Recombinant domain v of β2-glycoprotein i inhibits the formation of a 7-ketocholesteryl-9-carboxynonanoate and β2- glycoprotein i complex

Yingbiao Zhang, Wenzhe Li, Yan Chi, Renjun Wang, Dan Wang, Fan Zhang, Zhe Liu, Eiji Matsuura, Qingping Liu

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

Our prior study has been reported the formation of the oxidized low-density lipoprotein (oxLDL)/β2-glycoproteinI (β2-GPI)/autoantibody complex facilitated the antiphospholipid syndrome (APS) process. The domain V of β2-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 β2-GPI. In the present study, the oxLig-1/β2-GPI/ anti-β2-GPI Ab (WB-CAL-1) model was established. The recombinant domain V of β2-GPI (rβ2-GPI DV) expressed in Escherichia coli competitively inhibits the interaction between β2-GPI and oxLig-1 in the enzyme-linked immunoassay. Moreover, the rβ2-GPI DV significantly inhibits the formation of the oxLig-1/β2-GPI/autoantibody complex in an APS patient. The present work suggests a novel possibility that rβ2-GPI DV could be used to inhibit the formation of oxLDL/β2-GPI/autoantibody complex, and give us a hint for the development of new therapeutic strategies to prevent the APS process.

Original languageEnglish
Pages (from-to)35-42
Number of pages8
JournalJournal of biochemistry
Volume149
Issue number1
DOIs
Publication statusPublished - Jan 2011

Keywords

  • Antiphospholipid syndrome
  • oxLDL
  • oxLig-1
  • β
  • β domain V

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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