Document Detail

Malonyl-CoA and long chain acyl-CoA esters as metabolic coupling factors in nutrient-induced insulin secretion.
MedLine Citation:
PMID:  1556096     Owner:  NLM     Status:  MEDLINE    
Several approaches were used to test the hypothesis proposing a role for acyl-CoA esters in nutrient-induced insulin release (Prentki, M., and Matschinsky, F. M. (1987) Physiol. Rev. 67, 1185-1248; Corkey, B. E., Glennon, M. C., Chen, K. S., Deeney, J. T., Matschinsky, F. M., and Prentki, M. (1989) J. Biol. Chem. 264, 21608-21612). Exogenous saturated long chain fatty acids markedly potentiated glucose-induced insulin release and elevated long chain acyl-CoA esters in the clonal beta-cell line (HIT). The secretory action depended on the fatty acid chain length, occurred in the range 3-20 microM (free concentration of palmitate), and was reversible and inhibitable by the neuromodulator somatostatin. 2-Bromopalmitate, an inhibitor of carnitine palmitoyl transferase I, suppressed the oxidation of endogenous fatty acids and promoted release of insulin. Only the nutrients or the combination of nutrients that caused secretion elevated malonyl-CoA. The short-chain acyl-CoA profile of HIT cells stimulated by various nutrients was determined in the presence of the nonstimulatory fuel glutamine. Glucose and leucine each provoked similar changes in acyl-CoA compounds. Both secretagogues elevated malonyl-CoA 3-6-fold, whereas succinyl-CoA, free CoASH, acetyl-CoA, and the free CoASH to acetyl-CoA ratio remained unaltered. Furthermore, only when inhibition of fatty acid oxidation was associated with a rise in malonyl-CoA did the total (mitochondrial plus cytoplasmic) content of long chain acyl-CoA esters correlate inversely with insulin release promoted by various nutrients. The results are consistent with the concept that fuel stimuli cause a rise in malonyl-CoA which by inhibiting fatty acid oxidation increase cytosolic long chain acyl-CoA esters. These data provide further support for a model in which malonyl-CoA and long chain acyl-CoAs esters serve as metabolic coupling factors when pancreatic beta-cells are stimulated with glucose and other nutrient secretagogues.
M Prentki; S Vischer; M C Glennon; R Regazzi; J T Deeney; B E Corkey
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  267     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  1992 Mar 
Date Detail:
Created Date:  1992-05-04     Completed Date:  1992-05-04     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  5802-10     Citation Subset:  IM    
Division de Biochimie Clinique, University of Geneva, Switzerland.
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MeSH Terms
Acyl Coenzyme A / metabolism*
Cell Line
Fatty Acids, Nonesterified / metabolism,  pharmacology*
Glucose / pharmacology
Insulin / secretion*
Islets of Langerhans
Malonyl Coenzyme A / metabolism*
Models, Biological
Palmitates / pharmacology
Palmitic Acid
Palmitic Acids / metabolism,  pharmacology
Serum Albumin, Bovine / pharmacology
Structure-Activity Relationship
Grant Support
Reg. No./Substance:
0/Acyl Coenzyme A; 0/Fatty Acids, Nonesterified; 0/Palmitates; 0/Palmitic Acids; 0/Serum Albumin, Bovine; 11061-68-0/Insulin; 18263-25-7/2-bromopalmitate; 50-99-7/Glucose; 524-14-1/Malonyl Coenzyme A; 57-10-3/Palmitic Acid

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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