Recombinant domain V of β2-glycoprotein I inhibits the formation of a 7-ketocholesteryl-9-carboxynonanoate and β2-glycoprotein I complex.
Recombinant domain V of β2-glycoprotein I inhibits the formation of a 7-ketocholesteryl-9-carboxynonanoate and β2-glycoprotein I complex.
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DOI：
10.1093/jb/mvq111
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发表时间：
2011
影响因子：
2.7
通讯作者：
Yingbiao Zhang;Wenzhe Li;Y. Chi;Ren-jun Wang;Dan-Bing Wang;Fan Zhang;Zhe Liu;E. Matsuura;Qing-ping Liu
中科院分区：
文献类型：
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作者：
Yingbiao Zhang;Wenzhe Li;Y. Chi;Ren-jun Wang;Dan-Bing Wang;Fan Zhang;Zhe Liu;E. Matsuura;Qing-ping Liu
我们先前的研究已经报道，氧化型低密度脂蛋白(OxLDL)/β(2)-糖蛋白I(β(2)-GPI)/自身抗体复合体的形成促进了抗磷脂综合征的过程。β(2)-GPI的结构域V与来自oxLDL的带负电荷的分子如7-酮基-9-羧氧基-9-壬酸酯(oxLig-1)结合，并介导oxLDL与β(2)-GPI之间的相互作用。本研究建立了oxLig-1/β(2)-GPI/抗β(2)-GPI-Ab(WB-CAL-1)模型。在大肠杆菌中表达的β(2)-GPI重组结构域V(rβ(2)-GPI DV)在酶联免疫分析中竞争性地抑制了β(2)-GPI与oxLig-1的相互作用。此外，重组β(2)-GPI DV可显著抑制APS患者体内oxLig-1/β(2)-GPI/自身抗体复合体的形成。本工作提出了一种新的可能性，即rβ(2)-GPI DV可用于抑制oxLDL/β(2)-GPI/自身抗体复合体的形成，并为开发新的治疗策略以防止APS的发生提供了线索。
Our prior study has been reported the formation of the oxidized low-density lipoprotein (oxLDL)/β(2)-glycoproteinI (β(2)-GPI)/autoantibody complex facilitated the antiphospholipid syndrome (APS) process. The domain V of β(2)-GPI binds to the negatively charged molecules, e.g. 7-ketochoresteryl-9-caboxynonanoate (oxLig-1) derived from the oxLDL and mediates the interaction between oxLDL and β(2)-GPI. In the present study, the oxLig-1/β(2)-GPI/anti-β(2)-GPI Ab (WB-CAL-1) model was established. The recombinant domain V of β(2)-GPI (rβ(2)-GPI DV) expressed in Escherichia coli competitively inhibits the interaction between β(2)-GPI and oxLig-1 in the enzyme-linked immunoassay. Moreover, the rβ(2)-GPI DV significantly inhibits the formation of the oxLig-1/β(2)-GPI/autoantibody complex in an APS patient. The present work suggests a novel possibility that rβ(2)-GPI DV could be used to inhibit the formation of oxLDL/β(2)-GPI/autoantibody complex, and give us a hint for the development of new therapeutic strategies to prevent the APS process.