Document Detail

Regulation of triacylglycerol synthesis in permeabilized rat hepatocytes. Role of fatty acid concentration and diacylglycerol acyltransferase.
MedLine Citation:
PMID:  8163026     Owner:  NLM     Status:  MEDLINE    
Isolated hepatocytes from fed and starved rats, permeabilized with Staphylococcus aureus alpha-toxin, were incubated with increasing concentrations of radiolabelled fatty acids, in the presence of a saturating concentration of 3-GP. Incorporation of label into LPA, PA and DAG was lower in cells from starved rats than in cells from fed rats, apparently reflecting the lower activity of GPAT after starvation. This enzyme approached saturation at high fatty acid levels and determined the overall flux through the esterification pathway. TAG synthesis, however, was the same in both nutritional states and could not be saturated with fatty acid under the given conditions. Taken together with the observed accumulation of DAG, these data suggest that the rate of TAG synthesis is controlled by the fatty acid supply and, more particularly, by the affinity of DGAT for acyl-CoA.
H K Stals; W Top; P E Declercq
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  FEBS letters     Volume:  343     ISSN:  0014-5793     ISO Abbreviation:  FEBS Lett.     Publication Date:  1994 Apr 
Date Detail:
Created Date:  1994-05-20     Completed Date:  1994-05-20     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0155157     Medline TA:  FEBS Lett     Country:  NETHERLANDS    
Other Details:
Languages:  eng     Pagination:  99-102     Citation Subset:  IM    
Catholic University of Leuven, Faculty of Pharmaceutical Sciences, Laboratory of Clinical Chemistry, Belgium.
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MeSH Terms
Acyltransferases / metabolism*
Cell Membrane Permeability
Diacylglycerol O-Acyltransferase
Fatty Acids / metabolism*
Liver / cytology,  enzymology,  metabolism*
Rats, Wistar
Triglycerides / biosynthesis*
Reg. No./Substance:
0/Fatty Acids; 0/Triglycerides; EC 2.3.-/Acyltransferases; EC O-Acyltransferase

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

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