| First Author | Ong KT | Year | 2014 |
| Journal | J Lipid Res | Volume | 55 |
| Issue | 5 | Pages | 808-15 |
| PubMed ID | 24610891 | Mgi Jnum | J:210241 |
| Mgi Id | MGI:5569855 | Doi | 10.1194/jlr.M039867 |
| Citation | Ong KT, et al. (2014) Hepatic ATGL mediates PPAR-alpha signaling and fatty acid channeling through an L-FABP independent mechanism. J Lipid Res 55(5):808-15 |
| abstractText | 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 beta-oxidation and induces PPAR-alpha 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 beta-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 beta-hydroxybutyrate concentrations in vivo. Moreover, L-FABP deletion did not influence the effects of ATGL knockdown or overexpression on PPAR-alpha target gene expression. Taken together, we conclude that L-FABP is not required to channel ATGL-hydrolyzed FAs to mitochondria for beta-oxidation or the nucleus for PPAR-alpha regulation. |
