| Long chain acyl coenzyme A and signaling in neutrophils. An inhibitor of acyl coenzyme A synthetase, triacsin C, inhibits superoxide anion generation and degranulation by human neutrophils. | |
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MedLine Citation:
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PMID: 7982939 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Ligand-initiated activation of neutrophils triggers O2- generation, degranulation, phospholipid remodeling, and release of fatty acids such as arachidonate, oleate, and palmitate. Long chain acyl-CoA synthetase converts free fatty acids to acyl-CoA esters; a role for acyl-CoA esters as positive modulators of neutrophil functions is proposed. Physiologically relevant concentrations (1-10 microM) of acyl-CoA esters such as palmitoyl-CoA, enhanced O2- generation triggered by fMet-Leu-Phe or guanosine 5'-O-(thiotriphosphate) (GTP gamma S) but did not act as a trigger per se. Triacsin C, an inhibitor of acyl-CoA synthetase, inhibited fMet-Leu-Phe-elicited O2- generation and degranulation in a concentration-dependent manner. Triacsin C inhibited O2- generation elicited by fMet-Leu-Phe and GTP gamma S in electroporated neutrophils, indicating that acyl-CoA acted downstream from the receptor. Palmitoyl-CoA reversed the Triacsin C-induced inhibition of O2- generation. fMet-Leu-Phe elicited a prompt increase in total long chain acyl-CoA esters. Arachidonoyl-CoA and oleoyl-CoA were elevated 5 s after addition of fMet-Leu-Phe, while palmitoyl-CoA was not elevated until 60 s. Triacsin C inhibited fMet-Leu-Phe-initiated increases in arachidonoyl-CoA, oleoyl-CoA, and palmitoyl-CoA. These results suggest a role for acyl-CoA esters in regulating activation of O2- generation and degranulation at the G protein or subsequent step(s). |
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Authors:
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H M Korchak; L H Kane; M W Rossi; B E Corkey |
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Publication Detail:
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Type: Journal Article; Research Support, U.S. Gov't, P.H.S. |
Journal Detail:
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Title: The Journal of biological chemistry Volume: 269 ISSN: 0021-9258 ISO Abbreviation: J. Biol. Chem. Publication Date: 1994 Dec |
Date Detail:
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Created Date: 1994-12-30 Completed Date: 1994-12-30 Revised Date: 2007-11-14 |
Medline Journal Info:
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Nlm Unique ID: 2985121R Medline TA: J Biol Chem Country: UNITED STATES |
Other Details:
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Languages: eng Pagination: 30281-7 Citation Subset: IM |
Affiliation:
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Department of Pediatrics, University of Pennsylvania School of Medicine, Philadelphia 19104. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Acyl Coenzyme A
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blood* Coenzyme A Ligases / antagonists & inhibitors* Cytochalasin B / pharmacology Cytoplasmic Granules / drug effects, physiology* Humans Ionomycin / pharmacology Kinetics N-Formylmethionine Leucyl-Phenylalanine / pharmacology Neutrophils / drug effects, physiology* Signal Transduction* Superoxides / antagonists & inhibitors, blood* Tetradecanoylphorbol Acetate / pharmacology Triazenes / pharmacology* |
| Grant Support | |
ID/Acronym/Agency:
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AI 24840/AI/NIAID NIH HHS; DK 46200/DK/NIDDK NIH HHS; DK35914/DK/NIDDK NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Acyl Coenzyme A; 0/Triazenes; 11062-77-4/Superoxides; 14930-96-2/Cytochalasin B; 16561-29-8/Tetradecanoylphorbol Acetate; 56092-81-0/Ionomycin; 59880-97-6/N-Formylmethionine Leucyl-Phenylalanine; 76896-80-5/triacsin C; EC 6.2.1.-/Coenzyme A Ligases |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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