TRANSPORT AND DECARBOXYLATION OF LIPOSOMAL PHOSPHATIDYLSERINE - EFFECT OF CATIONS

Decarboxylation of liposomal phosphatidylserine by rat liver and Ehrlich ascites tumor mitochondria was taken as a measure of phospholipid transfer. The process was found to be greatly enhanced by the cytoplasmic fraction of rat liver containing nonspecific lipid transfer protein, but not by the cytoplasmic fraction from tumor cells. Divalent cations, like rat liver cytoplasmic fraction, also stimulated phosphatidylserine decarboxylation by facilitating the lipid association with mitochondria. In contrast. these cations, at 0.5-3 mM concentration, inhibited the cytoplasmic fraction-mediated phosphatidylserine transport. Monovalent cations were also inhibitory but at 20-150 mM concentration. However, they had no effect on phosphatidylserine decarboxylation in the absence of the cytoplasmic fraction. Further experiments with purified Tat liver nonspecific lipid transfer protein and pyrene-labeled phosphatidylcholine and phosphatidylserine have shown that cations by neutralizing net negative charge on phospholipid donor vesicles decrease the interaction of protein with them and, in consequence, lower the rate of release of molecules to the water phase.