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 beta2 glycoprotein I (beta2GPI) or anti-beta2GPI 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 beta2GPI in solution. Anti-beta2GPIs alone or previously mixed with beta2GPI caused coalescence of charged but not neutral vesicles, i.e. for neutral membranes the effect of beta2GPI was abolished by the presence of anti-beta2GPIs. 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.