The acyl-CoA synthetase inhibitor triacsin C enhanced eicosanoid release in leukocytes.
Triacsin C was previously reported to inhibit long-chain acyl-CoA synthetase and to reduce the production of acyl-CoA in rat neutrophils dose- and time-dependently. We found that preincubation with triacsin C inhibited the incorporation of labeled arachidonic acid into rat neutrophils. Furthermore, when triacsin C-treated neutrophils were stimulated with the Ca-ionophore A23187, they released an increased amount of eicosanoids into the culture medium. These results indicate that triacsin C suppressed acylation of arachidonic acid, which resulted in an increase in its metabolites.
Oh-ishi
S
S
Department of Pharmacology, School of Pharmaceutical Sciences, Kitasato University, Tokyo, Japan.
Yamaki
K
K
Abe
M
M
Tomoda
H
H
Omura
S
S
D000818:Animals; D016718:Arachidonic Acid / Q000378:metabolism; D002250:Carbon Radioisotopes; D003066:Coenzyme A Ligases / Q000037:antagonists & inhibitors*; D015777:Eicosanoids / Q000378:metabolism*; D066298:In Vitro Techniques; D007962:Leukocytes / Q000187:drug effects* / Q000378:metabolism; D051381:Rats; D014226:Triazenes / Q000494:pharmacology*; D014665:Vasodilator Agents / Q000494:pharmacology
D002250:Carbon Radioisotopes; D015777:Eicosanoids; D014226:Triazenes; D014665:Vasodilator Agents; D016718:Arachidonic Acid; C034613:triacsin C; D003066:Coenzyme A Ligases