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J Lipid Res. 2014 May;55(5):808-15. doi: 10.1194/jlr.M039867. Epub 2014 Mar 8.

Hepatic ATGL mediates PPAR-α signaling and fatty acid channeling through an L-FABP independent mechanism.

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1
Department of Food Science and Nutrition, University of Minnesota, St. Paul, MN.

Abstract

Adipose TG lipase (ATGL) catalyzes the rate-limiting step in TG hydrolysis in most tissues. We have shown that hepatic ATGL preferentially channels hydrolyzed FAs to β-oxidation and induces PPAR-α signaling. Previous studies have suggested that liver FA binding protein (L-FABP) transports FAs from lipid droplets to the nucleus for ligand delivery and to the mitochondria for β-oxidation. To determine if L-FABP is involved in ATGL-mediated FA channeling, we used adenovirus-mediated suppression or overexpression of hepatic ATGL in either WT or L-FABP KO mice. Hepatic ATGL knockdown increased liver weight and TG content of overnight fasted mice regardless of genotype. L-FABP deletion did not impair the effects of ATGL overexpression on the oxidation of hydrolyzed FAs in primary hepatocyte cultures or on serum β-hydroxybutyrate concentrations in vivo. Moreover, L-FABP deletion did not influence the effects of ATGL knockdown or overexpression on PPAR-α target gene expression. Taken together, we conclude that L-FABP is not required to channel ATGL-hydrolyzed FAs to mitochondria for β-oxidation or the nucleus for PPAR-α regulation.

KEYWORDS:

adipose triglyceride lipase; liver fatty acid binding protein; peroxisome proliferator-activated receptor-α; β-oxidation

PMID:
24610891
PMCID:
PMC3995459
DOI:
10.1194/jlr.M039867
[Indexed for MEDLINE]
Free PMC Article
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