Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1949784 | Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids | 2009 | 11 Pages |
Abstract
Mouse esterase-x/carboxylesterase 1 (Es-x/Ces1) is a close homolog of triacylglycerol hydrolase/carboxylesterase 3 (TGH/Ces3). Es-x possesses a conserved esterase/lipase active site motif, suggesting that like TGH it could play a role in hepatic triacylglycerol (TG) metabolism. McArdle-RH7777 cells stably transfected with Es-x cDNA accumulated significantly less TG and had increased production of acid-soluble metabolites (an indicator of β-oxidation) during incubations with 0.4 mM oleic acid when compared to empty vector or TGH cDNA transfected cells. Reduction of cellular TG persisted in the presence of esterase/lipase inhibitor E600 indicating that Es-x-mediated TG lowering can be largely explained by reduced partitioning of exogenous fatty acids to TG and increased redirection to β-oxidation, rather than by increased TG turnover. Glycerol supplementation increased TG synthesis in both control and Es-x expressing cells to similar extent suggesting that Es-x expression did not reduce flux of metabolic intermediates through the glycerol-3-phosphate pathway. While Es-x expression reduced cellular TG levels, secretion of TG and apolipoprotein B remained unchanged when compared to control cells. Overall, these results suggest that Es-x limits hepatic TG accumulation by promoting β-oxidation.
Keywords
PDIECLPNPASMADRPHRPapoBG-3-PMCAp-nitrophenylApolipoprotein BAtglEsteraseOleic acidphosphatidic acidenhanced chemiluminescenceMUHdiacylglycerolendoplasmic reticulumphosphatidylcholinephosphatidylethanolamineadipose triglyceride lipaseHorseradish peroxidaseprotein disulfide isomeraseadipose differentiation-related proteinPNSglycerol-3-phosphate
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Authors
Kerry W.S. Ko, Bruce Erickson, Richard Lehner,