Abstract
We investigated the effects of various phospholipids on the presynaptic levels of newly synthesized [3H]acetylcholine (ACh) in rat cerebral cortical synaptosomes. When administered as small unilamellar vesicles (200-500 A diameters) dipalmitoylphosphatidylcholine (DPPC) reduced [3H]ACh levels in concentration and time-related manners, while increasing the efflux of labelled choline to a similar extent. The reductions in synaptosomal [3H]-ACh levels induced by DPPC (3 mg/ml) were found in the cytosolic S3 but not microsomal P3 fraction, arguing for a cytoplasmic, non-vesicular site of action. DPPC-induced reductions in [3H]ACh levels were blocked by 100 microM eserine, a tertiary amine cholinesterase inhibitor, but not with 100 microM neostigmine, a quaternary ammonium inhibitor. Large unilamellar vesicles (2000-5000 A diameters) consisting of soybean-phosphatidylcholine reduced [3H]ACh levels to the same extent that small vesicles did at the same concentration (3 mg/ml). Taken together, these results suggest that DPPC can fuse with membranes to increase the hydrolysis of cytoplasmic ACh via a small intra-terminal subpopulation of cholinesterases.
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