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Lo V.,University of Alberta | Erickson B.,University of Alberta | Thomason-Hughes M.,University of Alberta | Ko K.W.S.,University of Alberta | And 3 more authors.
Journal of Lipid Research | Year: 2010

Mobilization of hepatic triacylglycerol stores provides substrates for mitochondrial -oxidation and assembly of VLDLs; however, the identity of lipolytic enzymes involved in the regulation of this process remains largely unknown. Arylacetamide deacetylase (AADA) shares homology with hormone-sensitive lipase and therefore could potentially participate in hepatic lipid metabolism, including the regulation of hepatic triacylglycerol levels. We have established McArdle-RH7777 (rat hepatoma) cell lines stably expressing mouse AADA cDNA and performed metabolic labeling as well as lipid mass analyses. Expression of AADA cDNA in McArdle-RH7777 cells signifi cantly reduced intracellular triacylglycerol levels and apolipoprotein B secretion and increased fatty acid oxidation. These results suggest that fatty acids released by AADA-mediated hydrolysis of lipids are channeled for -oxidation rather than for the assembly of lipoproteins.-Lo, V., B. Erickson, M. Thomason-Hughes, K. W. S. Ko, V. W. Dolinsky, R. Nelson, and R. Lehner. Arylacetamide deacetylase attenuates fatty-acidinduced triacylglycerol accumulation in rat hepatoma cells. Copyright © 2010 by the American Society for Biochemistry and Molecular Biology, Inc. Source

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