholipid-binding protein, is one of the major target antigens for antiphospholipid antibodies (aPL) found in patients with antiphospholipid syndrome (APS). Thrombophilic disorders in APS patients are strongly associated with aPL, and their pathogenic properties depend on the presence of beta2GPI. Procoagulant cell stimulation by aPL, via beta2GPI, is one of the most plausible mechanisms of thrombosis in APS, and p38 mitogen activated protein kinase (MAPK) pathway plays a crucial role in such activation. beta2GPI is proteolytically cleaved in domain V by activated factor X or plasmin, leading to the generation of the nicked form of beta2GPI. Recently, increasing attention is focused on the role of nicked-beta2GPI as a regulator of extrinsic fibrinolysis pathway.
β2糖蛋白I（β2GPI）是一种磷脂结合蛋白，是抗磷脂综合征（APS）患者体内发现的抗磷脂抗体（aPL）的主要靶抗原之一。APS患者的血栓形成倾向疾病与aPL密切相关，其致病特性取决于β2GPI的存在。aPL通过β2GPI对促凝细胞的刺激是APS中最可能的血栓形成机制之一，p38丝裂原活化蛋白激酶（MAPK）途径在这种激活中起关键作用。β2GPI在结构域V被活化的因子X或纤溶酶进行蛋白水解切割，导致产生带切口形式的β2GPI。最近，人们越来越关注带切口的β2GPI作为外源性纤维蛋白溶解途径调节剂的作用。
