Experimental study reveals calcium-dependent mitochondrial transfer of acetyl coenzyme A in rat synaptosomes, suggesting direct membrane permeabilization drives acetylcholine synthesis.
Labeled acetylcholine derived from labeled pyruvate in a synaptosomal preparation from rat brain, incubated with nicotinamide adenine dinucleotide as well as coenzyme A, is stimulated by calcium ions in the absence but not in the presence of Triton X-100. Whereas citrate is taken up by cholinergic synaptosomes because it suppresses the formation of acetylcholine from pyruvate, it is not itself converted into acetylcholine. The evidence suggests that there is a calcium-dependent transfer of mitochondrial acetyl coenzyme A into the cholinergic synaptoplasm, which is apparently devoid of the citrate cleavage enzyme, and is there converted into acetylcholine. The permeability of the inner mitochondrial membrane to coenzyme A and acetyl coenzyme A seems to be enhanced by calcium ions, and this effect may be mediated by mitochondrial phospholipase A2.
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Benjamin et al. (1981) studied this question.
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