J. Lipid Res.  Neurobiology of Lipids (ISSN1683-5506)
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A more recent version of this article appeared on September 1, 2006

Papers In Press, published online ahead of print June 13, 2006
J. Lipid Res., doi:10.1194/jlr.M600150-JLR200
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Submitted on March 30, 2006
Revised on June 8, 2006
Accepted on June 13, 2006

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

Douglas G. Mashek, Lei O. Li, and Rosalind A. Coleman

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

Corresponding Author: rcoleman{at}unc.edu

Distinct isoforms of long chain acyl-CoA synthetases (ACSL) may partition fatty acids towards 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. The data further suggest that translational or post-translational modifications are likely to contribute to the regulation of ACSL isoforms.


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