Publication Date:
1981-09-25
Description:
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.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Benjamin, A M -- Quastel, J H -- New York, N.Y. -- Science. 1981 Sep 25;213(4515):1495-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7280667" target="_blank"〉PubMed〈/a〉
Keywords:
ATP Citrate (pro-S)-Lyase/metabolism
;
Acetyl Coenzyme A/*metabolism
;
Acetylcholine/*biosynthesis
;
Animals
;
Brain/*metabolism
;
Calcium/physiology
;
Citrates/metabolism
;
Mitochondria/*metabolism
;
NAD/metabolism
;
Phospholipases A/metabolism
;
Phospholipases A2
;
Rats
;
Synaptosomes/*metabolism
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
