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Thromb Haemost 1998; 80(04): 610-614
DOI: 10.1055/s-0037-1615431
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Characterization of β2-Glycoprotein I Binding to Phospholipid Membranes

Mark F. Harper
1   From the Division of Rheumatology and Immunology, Department of Medicine
,
Peter M. Hayes
1   From the Division of Rheumatology and Immunology, Department of Medicine
,
Barry R. Lentz
2   From the Department of Biochemistry and Biophysics, The University of North Carolina at Chapel Hill, Chapel Hill, NC, USA
,
Robert A. S. Roubey
1   From the Division of Rheumatology and Immunology, Department of Medicine
› Author Affiliations
Further Information

Publication History

Received 20 August 1996

Accepted after revision 05 June 1998

Publication Date:
08 December 2017 (online)

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Summary

The plasma protein β2-glycoprotein I (β2-GPI) is a major target of autoantibodies in patients with the antiphospholipid syndrome. To understand the physiological function of β2-GPI and its potential role in the pathophysiology of the antiphospholipid syndrome, the binding of β2-GPI to phospholipid membranes was characterized. The interaction of β2-GPI with unilamellar vesicles containing varying amounts of acidic phospholipids with phosphatidylcholine (PC) was measured at equilibrium via relative light scattering. Analysis of binding isotherms gave apparent Kd values ranging from approximately 5.0 to 0.5 μM over a range of 5-20 mol % anionic phospholipid. Inhibition of binding by increasing ionic strength and Ca2+ ions suggests that binding is primarily electrostatic. These data indicate that β2-GPI binding to membranes with physiological anionic phospholipid content is relatively weak in comparison to plasma coagulation proteins, suggesting that β2-GPI does not function as a physiological anticoagulant based on its phospholipid-binding properties.

 

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