1. Endoplasmic reticulum-localized hepatic lipase decreases triacylglycerol storage and VLDL secretion.
- Author
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Erickson B, Selvan SP, Ko KW, Kelly K, Quiroga AD, Li L, Nelson R, King-Jones K, Jacobs RL, and Lehner R
- Subjects
- Animals, Apolipoproteins B metabolism, Cells, Cultured, Cholesterol Esters metabolism, Fatty Acids metabolism, Hepatocytes cytology, Lipid Metabolism, Liver cytology, Mice, Oxidation-Reduction, PPAR alpha metabolism, Endoplasmic Reticulum enzymology, Hepatocytes enzymology, Lipase metabolism, Lipoproteins, VLDL metabolism, Liver enzymology, Triglycerides metabolism
- Abstract
Hepatic triacylglycerol levels are governed through synthesis, degradation and export of this lipid. Here we demonstrate that enforced expression of hepatic lipase in the endoplasmic reticulum in McArdle RH7777 hepatocytes resulted in a significant decrease in the incorporation of fatty acids into cellular triacylglycerol and cholesteryl ester accompanied by attenuation of secretion of apolipoprotein B-containing lipoproteins. Hepatic lipase-mediated depletion of intracellular lipid storage increased the expression of peroxisome proliferator-activated receptor α and its target genes and augmented oxidation of fatty acids. These data show that 1) hepatic lipase is active in the endoplasmic reticulum and 2) intracellular hepatic lipase modulates cellular lipid metabolism and lipoprotein secretion., (Copyright © 2013 Elsevier B.V. All rights reserved.)
- Published
- 2013
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