| Literature DB >> 6123958 |
J Strosznajder, W Tang, R Manning, A Y Lin, R MacQuarrie, G Y Sun.
Abstract
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.Entities:
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Year: 1981 PMID: 6123958 DOI: 10.1007/bf00966680
Source DB: PubMed Journal: Neurochem Res ISSN: 0364-3190 Impact factor: 3.996