Document Detail


Overexpressed FATP1, ACSVL4/FATP4 and ACSL1 increase the cellular fatty acid uptake of 3T3-L1 adipocytes but are localized on intracellular membranes.
MedLine Citation:
PMID:  23024797     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Long chain acyl-CoA synthetases are essential enzymes of lipid metabolism, and have also been implicated in the cellular uptake of fatty acids. It is controversial if some or all of these enzymes have an additional function as fatty acid transporters at the plasma membrane. The most abundant acyl-CoA synthetases in adipocytes are FATP1, ACSVL4/FATP4 and ACSL1. Previous studies have suggested that they increase fatty acid uptake by direct transport across the plasma membrane. Here, we used a gain-of-function approach and established FATP1, ACSVL4/FATP4 and ACSL1 stably expressing 3T3-L1 adipocytes by retroviral transduction. All overexpressing cell lines showed increased acyl-CoA synthetase activity and fatty acid uptake. FATP1 and ACSVL4/FATP4 localized to the endoplasmic reticulum by confocal microscopy and subcellular fractionation whereas ACSL1 was found on mitochondria. Insulin increased fatty acid uptake but without changing the localization of FATP1 or ACSVL4/FATP4. We conclude that overexpressed acyl-CoA synthetases are able to facilitate fatty acid uptake in 3T3-L1 adipocytes. The intracellular localization of FATP1, ACSVL4/FATP4 and ACSL1 indicates that this is an indirect effect. We suggest that metabolic trapping is the mechanism behind the influence of acyl-CoA synthetases on cellular fatty acid uptake.
Authors:
Tianzuo Zhan; Margarete Poppelreuther; Robert Ehehalt; Joachim Füllekrug
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2012-09-14
Journal Detail:
Title:  PloS one     Volume:  7     ISSN:  1932-6203     ISO Abbreviation:  PLoS ONE     Publication Date:  2012  
Date Detail:
Created Date:  2012-10-01     Completed Date:  2013-02-15     Revised Date:  2013-07-11    
Medline Journal Info:
Nlm Unique ID:  101285081     Medline TA:  PLoS One     Country:  United States    
Other Details:
Languages:  eng     Pagination:  e45087     Citation Subset:  IM    
Affiliation:
Molecular Cell Biology Laboratory, Internal Medicine IV, University of Heidelberg, Heidelberg, Germany.
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MeSH Terms
Descriptor/Qualifier:
3T3-L1 Cells
Adipocytes / drug effects,  metabolism*
Animals
Coenzyme A Ligases / genetics*,  metabolism
Endoplasmic Reticulum / metabolism
Fatty Acid Transport Proteins / genetics*,  metabolism
Fatty Acids / metabolism*
Gene Expression*
Glucose / metabolism
Humans
Insulin / pharmacology
Intracellular Membranes / metabolism*
Mice
Mitochondria / metabolism
Protein Transport / drug effects
Rats
Chemical
Reg. No./Substance:
0/Fatty Acid Transport Proteins; 0/Fatty Acids; 0/Insulin; 0/Slc27a1 protein, mouse; 50-99-7/Glucose; EC 6.2.1.-/Coenzyme A Ligases; EC 6.2.1.3/Acsl1 protein, rat
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