Phospholipid transverse diffusion in synaptosomes: evidence for the involvement of the aminophospholipid translocase.

We have studied in Torpedo marmorata electric organ synaptosomes the equilibration kinetics of spin-labeled phospholipid analogues initially incorporated into the outer plasma membrane monolayer. As assayed by evoked releases of both ATP and acetylcholine, the nerve endings were closed vesicles containing an energy source. The aminophospholipids (phosphatidylethanolamine and phosphatidylserine) were translocated toward the inner membrane leaflet faster and to a higher extent than their choline-containing counterparts (phosphatidylcholine and sphingomyelin). This difference was abolished by incubation of synaptosomal membranes with N-ethylmaleimide, suggesting that the accumulation of aminophospholipids in the inner layer was driven by a protein. This phenomenon is comparable with what was described in plasma membranes of other eucaryotic cells (erythrocyte, lymphocyte, platelet, fibroblast), and thus we would suggest that an aminophospholipid translocase, capable of moving the aminophospholipids from the outer to the inner layer at the expense of ATP, is also present in the synaptosomal plasma membrane.