Neurochemical characterization of an antimony-choline analog in rat cortical synaptosomes.
An analog of choline, in which nitrogen was replaced by antimony, was neurochemically characterized in rat cortical synaptosomes. It was found to be a substrate for several cholinergic enzymes, transported by a Na+-dependent, hemicholinium-3-sensitive process, acetylated, and subsequently released by depolarization in a calcium-dependent manner. Sb-choline also completed with choline for Na+-dependent uptake and for acetylation by [14C]acetyl-CoA in synaptosomes. These results suggest that Sb-choline and its acetylated product should be useful substrates for the x-ray microanalytical localization of cholinergic pools in intact nerve terminals.
D000105:Acetyl Coenzyme A / Q000378:metabolism; D000107:Acetylation; D000818:Animals; D000965:Antimony / Q000378:metabolism*; D002540:Cerebral Cortex / Q000378:metabolism*; D002794:Choline / Q000031:analogs & derivatives* / Q000378:metabolism*; D002797:Choline Kinase / Q000378:metabolism; D002795:Choline O-Acetyltransferase / Q000378:metabolism; D006426:Hemicholinium 3 / Q000494:pharmacology; D008297:Male; D009942:Organometallic Compounds; D051381:Rats; D011919:Rats, Inbred Strains; D012441:Saccharomyces cerevisiae / Q000201:enzymology; D012964:Sodium / Q000494:pharmacology; D013574:Synaptosomes / Q000378:metabolism*
D009942:Organometallic Compounds; D006426:Hemicholinium 3; D000105:Acetyl Coenzyme A; C033204:antimony choline; D000965:Antimony; D012964:Sodium; D002795:Choline O-Acetyltransferase; D002797:Choline Kinase; D002794:Choline