Rheumatology Advance Access published online on July 4, 2006
Rheumatology, doi:10.1093/rheumatology/kel200
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1 Department of Rheumatology, University Medical Centre, University of Ljubljana, Ljubljana, Slovenia
* To whom correspondence should be addressed. Objectives. Anti-phospholipid antibodies have been recognized to play a role in vascular thrombosis and pregnancy morbidity. They were first thought to be directed to phospholipids, but it is now known that the majority of pathogenic antibodies recognizes epitopes on phospholipid-binding plasma proteins such as Methods. Giant phospholipid vesicles (GPVs) were used as a simple model of the membrane surface. GPVs composed of phosphatidylserine and phosphatidylcholine were produced in an aqueous medium. A single GPV was transferred to the solution containing ANXA5 conjugated with Alexa Fluor 488 (FANXA5) and (i) aANXA5 or a Results. Conclusions. Our results point to the competition between FANXA5 and complexes of
Received January 25, 2006
Accepted May 9, 2006
Original Papers
Annexin A5 binding to giant phospholipid vesicles is differentially affected by anti-
N. Ga
2-glycoprotein I and anti-annexin A5 antibodies
peri
1 *,
A. Ambro
i 1,
B. Boi 1,
J. Majhenc 2,
S. Svetina 2,
and
B. Rozman 1
2 Institute of Biophysics, School of Medicine, University of Ljubljana, Ljubljana, Slovenia
N. Gaperi, E-mail: ngaspersic{at}yahoo.com
Abstract 
2-glycoprotein I (2GPI) or possibly also annexin A5 (ANXA5). The mechanism of their prothrombotic action is still not completely understood. The aim of the present study was to observe the effect of antibodies against ANXA5 (aANXA5) and antibodies against 2GPI (a2GPI) on the binding of ANXA5 to the negatively charged phospholipid membrane.2GPI and (ii) different concentrations of a2GPI together with 2GPI. The emission of the fluorescent light from the GPV surface, as the result of FANXA5 binding, was measured.2GPI together with a2GPI reduced the binding of FANXA5 to GPVs. On the contrary, aANXA5 enhanced the binding of ANXA5 to the GPV surface.2GPI-a2GPI for the same binding sites and therefore support the hypothesis of the disruption of the ANXA5 protective shield on procoagulant phospholipid surface. The influence of increased cell surface ANXA5 concentration in the presence of aANXA5 on coagulation needs to be further studied.2-glycoprotein I; Giant phospholipid vesicles.
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