No evidence for lysophospholipid formation during peroxidation of phospholipids by NADPH-cytochrome P-450 reductase and iron ions.

Liposomes comprised of liver microsomal phospholipids and radioactive phosphatidylcholine or phosphatidylethanolamine as tracers were incubated with isolated liver microsomal NADPH-cytochrome P-450 reductase, NADPH and ADP-EDTA-chelated iron ions, a system which stimulates peroxidation of unsaturated fatty acids of phospholipids. Phospholipids and their reaction products were extracted and chromatographed on HPLC. Phosphatidylcholine and phosphatidylethanolamine considerably decreased after 30 min incubation, depending on the enzyme and NADPH as measured by UV absorbance and radioactivity. However, neither a lysophospholipid peak nor a lysophospholipid-like peak were detectable. We suggest that lysophospholipid formation during microsomal lipid peroxidation is exclusively due to phospholipase A2 and not due to peroxidative breakdown of the unsaturated fatty acid in the beta-position of glycerol.