Metabolism of oleoyl-CoA in rat brain synaptosomes: effects of calcium and post-decapitative ischemia.
The hydrolysis of acyl-CoA by acyl-CoA hydrolase (EC 3.1.2.2.) in brain synaptosomes was inhibited by calcium. This inhibition was partly due to interaction of Ca2+ with the acyl-CoA, which was present in the soluble form, and partly due to complex formation among acyl-CoA, Ca2+ and membrane phospholipids. The inhibition of acyl-CoA hydrolase activity, as well as the complex formation, could be reversed if incubation was carried out in the presence of Ca2+ chelating agents. Synaptosomes isolated from brain samples after 1 min of postdecapitative treatment showed a decrease in oleoyl-CoA hydrolase activity. The physiological implication of acyl-CoA metabolism in relation to synaptic function is discussed.
D000214:Acyl Coenzyme A / Q000378:metabolism*; D000818:Animals; D002545:Brain Ischemia / Q000378:metabolism; D002118:Calcium / Q000494:pharmacology*; D002540:Cerebral Cortex / Q000098:blood supply / Q000378:metabolism*; D007425:Intracellular Membranes / Q000201:enzymology; D010170:Palmitoyl-CoA Hydrolase / Q000037:antagonists & inhibitors; D051381:Rats; D011919:Rats, Inbred Strains; D013574:Synaptosomes / Q000187:drug effects / Q000378:metabolism*
D000214:Acyl Coenzyme A; C017585:oleoyl-coenzyme A; D010170:Palmitoyl-CoA Hydrolase; D002118:Calcium