Self-interaction of soluble and surface-bound β2-glycoprotein I and its enhancement by lupus anticoagulants

Akira Hayashi, Ayumi Hayashi, Eiji Matsuura, Koji Suzuki, Takao Koike, Eikichi Hashimoto, Hiroyuki Takeya

Research output: Contribution to journalArticlepeer-review

2 Citations (Scopus)

Abstract

Antiphospholipid antibodies found in antiphospholipid syndrome are autoantibodies to phospholipid-binding proteins, such as β2-glycoprotein I (β2GPI). We have previously reported that among these antibodies, the so-called lupus anticoagulants (LAs) augment β2GPI binding to the phospholipid membrane surface, which is associated with the pathological action of LAs. However, the molecular mechanisms underlying this augmentation are uncertain. Here we show that β2GPI, which is monomeric in solution, self-interacts at the interface of soluble and surface-bound molecules. In addition, this self-interaction is enhanced by LA-positive, but not LA-negative, anti-β2GPI monoclonal antibodies. This study suggests that β2GPI self-interaction upon surface binding could be involved in the LA-induced potentiation of β2GPI binding to the phospholipid surface. Structured summary: MINT-6743767:beta2GPI (uniprotkb:P02749) binds (MI:0407) to beta2GPI (uniprotkb:P02749) by surface plasmon resonance (MI:0107)MINT-6743776:beta2GPI (uniprotkb:P02749) binds (MI:0407) to beta2GPI (uniprotkb:P02749) by saturation binding (MI:0440).

Original languageEnglish
Pages (from-to)3308-3312
Number of pages5
JournalFEBS Letters
Volume582
Issue number23-24
DOIs
Publication statusPublished - Oct 15 2008

Keywords

  • Antiphospholipid
  • Cardiolipin
  • Lupus anticoagulant
  • Phosphatidylserine
  • Surface plasmon resonance
  • β-Glycoprotein I

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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