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Journal of Lipid Research, Vol. 47, 2004-2010, September 2006
Copyright © 2006 by American Society for Biochemistry and Molecular Biology

Rat long-chain acyl-CoA synthetase mRNA, protein, and activity vary in tissue distribution and in response to diet

Douglas G. Mashek¹, Lei O. Li and Rosalind A. Coleman²

Department of Nutrition, University of North Carolina, Chapel Hill, NC 27599

Published, JLR Papers in Press, June 13, 2006.

¹ Present address of D. G. Mashek: Department of Food Science and Nutrition, University of Minnesota, 225 Food Science and Nutrition, 1334 Eckles Avenue, St. Paul, MN 55108-1038.

² To whom correspondence should be addressed. e-mail: rcoleman{at}unc.edu

Distinct isoforms of long-chain acyl-CoA synthetases (ACSLs) may partition fatty acids toward specific metabolic cellular pathways. For each of the five members of the rat ACSL family, we analyzed tissue mRNA distributions, and we correlated the mRNA, protein, and activity of ACSL1 and ACSL4 after fasting and refeeding a 69% sucrose diet. Not only did quantitative real-time PCR analyses reveal unique tissue expression patterns for each ACSL isoform, but expression varied markedly in different adipose depots. Fasting increased ACSL4 mRNA abundance in liver, muscle, and gonadal and inguinal adipose tissues, and refeeding decreased ACSL4 mRNA. A similar pattern was observed for ACSL1, but both fasting and refeeding decreased ACSL1 mRNA in gonadal adipose. Fasting also decreased ACSL3 and ACSL5 mRNAs in liver and ACSL6 mRNA in muscle. Surprisingly, in nearly every tissue measured, the effects of fasting and refeeding on the mRNA abundance of ACSL1 and ACSL4 were discordant with changes in protein abundance. These data suggest that the individual ACSL isoforms are distinctly regulated across tissues and show that mRNA expression may not provide useful information about isoform function. They further suggest that translational or posttranslational modifications are likely to contribute to the regulation of ACSL isoforms.

Supplementary key words coenzyme A • acyl-CoA synthetase • fatty acid metabolism

Abbreviations: ACSL, long-chain acyl-coenzyme A synthetase; PPAR, peroxisome proliferator-activated receptor; SREBP, sterol-response element binding protein; TAG, triacylglycerol

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