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[Transmembrane migration of phosphatidylcholine and peroxidation of lipids in rat liver microsomes].

The exchangeability of phosphatidylcholine in microsomes differing in the degree of lipid peroxidation was determined by incubation of microsomes labelled in vivo with [methyl-14C]choline chloride with an excess of phosphatidylcholine liposomes and phosphatidyl-exchange protein from beef liver. The phosphatidylcholine peroxidation products were shown to act as substrates for the phosphatidylcholine-exchange protein. The level of exchangeable microsomal phosphatidylcholine did not depend on the degree of lipid peroxidation in the microsomes. Stimulation of lipid peroxidation by Fe2+-ascorbate or inhibition of lipid peroxidation by alpha-tocopherol did not influence the exchange of microsomal phosphatidylcholine. However, with highly peroxidized phosphatidylcholine liposomes as acceptor particles the exchange of microsomal phosphatidylcholine in the presence of phosphatidylcholine-exchange protein was strongly inhibited. In all cases the percentage of microsomal phosphatidylcholine exchangeable within 1-2 hrs was 85-90%. It is concluded that lipid peroxidation is not responsible for the rapid translocation (flip-flop) of phosphatidylcholine in rat liver microsomes. A possible involvement of membrane proteins in this process is proposed.