Document Detail

Loss of intracellular lipid binding proteins differentially impacts saturated fatty acid uptake and nuclear targeting in mouse hepatocytes.
MedLine Citation:
PMID:  22859366     Owner:  NLM     Status:  MEDLINE    
The liver expresses high levels of two proteins with high affinity for long-chain fatty acids (LCFAs): liver fatty acid binding protein (L-FABP) and sterol carrier protein-2 (SCP-2). Real-time confocal microscopy of cultured primary hepatocytes from gene-ablated (L-FABP, SCP-2/SCP-x, and L-FABP/SCP-2/SCP-x null) mice showed that the loss of L-FABP reduced cellular uptake of 12-N-methyl-(7-nitrobenz-2-oxa-1,3-diazo)-aminostearic acid (a fluorescent-saturated LCFA analog) by ∼50%. Importantly, nuclear targeting of the LCFA was enhanced when L-FABP was upregulated (SCP-2/SCP-x null) but was significantly reduced when L-FABP was ablated (L-FABP null), thus impacting LCFA nuclear targeting. These effects were not associated with a net decrease in expression of key membrane proteins involved in LCFA or glucose transport. Since hepatic LCFA uptake and metabolism are closely linked to glucose uptake, the effect of glucose on L-FABP-mediated LCFA uptake and nuclear targeting was examined. Increasing concentrations of glucose decreased cellular LCFA uptake and even more extensively decreased LCFA nuclear targeting. Loss of L-FABP exacerbated the decrease in LCFA nuclear targeting, while loss of SCP-2 reduced the glucose effect, resulting in enhanced LCFA nuclear targeting compared with control. Simply, ablation of L-FABP decreases LCFA uptake and even more extensively decreases its nuclear targeting.
Stephen M Storey; Avery L McIntosh; Huan Huang; Gregory G Martin; Kerstin K Landrock; Danilo Landrock; H Ross Payne; Ann B Kier; Friedhelm Schroeder
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural     Date:  2012-08-02
Journal Detail:
Title:  American journal of physiology. Gastrointestinal and liver physiology     Volume:  303     ISSN:  1522-1547     ISO Abbreviation:  Am. J. Physiol. Gastrointest. Liver Physiol.     Publication Date:  2012 Oct 
Date Detail:
Created Date:  2012-10-02     Completed Date:  2012-12-18     Revised Date:  2013-10-10    
Medline Journal Info:
Nlm Unique ID:  100901227     Medline TA:  Am J Physiol Gastrointest Liver Physiol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  G837-50     Citation Subset:  IM    
Department of Physiology and Pharmacology, Texas A & M University, TVMC, College Station, TX 77843-4466, USA.
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MeSH Terms
Biological Transport / physiology
Blotting, Western
Carrier Proteins / metabolism*
Cells, Cultured
Fatty Acid-Binding Proteins / metabolism*
Glucose / metabolism
Hepatocytes / physiology*
Lipid Metabolism
Membrane Proteins / metabolism
Mice, Inbred C57BL
Microscopy, Confocal
Stearic Acids / metabolism*
Up-Regulation / physiology
Grant Support
Reg. No./Substance:
0/Carrier Proteins; 0/Fatty Acid-Binding Proteins; 0/Membrane Proteins; 0/Stearic Acids; 0/sterol carrier proteins; 50-99-7/Glucose

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