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重新审视β2糖蛋白I,抗磷脂综合征中的主要自身抗原。

Revisiting beta 2 glycoprotein I, the major autoantigen in the antiphospholipid syndrome.

作者信息

Rahgozar Soheila

机构信息

Division of Cell, Molecular and Developmental Biology, Department of Biology, Faculty of Science, University of Isfahan, Isfahan, Iran, e-mail:

出版信息

Iran J Immunol. 2012 Jun;9(2):73-85.

PMID:22735795
Abstract

Beta 2 glycoprotein I (β2GPI) is a single chain 50 kDa highly glycosylated glycoprotein at an approximate concentration of 4 μM in cells. The abundance of this protein in plasma and its high state of preservation indicate the important role of this protein in mammalians. In addition, β2GPI has a particular structure in the fifth domain, and is categorized as the major antigen recognized by autoantibodies present in antiphospholipid syndrome. Beta 2 glycoprotein I has been usually studied in the context of antiphospholipid antibody production. Complexes of β2GPI/anti-β2GPI antibodies have been examined in different coagulation and cell activation pathways. However, the function of β2GPI, independent from the antibodies, has not been clearly determined. In this paper different features of β2GPI including its structure, plasma concentration and its proposed in vitro and in vivo functions in clot formation and fibrinolysis along with anti-β2GPI antibodies (Abs) are discussed. Their inhibitory or promotive effects are delineated in each facet.

摘要

β2糖蛋白I(β2GPI)是一种单链50 kDa的高度糖基化糖蛋白,在细胞中的浓度约为4 μM。这种蛋白质在血浆中的丰度及其高度保守的状态表明了它在哺乳动物中的重要作用。此外,β2GPI在第五结构域具有特殊结构,被归类为抗磷脂综合征中自身抗体识别的主要抗原。β2糖蛋白I通常在抗磷脂抗体产生的背景下进行研究。β2GPI/抗β2GPI抗体复合物已在不同的凝血和细胞激活途径中进行了检测。然而,β2GPI独立于抗体的功能尚未明确确定。本文讨论了β2GPI的不同特征,包括其结构、血浆浓度及其在体外和体内在凝血和纤维蛋白溶解中的假定功能,以及抗β2GPI抗体(Abs)。在每个方面都描述了它们的抑制或促进作用。

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Protective Effects of Reduced Beta 2 Glycoprotein I on Liver Injury in Streptozotocin (STZ)-Diabetic Rats by Activation of AMP-Activated Protein Kinase.还原型β 2 糖蛋白 I 通过激活 AMP 激活的蛋白激酶对链脲佐菌素(STZ)-糖尿病大鼠肝损伤的保护作用。
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Reduced beta 2 glycoprotein I prevents high glucose-induced cell death in HUVECs through miR-21/PTEN.
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Am J Transl Res. 2017 Sep 15;9(9):3935-3949. eCollection 2017.
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