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PPAR Research
Volume 2007, Article ID 86394, 6 pages
http://dx.doi.org/10.1155/2007/86394
Review Article

Metabolic Functions of Peroxisome Proliferator-Activated Receptor β/δ in Skeletal Muscle

INSERM U636, Centre de Biochimie, UFR Sciences, Université de Nice Sophia Antipolis, Parc Valrose, Nice 06108, France

Received 13 September 2006; Revised 16 November 2006; Accepted 21 November 2006

Academic Editor: Wallace Harrington

Copyright © 2007 Céline Gaudel and Paul A. Grimaldi. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Linked References

  1. R. H. Unger and L. Orci, “Lipotoxic diseases of nonadipose tissues in obesity,” International Journal of Obesity, vol. 24, 4, pp. S28–S32, 2000. View at Publisher · View at Google Scholar
  2. M. Fasshauer and R. Paschke, “Regulation of adipocytokines and insulin resistance,” Diabetologia, vol. 46, no. 12, pp. 1594–1603, 2003. View at Publisher · View at Google Scholar
  3. W. C. Knowler, E. Barrett-Connor, S. E. Fowler et al., “Reduction in the incidence of type 2 diabetes with lifestyle intervention or metformin,” New England Journal of Medicine, vol. 346, no. 6, pp. 393–403, 2002. View at Publisher · View at Google Scholar
  4. I. Issemann, R. A. Prince, J. D. Tugwood, and S. Green, “The peroxisome proliferator-activated receptor: retinoid X receptor heterodimer is activated by fatty acids and fibrate hypolipidaemic drugs,” Journal of Molecular Endocrinology, vol. 11, no. 1, pp. 37–47, 1993. View at Google Scholar
  5. P. Tontonoz, E. Hu, R. A. Graves, A. I. Budavari, and B. M. Spiegelman, “mPPARγ2: tissue-specific regulator of an adipocyte enhancer,” Genes and Development, vol. 8, no. 10, pp. 1224–1234, 1994. View at Publisher · View at Google Scholar
  6. E.-Z. Amri, F. Bonino, G. Ailhaud, N. A. Abumrad, and P. A. Grimaldi, “Cloning of a protein that mediates transcriptional effects of fatty acids in preadipocytes. Homology to peroxisome proliferator-activated receptors,” Journal of Biological Chemistry, vol. 270, no. 5, pp. 2367–2371, 1995. View at Publisher · View at Google Scholar
  7. O. Braissant, F. Foufelle, C. Scotto, M. Dauça, and W. Wahli, “Differential expression of peroxisome proliferator-activated receptors (PPARs): tissue distribution of PPAR-α, -β, and -γ in the adult rat,” Endocrinology, vol. 137, no. 1, pp. 354–366, 1996. View at Publisher · View at Google Scholar
  8. R. T. Nolte, G. B. Wisely, S. Westin et al., “Ligand binding and co-activator assembly of the peroxisome proliferator- activated receptor-?,” Nature, vol. 395, no. 6698, pp. 137–143, 1998. View at Publisher · View at Google Scholar
  9. H. E. Xu, M. H. Lambert, V. G. Montana et al., “Molecular recognition of fatty acids by peroxisome proliferator-activated receptors,” Molecular Cell, vol. 3, no. 3, pp. 397–403, 1999. View at Publisher · View at Google Scholar
  10. L. Michalik and W. Wahli, “Peroxisome proliferator-activated receptors: three isotypes for a multitude of functions,” Current Opinion in Biotechnology, vol. 10, no. 6, pp. 564–570, 1999. View at Publisher · View at Google Scholar
  11. P. Tontonoz, E. Hu, J. Devine, E. G. Beale, and B. M. Spiegelman, “PPARγ2 regulates adipose expression of the phosphoenolpyruvate carboxykinase gene,” Molecular and Cellular Biology, vol. 15, no. 1, pp. 351–357, 1995. View at Google Scholar
  12. S. Surapureddi, S. Yu, H. Bu et al., “Identification of a transcriptionally active peroxisome proliferator-activated receptor a-interacting cofactor complex in rat liver and characterization of PRIC285 as a coactivator,” Proceedings of the National Academy of Sciences of the United States of America, vol. 99, no. 18, pp. 11836–11841, 2002. View at Publisher · View at Google Scholar
  13. P. A. Grimaldi, S. M. Knobel, R. R. Whitesell, and N. A. Abumrad, “Induction of aP2 gene expression by nonmetabolized long-chain fatty acids,” Proceedings of the National Academy of Sciences of the United States of America, vol. 89, no. 22, pp. 10930–10934, 1992. View at Publisher · View at Google Scholar
  14. B. M. Forman, P. Tontonoz, J. Chen, R. P. Brun, B. M. Spiegelman, and R. M. Evans, “15-deoxy-Δ12, 14prostaglandin J2 is a ligand for the adipocyte determination factor PPARγ,” Cell, vol. 83, no. 5, pp. 803–812, 1995. View at Publisher · View at Google Scholar
  15. P. R. Devchand, H. Keller, J. M. Peters, M. Vazquez, F. J. Gonzalez, and W. Wahli, “The PPARα-leukotriene B4 pathway to inflammation control,” Nature, vol. 384, no. 6604, pp. 39–43, 1996. View at Publisher · View at Google Scholar
  16. J. Fu, S. Gaetani, F. Oveisi et al., “Oleylethanolamide regulates feeding and body weight through activation of the nuclear receptor PPAR-a,” Nature, vol. 425, no. 6953, pp. 90–93, 2003. View at Publisher · View at Google Scholar
  17. H. Lim, R. A. Gupta, W.-G. Ma et al., “Cyclo-oxygenase-2-derived prostacyclin mediates embryo implantation in the mouse via PPARd,” Genes and Development, vol. 13, no. 12, pp. 1561–1574, 1999. View at Google Scholar
  18. T. Lemberger, R. Saladin, M. Vázquez et al., “Expression of the peroxisome proliferator-activated receptor a gene is stimulated by stress and follows a diurnal rhythm,” Journal of Biological Chemistry, vol. 271, no. 3, pp. 1764–1769, 1996. View at Publisher · View at Google Scholar
  19. J. M. Lehmann, L. B. Moore, T. A. Smith-Oliver, W. O. Wilkison, T. M. Willson, and S. A. Kliewer, “An antidiabetic thiazolidinedione is a high affinity ligand for peroxisome proliferator-activated receptor γ (PPARγ),” Journal of Biological Chemistry, vol. 270, no. 22, pp. 12953–12956, 1995. View at Publisher · View at Google Scholar
  20. T. Kadowaki, K. Hara, T. Yamauchi, Y. Terauchi, K. Tobe, and R. Nagai, “Molecular mechanism of insulin resistance and obesity,” Experimental Biology and Medicine, vol. 228, no. 10, pp. 1111–1117, 2003. View at Google Scholar
  21. W. R. Oliver Jr., J. L. Shenk, M. R. Snaith et al., “A selective peroxisome proliferator-activated receptor d agonist promotes reverse cholesterol transport,” Proceedings of the National Academy of Sciences of the United States of America, vol. 98, no. 9, pp. 5306–5311, 2001. View at Publisher · View at Google Scholar
  22. T. Tanaka, J. Yamamoto, S. Iwasaki et al., “Activation of peroxisome proliferator-activated receptor d induces fatty acid ß-oxidation in skeletal muscle and attenuates metabolic syndrome,” Proceedings of the National Academy of Sciences of the United States of America, vol. 100, no. 26, pp. 15924–15929, 2003. View at Publisher · View at Google Scholar
  23. M. L. Sznaidman, C. D. Haffner, P. R. Maloney et al., “Novel selective small molecule agonists for peroxisome proliferator-activated receptor d (PPARd)—synthesis and biological activity,” Bioorganic and Medicinal Chemistry Letters, vol. 13, no. 9, pp. 1517–1521, 2003. View at Publisher · View at Google Scholar
  24. Y.-X. Wang, C.-H. Lee, S. Tiep et al., “Peroxisome-proliferator-activated receptor d activates fat metabolism to prevent obesity,” Cell, vol. 113, no. 2, pp. 159–170, 2003. View at Publisher · View at Google Scholar
  25. E. Chevillotte, J. Rieusset, M. Roques, M. Desage, and H. Vidal, “The regulation of uncoupling protein-2 gene expression by ω-6 polyunsaturated fatty acids in human skeletal muscle cells involves multiple pathways, including the nuclear receptor peroxisome proliferator-activated receptor β,” Journal of Biological Chemistry, vol. 276, no. 14, pp. 10853–10860, 2001. View at Publisher · View at Google Scholar
  26. D. Holst, S. Luquet, V. Nogueira, K. Kristiansen, X. Leverve, and P. A. Grimaldi, “Nutritional regulation and role of peroxisome proliferator-activated receptor δ in fatty acid catabolism in skeletal muscle,” Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids, vol. 1633, no. 1, pp. 43–50, 2003. View at Publisher · View at Google Scholar
  27. S. Luquet, J. López-Soriano, D. Holst et al., “Peroxisome proliferator-activated receptor d controls muscle development and oxidative capability,” The FASEB Journal, vol. 17, no. 15, pp. 2299–2301, 2003. View at Publisher · View at Google Scholar
  28. M. J. Watt, R. J. Southgate, A. G. Holmes, and M. A. Febbraio, “Suppression of plasma free fatty acids upregulates peroxisome proliferator-activated receptor (PPAR) α and δ and PPAR coactivator 1α in human skeletal muscle, but not lipid regulatory genes,” Journal of Molecular Endocrinology, vol. 33, no. 2, pp. 533–544, 2004. View at Publisher · View at Google Scholar
  29. D. J. Mahoney, G. Parise, S. Melov, A. Safdar, and M. A. Tarnopolsky, “Analysis of global mRNA expression in human skeletal muscle during recovery from endurance exercise,” The FASEB Journal, vol. 19, no. 11, pp. 1498–1500, 2005. View at Publisher · View at Google Scholar
  30. T. Fritz, D. K. Kramer, H. K. R. Karlsson et al., “Low-intensity exercise increases skeletal muscle protein expression of PPARd and UCP3 in type 2 diabetic patients,” Diabetes/Metabolism Research and Reviews, vol. 22, no. 6, pp. 492–498, 2006. View at Publisher · View at Google Scholar
  31. R. A. DeFronzo, R. Gunnarsson, O. Bjorkman, M. Olsson, and J. Wahren, “Effects of insulin on peripheral and splanchnic glucose metabolism in noninsulin-dependent (type II) diabetes mellitus,” Journal of Clinical Investigation, vol. 76, no. 1, pp. 149–155, 1985. View at Google Scholar
  32. L. J. Goodyear and B. B. Kahn, “Exercise, glucose transport, and insulin sensitivity,” Annual Review of Medicine, vol. 49, pp. 235–261, 1998. View at Publisher · View at Google Scholar
  33. P. Andersen and J. Henriksson, “Training induced changes in the subgroups of human type II skeletal muscle fibres,” Acta Physiologica Scandinavica, vol. 99, no. 1, pp. 123–125, 1977. View at Google Scholar
  34. E. Jansson and L. Kaijser, “Muscle adaptation to extreme endurance training in man,” Acta Physiologica Scandinavica, vol. 100, no. 3, pp. 315–324, 1977. View at Google Scholar
  35. D. L. Allen, B. C. Harrison, A. Maass, M. L. Bell, W. C. Byrnes, and L. A. Leinwand, “Cardiac and skeletal muscle adaptations to voluntary wheel running in the mouse,” Journal of Applied Physiology, vol. 90, no. 5, pp. 1900–1908, 2001. View at Google Scholar
  36. J. Mercier, A. Perez-Martin, X. Bigard, and R. Ventura, “Muscle plasticity and metabolism: effects of exercise and chronic diseases,” Molecular Aspects of Medicine, vol. 20, no. 6, pp. 319–373, 1999. View at Publisher · View at Google Scholar
  37. C. J. Tanner, H. A. Barakat, G. L. Dohm et al., “Muscle fiber type is associated with obesity and weight loss,” American Journal of Physiology - Endocrinology and Metabolism, vol. 282, no. 6, pp. E1191–E1196, 2002. View at Google Scholar
  38. D. M. Muoio, P. S. MacLean, D. B. Lang et al., “Fatty acid homeostasis and induction of lipid regulatory genes in skeletal muscles of peroxisome proliferator-activated receptor (PPAR) a knock-out mice. Evidence for compensatory regulation by PPARd,” Journal of Biological Chemistry, vol. 277, no. 29, pp. 26089–26097, 2002. View at Publisher · View at Google Scholar
  39. U. Dressel, T. L. Allen, J. B. Pippal, P. R. Rohde, P. Lau, and G. E. O. Muscat, “The peroxisome proliferator-activated receptor β/δ agonist, GW501516, regulates the expression of genes involved in lipid catabolism and energy uncoupling in skeletal muscle cells,” Molecular Endocrinology, vol. 17, no. 12, pp. 2477–2493, 2003. View at Publisher · View at Google Scholar
  40. Y.-X. Wang, C.-L. Zhang, R. T. Yu et al., “Regulation of muscle fiber type and running endurance by PPARd,” PLoS Biology, vol. 2, no. 10, p. e294, 2004. View at Publisher · View at Google Scholar
  41. J. Lin, H. Wu, P. T. Tarr et al., “Transcriptional co-activator PGC-1a drives the formation of slow-twitch muscle fibres,” Nature, vol. 418, no. 6899, pp. 797–801, 2002. View at Publisher · View at Google Scholar
  42. J. López-Soriano, C. Chiellini, M. Maffei, P. A. Grimaldi, and J. M. Argilés, “Roles of skeletal muscle and peroxisome proliferators-activated receptors in the development and treatment of obesity,” Endocrine Reviews, vol. 27, no. 3, pp. 318–329, 2006. View at Publisher · View at Google Scholar