Coalescence of phospholipid membranes as a possible origin of anticoagulant effect of serum proteins

Interactions between phospholipid membranes (made of palmitoyloleoylphosphatidylcholine, cardiolipin and cholesterol) after addition of β2 glycoprotein I (β2GPI) or anti-β2GPI antibodies or a mixture of both were studied by observing giant phospholipid vesicles under the phase contrast microscope. Both, negatively charged and neutral vesicles coalesced into complexes and adhered to the bottom of the observation chamber in the presence of β2GPI in solution. Anti-β2GPIs alone or previously mixed with β2GPI caused coalescence of charged but not neutral vesicles, i.e. for neutral membranes the effect of β2GPI was abolished by the presence of anti-β2GPIs. Since the presence of the above adhesion mediators can prevent fragmentation of the membrane we propose a (new) possible anticoagulant mechanism for some serum proteins by preventing the release of prothrombogenic microexovesicles into circulation.