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Gene Review

Acsl1  -  acyl-CoA synthetase long-chain family...

Rattus norvegicus

Synonyms: ACS, Acas, Acs1, Acsl2, COAA, ...
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Disease relevance of Acsl1


High impact information on Acsl1

  • We report herein the cDNA cloning of a novel rat acyl-CoA synthetase (ACS) that preferentially uses arachidonate and eicosapentaenoate [5].
  • Ad-ACSL1, located on the endoplasmic reticulum but not on mitochondria or plasma membrane, increased ACS specific activity 3.7-fold [6].
  • Long chain fatty acids are converted to acyl-CoAs by acyl-CoA synthetase (fatty acid CoA ligase: AMP forming, E.C.; ACS) [1].
  • In the fadD background, the rat ACS isoforms 1, 2, 3, 4 and 5 oxidized [(14)C]oleate at 5 to 25% of the wild type levels, but only ACS5 restored growth on oleate as the sole carbon source [1].
  • Rodents have five ACS isoforms that differ in substrate specificity, tissue expression, and subcellular localization and are believed to channel fatty acids toward distinct metabolic pathways [1].

Chemical compound and disease context of Acsl1

  • Morris 7800 C1 hepatoma cell acyl-CoA synthetase (ACS) and peroxisomal acyl-CpA oxidase (ACO) were induced by thia fatty acids of all chain lengths, and with the sulphur atom(s) in different positions [7].

Biological context of Acsl1

  • Moreover, intrathecal injection of MK801, a noncompetitive NMDA antagonist, partially prevented these inductions, highlighting the involvement of the neurotransmitter glutamate in the central ACS and ACO up-regulation [8].
  • Two types of acyl-CoA synthetase (ACS), designated ACS1 and ACS2, are structurally similar isozymes with different tissue distributions [9].
  • Through the use of heterodimer-selective compounds, it was demonstrated that the modulatory effect of these rexinoids on FATP-1 and ACS gene expression was mediated through activation of RXR in the context of the PPAR-RXR heterodimer [10].
  • Transverse-plane topography of mitochondrial outer-membrane long-chain acyl-CoA synthetase was investigated using proteases as probes for exposure of crucial domains, i.e. domains containing the active site or otherwise required for enzymatic activity [11].
  • Analysis of two overlapping genomic clones for the rat ACS gene revealed that the three 5'-untranslated regions of the mRNAs are individually encoded by three different exons located within a 20-kilobase genomic fragment [12].

Anatomical context of Acsl1


Associations of Acsl1 with chemical compounds


Other interactions of Acsl1


Analytical, diagnostic and therapeutic context of Acsl1

  • Using semiquantitative RT-PCR, we explored in the neuraxis the mRNA expression of brain acyl-CoA synthetases (ACS) and acyl-CoA oxidase (ACO), which are major fatty acid-metabolizing enzymes, following complete Freund's adjuvant (CFA) injection into a hind paw [8].
  • This ACS PPRE contains three imperfect half sites spaced by 1 and 3 oligonucleotides and binds PPAR.retinoid X receptor heterodimers in gel retardation assays [2].
  • Molecular cloning of cDNA encoding rat very long-chain acyl-CoA synthetase [19].
  • This regulation of FATP and ACS expression by PPAR activators was shown to be at the transcriptional level and could also be reproduced in vitro in cell culture systems [24].
  • Western blot analysis using tissue homogenates of rat liver, heart, kidney, lung, brain, and ileum showed that LACS was found in every tissue investigated, with the greatest expression in the liver [25].


  1. Rat long chain acyl-CoA synthetase 5, but not 1, 2, 3, or 4, complements Escherichia coli fadD. Caviglia, J.M., Li, L.O., Wang, S., DiRusso, C.C., Coleman, R.A., Lewin, T.M. J. Biol. Chem. (2004) [Pubmed]
  2. Induction of the acyl-coenzyme A synthetase gene by fibrates and fatty acids is mediated by a peroxisome proliferator response element in the C promoter. Schoonjans, K., Watanabe, M., Suzuki, H., Mahfoudi, A., Krey, G., Wahli, W., Grimaldi, P., Staels, B., Yamamoto, T., Auwerx, J. J. Biol. Chem. (1995) [Pubmed]
  3. Disruption of the Saccharomyces cerevisiae FAT1 gene decreases very long-chain fatty acyl-CoA synthetase activity and elevates intracellular very long-chain fatty acid concentrations. Watkins, P.A., Lu, J.F., Steinberg, S.J., Gould, S.J., Smith, K.D., Braiterman, L.T. J. Biol. Chem. (1998) [Pubmed]
  4. Rapid enhancement of acyl-CoA synthetase, LPL, and GLUT-4 mRNAs in adipose tissue of VMH rats. Shimomura, I., Takahashi, M., Tokunaga, K., Keno, Y., Nakamura, T., Yamashita, S., Takemura, K., Yamamoto, T., Funahashi, T., Matsuzawa, Y. Am. J. Physiol. (1996) [Pubmed]
  5. A novel arachidonate-preferring acyl-CoA synthetase is present in steroidogenic cells of the rat adrenal, ovary, and testis. Kang, M.J., Fujino, T., Sasano, H., Minekura, H., Yabuki, N., Nagura, H., Iijima, H., Yamamoto, T.T. Proc. Natl. Acad. Sci. U.S.A. (1997) [Pubmed]
  6. Overexpression of Rat Long Chain Acyl-CoA Synthetase 1 Alters Fatty Acid Metabolism in Rat Primary Hepatocytes. Li, L.O., Mashek, D.G., An, J., Doughman, S.D., Newgard, C.B., Coleman, R.A. J. Biol. Chem. (2006) [Pubmed]
  7. Effects of chain length and sulphur position of thia fatty acids on their incorporation into phospholipids in 7800 C1 hepatoma cells and isolated rat hepatocytes, and their effects on fatty acid composition of phospholipids. Wu, P., Grav, H.J., Horn, R., Bremer, J. Biochem. Pharmacol. (1996) [Pubmed]
  8. Up-regulation of fatty acid metabolizing-enzymes mRNA in rat spinal cord during persistent peripheral local inflammation. Benani, A., Vol, C., Heurtaux, T., Asensio, C., Dauça, M., Lapicque, F., Netter, P., Minn, A. Eur. J. Neurosci. (2003) [Pubmed]
  9. Biochemical studies of two rat acyl-CoA synthetases, ACS1 and ACS2. Iijima, H., Fujino, T., Minekura, H., Suzuki, H., Kang, M.J., Yamamoto, T. Eur. J. Biochem. (1996) [Pubmed]
  10. Induction of the fatty acid transport protein 1 and acyl-CoA synthase genes by dimer-selective rexinoids suggests that the peroxisome proliferator-activated receptor-retinoid X receptor heterodimer is their molecular target. Martin, G., Poirier, H., Hennuyer, N., Crombie, D., Fruchart, J.C., Heyman, R.A., Besnard, P., Auwerx, J. J. Biol. Chem. (2000) [Pubmed]
  11. Transverse-plane topography of long-chain acyl-CoA synthetase in the mitochondrial outer membrane. Hesler, C.B., Olymbios, C., Haldar, D. J. Biol. Chem. (1990) [Pubmed]
  12. Multiple promoters in rat acyl-CoA synthetase gene mediate differential expression of multiple transcripts with 5'-end heterogeneity. Suzuki, H., Watanabe, M., Fujino, T., Yamamoto, T. J. Biol. Chem. (1995) [Pubmed]
  13. Acyl-CoA synthetase isoforms 1, 4, and 5 are present in different subcellular membranes in rat liver and can be inhibited independently. Lewin, T.M., Kim, J.H., Granger, D.A., Vance, J.E., Coleman, R.A. J. Biol. Chem. (2001) [Pubmed]
  14. Structure and regulation of rat long-chain acyl-CoA synthetase. Suzuki, H., Kawarabayasi, Y., Kondo, J., Abe, T., Nishikawa, K., Kimura, S., Hashimoto, T., Yamamoto, T. J. Biol. Chem. (1990) [Pubmed]
  15. Troglitazone inhibits fatty acid oxidation and esterification, and gluconeogenesis in isolated hepatocytes from starved rats. Fulgencio, J.P., Kohl, C., Girard, J., Pégorier, J.P. Diabetes (1996) [Pubmed]
  16. Expression and characterization of recombinant rat Acyl-CoA synthetases 1, 4, and 5. Selective inhibition by triacsin C and thiazolidinediones. Kim, J.H., Lewin, T.M., Coleman, R.A. J. Biol. Chem. (2001) [Pubmed]
  17. Engineering of glycerol-stimulated insulin secretion in islet beta cells. Differential metabolic fates of glucose and glycerol provide insight into mechanisms of stimulus-secretion coupling. Noel, R.J., Antinozzi, P.A., McGarry, J.D., Newgard, C.B. J. Biol. Chem. (1997) [Pubmed]
  18. Characterization of liver cholic acid coenzyme A ligase activity. Evidence that separate microsomal enzymes are responsible for cholic acid and fatty acid activation. Polokoff, M.A., Bell, R.M. J. Biol. Chem. (1977) [Pubmed]
  19. Molecular cloning of cDNA encoding rat very long-chain acyl-CoA synthetase. Uchiyama, A., Aoyama, T., Kamijo, K., Uchida, Y., Kondo, N., Orii, T., Hashimoto, T. J. Biol. Chem. (1996) [Pubmed]
  20. The malonyl-CoA-sensitive form of carnitine palmitoyltransferase is not localized exclusively in the outer membrane of rat liver mitochondria. Hoppel, C.L., Kerner, J., Turkaly, P., Turkaly, J., Tandler, B. J. Biol. Chem. (1998) [Pubmed]
  21. Gene expression profiling reveals multiple toxicity endpoints induced by hepatotoxicants. Huang, Q., Jin, X., Gaillard, E.T., Knight, B.L., Pack, F.D., Stoltz, J.H., Jayadev, S., Blanchard, K.T. Mutat. Res. (2004) [Pubmed]
  22. Fatty acyl-CoA oxidase activity is induced before long-chain acyl-CoA hydrolase activity and acyl-CoA binding protein in liver of rat treated with peroxisome proliferating 3-thia fatty acids. Skorve, J., Rosendal, J., Vaagenes, H., Knudsen, J., Lillehaug, J.R., Berge, R.K. Xenobiotica (1995) [Pubmed]
  23. Long-chain acyl-CoA synthetase and "outer" carnitine long-chain acyltransferase activities of intact brown adipose tissue mitochondria. Normann, P.T., Flatmark, T. Biochim. Biophys. Acta (1978) [Pubmed]
  24. Coordinate regulation of the expression of the fatty acid transport protein and acyl-CoA synthetase genes by PPARalpha and PPARgamma activators. Martin, G., Schoonjans, K., Lefebvre, A.M., Staels, B., Auwerx, J. J. Biol. Chem. (1997) [Pubmed]
  25. Expression of rat liver long-chain acyl-CoA synthetase and characterization of its role in the metabolism of R-ibuprofen and other fatty acid-like xenobiotics. Bruggera, R., Reichel, C., Garcia Alia, B., Brune, K., Yamamoto, T., Tegeder, I., Geisslinger, G., Geissinger, G. Biochem. Pharmacol. (2001) [Pubmed]
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