Document Detail

A novel role for fatty acid transport protein 1 in the regulation of tricarboxylic acid cycle and mitochondrial function in 3T3-L1 adipocytes.
MedLine Citation:
PMID:  19535819     Owner:  NLM     Status:  MEDLINE    
Fatty acid transport proteins (FATPs) are integral membrane acyl-CoA synthetases implicated in adipocyte fatty acid influx and esterification. Whereas some FATP1 translocates to the plasma membrane in response to insulin, the majority of FATP1 remains within intracellular structures and bioinformatic and immunofluorescence analysis of FATP1 suggests the protein primarily resides in the mitochondrion. To evaluate potential roles for FATP1 in mitochondrial metabolism, we used a proteomic approach following immunoprecipitation of endogenous FATP1 from 3T3-L1 adipocytes and identified mitochondrial 2-oxoglutarate dehydrogenase. To assess the functional consequence of the interaction, purified FATP1 was reconstituted into phospholipid-containing vesicles and its effect on 2-oxoglutarate dehydrogenase activity evaluated. FATP1 enhanced the activity of 2-oxoglutarate dehydrogenase independently of its acyl-CoA synthetase activity whereas silencing of FATP1 in 3T3-L1 adipocytes resulted in decreased activity of 2-oxoglutarate dehydrogenase. FATP1 silenced 3T3-L1 adipocytes exhibited decreased tricarboxylic acid cycle activity, increased cellular NAD(+)/NADH, increased fatty acid oxidation, and increased lactate production indicative of altered mitochondrial energy metabolism. These results reveal a novel role for FATP1 as a regulator of tricarboxylic acid cycle activity and mitochondrial function.
Brian M Wiczer; David A Bernlohr
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2009-06-17
Journal Detail:
Title:  Journal of lipid research     Volume:  50     ISSN:  0022-2275     ISO Abbreviation:  J. Lipid Res.     Publication Date:  2009 Dec 
Date Detail:
Created Date:  2009-12-07     Completed Date:  2010-03-23     Revised Date:  2013-06-02    
Medline Journal Info:
Nlm Unique ID:  0376606     Medline TA:  J Lipid Res     Country:  United States    
Other Details:
Languages:  eng     Pagination:  2502-13     Citation Subset:  IM    
Department of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota, Minneapolis, MN, USA.
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MeSH Terms
3T3-L1 Cells
Adipocytes / metabolism*
Cells, Cultured
Citric Acid Cycle / physiology*
Fatty Acid Transport Proteins / metabolism*
Mice, Inbred C57BL
Mitochondria / metabolism*
Reg. No./Substance:
0/Fatty Acid Transport Proteins; 0/Slc27a1 protein, mouse

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