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.
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Authors | J Strosznajder, W Tang, R Manning, A Y Lin, R MacQuarrie, G Y Sun |
Journal | Neurochemical research
(Neurochem Res)
Vol. 6
Issue 11
Pg. 1231-40
(Nov 1981)
ISSN: 0364-3190 [Print] United States |
PMID | 6123958
(Publication Type: Journal Article, Research Support, Non-U.S. Gov't, Research Support, U.S. Gov't, P.H.S.)
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Chemical References |
- Acyl Coenzyme A
- oleoyl-coenzyme A
- Palmitoyl-CoA Hydrolase
- Calcium
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Topics |
- Acyl Coenzyme A
(metabolism)
- Animals
- Brain Ischemia
(metabolism)
- Calcium
(pharmacology)
- Cerebral Cortex
(blood supply, metabolism)
- Intracellular Membranes
(enzymology)
- Palmitoyl-CoA Hydrolase
(antagonists & inhibitors)
- Rats
- Rats, Inbred Strains
- Synaptosomes
(drug effects, metabolism)
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