|
|
||||||||
Papers In Press, published online ahead of print June 13, 2006
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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.
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
![]()
CiteULike
Complore
Connotea
Del.icio.us
Digg
Reddit
Technorati What's this?
This article has been cited by other articles:
![]() |
R. R. Almon, E. Yang, W. Lai, I. P. Androulakis, S. Ghimbovschi, E. P. Hoffman, W. J. Jusko, and D. C. DuBois Relationships between circadian rhythms and modulation of gene expression by glucocorticoids in skeletal muscle Am J Physiol Regulatory Integrative Comp Physiol, October 1, 2008; 295(4): R1031 - R1047. [Abstract] [Full Text] [PDF] |
||||
![]() |
J. T. Green, S. K. Orr, and R. P. Bazinet The emerging role of group VI calcium-independent phospholipase A2 in releasing docosahexaenoic acid from brain phospholipids J. Lipid Res., May 1, 2008; 49(5): 939 - 944. [Abstract] [Full Text] [PDF] |
||||
![]() |
J. Westerbacka, M. Kolak, T. Kiviluoto, P. Arkkila, J. Siren, A. Hamsten, R. M. Fisher, and H. Yki-Jarvinen Genes Involved in Fatty Acid Partitioning and Binding, Lipolysis, Monocyte/Macrophage Recruitment, and Inflammation Are Overexpressed in the Human Fatty Liver of Insulin-Resistant Subjects Diabetes, November 1, 2007; 56(11): 2759 - 2765. [Abstract] [Full Text] [PDF] |
||||
![]() |
C. M. Mansbach II and F. Gorelick Development and Physiological Regulation of Intestinal Lipid Absorption. II. Dietary lipid absorption, complex lipid synthesis, and the intracellular packaging and secretion of chylomicrons Am J Physiol Gastrointest Liver Physiol, October 1, 2007; 293(4): G645 - G650. [Abstract] [Full Text] [PDF] |
||||
![]() |
Y. Zhou, P. Abidi, A. Kim, W. Chen, T.-T. Huang, F. B. Kraemer, and J. Liu Transcriptional Activation of Hepatic ACSL3 and ACSL5 by Oncostatin M Reduces Hypertriglyceridemia Through Enhanced {beta}-Oxidation Arterioscler. Thromb. Vasc. Biol., October 1, 2007; 27(10): 2198 - 2205. [Abstract] [Full Text] [PDF] |
||||
![]() |
L. O. Li, D. G. Mashek, J. An, S. D. Doughman, C. B. Newgard, and R. A. Coleman Overexpression of Rat Long Chain Acyl-CoA Synthetase 1 Alters Fatty Acid Metabolism in Rat Primary Hepatocytes J. Biol. Chem., December 1, 2006; 281(48): 37246 - 37255. [Abstract] [Full Text] [PDF] |
||||
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH |
| All ASBMB Journals | Journal of Biological Chemistry |
| Molecular and Cellular Proteomics | ASBMB Today |