Anti-β2-glycoprotein I antibody: Specificity and clinical significance

T. Koike, E. Matsuura

Research output: Contribution to journalArticlepeer-review

25 Citations (Scopus)


Cardiolipin binding of IgG-class anticardiolipin antibody (aCL) depends on the existence of β2-glycoprotein I (β2-GPI). We developed an EIA system that enables detection of antibodies against β2-GPI, without the presence of cardiolipin. This system involves use of irradiated polystyrene plates, in which oxygen atoms are introduced onto the surfaces of the plates. β2-GPI bound to the surface of these plates is assumed to undergo a conformational change that exposes normally cryptic epitopes. Anti-β2-GPI antibody measured using this EIA system showed good correlation with aCL measured by conventional EIA methods and may prove useful in evaluating the risk of thrombosis and monitoring the clinical course in patients with SLE. Utilizing this EIA system and β2-GPI-deleted mutants, we found that the fourth domain of β2-GPI is involved in expression of one of the cryptic epitopes recognized by aCL. We also found that oxidized LDL are sequentially targeted by β2-GPI and aCL.

Original languageEnglish
Pages (from-to)378-380
Number of pages3
Issue number5
Publication statusPublished - 1996
Externally publishedYes


  • Anti-β-glycoprotein I antibody
  • Anticardiolipin antibody
  • β-glycoprotein I

ASJC Scopus subject areas

  • Rheumatology


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