Characterization of β2-Glycoprotein I Binding to Phospholipid Membranes

Mark F. Harper; Peter M. Hayes; Barry R. Lentz; Robert A. S. Roubey

doi:10.1055/s-0037-1615431

Thrombosis and Haemostasis, Inhaltsverzeichnis

Thromb Haemost 1998; 80(04): 610-614
DOI: 10.1055/s-0037-1615431

Rapid Communication

Schattauer GmbH

Characterization of β₂-Glycoprotein I Binding to Phospholipid Membranes

Mark F. Harper

¹From the Division of Rheumatology and Immunology, Department of Medicine

,

Peter M. Hayes

¹From the Division of Rheumatology and Immunology, Department of Medicine

,

Barry R. Lentz

²From the Department of Biochemistry and Biophysics, The University of North Carolina at Chapel Hill, Chapel Hill, NC, USA

,

Robert A. S. Roubey

¹From the Division of Rheumatology and Immunology, Department of Medicine

› Institutsangaben

Abstract

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 K_d 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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