Abstract
Triacsin C, a product of Streptmyces sp. SK-1894, was previously reported as an inhibitor of long chain acyl-CoA synthetase. Pretreatment with triacsin C (500 nM) for 1h enhanced production of platelet-activating factor in rat neutrophils, followed by stimulation with A23187 or fMLP. Amount of lyso-PAF was also augumented. Triacsin C alone did not increase PAF content and did not modulate enzymatic activities of acytransferase, cholinephosphotransferase, acetylhydrolase, acetyltransferase or phospholipase A2. These results suggest that triacsin C might enhance supply of substrate for PAF synthesis, i.e. accumulation of lyso-PAF by interfering reacylation pathway.
MeSH terms
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Acylation
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Animals
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Calcimycin / pharmacology
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Coenzyme A Ligases / antagonists & inhibitors*
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Male
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N-Formylmethionine Leucyl-Phenylalanine / pharmacology
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Neutrophils / drug effects
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Neutrophils / metabolism*
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Platelet Activating Factor / analogs & derivatives
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Platelet Activating Factor / biosynthesis*
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Rats
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Rats, Sprague-Dawley
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Repressor Proteins*
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Saccharomyces cerevisiae Proteins*
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Triazenes / pharmacology*
Substances
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O-deacetyl platelet activating factor
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Platelet Activating Factor
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Repressor Proteins
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Saccharomyces cerevisiae Proteins
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Triazenes
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Calcimycin
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N-Formylmethionine Leucyl-Phenylalanine
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triacsin C
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Coenzyme A Ligases
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FAA2 protein, S cerevisiae
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long-chain-fatty-acid-CoA ligase