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PPAR Research
Volume 2010 (2010), Article ID 435689, 10 pages
http://dx.doi.org/10.1155/2010/435689
Review Article

PPARs: Nuclear Receptors Controlled by, and Controlling, Nutrient Handling through Nuclear and Cytosolic Signaling

1Dipartimento di Scienze Biologiche ed Ambientali, Università degli Studi del Sannio, Via Port'Arsa 11, 82100 Benevento, Italy
2Dipartimento delle Scienze Biologiche, Sezione Fisiologia ed Igiene, Università degli Studi di Napoli “Federico II”, Via Mezzocannone 8, 80134 Napoli, Italy
3Dipartimento di Scienze della Vita, Seconda Università degli Studi di Napoli, Via Vivaldi 43, 81100 Caserta, Italy

Received 28 March 2010; Revised 31 May 2010; Accepted 30 June 2010

Academic Editor: Yaacov Barak

Copyright © 2010 Maria Moreno et al. 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. Nuclear Receptors Nomenclature Committee, “A unified nomenclature system for the nuclear receptor superfamily,” Cell, vol. 97, no. 2, pp. 161–163, 1999. View at Google Scholar · View at Scopus
  2. T. Sher, H.-F. Yi, O. W. McBride, and F. J. Gonzalez, “cDNA cloning, chromosomal mapping, and functional characterization of the human peroxisome proliferator activated receptor,” Biochemistry, vol. 32, no. 21, pp. 5598–5604, 1993. View at Google Scholar · View at Scopus
  3. D. Auboeuf, J. Rieusset, L. Fajas et al., “Tissue distribution and quantification of the expression of mRNAs of peroxisome proliferator-activated receptors and liver X receptor-α in humans: no alteration in adipose tissue of obese and NIDDM patients,” Diabetes, vol. 46, no. 8, pp. 1319–1327, 1997. View at Google Scholar · View at Scopus
  4. J. Skogsberg, K. Kannisto, L. Roshani et al., “Characterization of the human peroxisome proliferator activated receptor delta gene and its expression,” International Journal of Molecular Medicine, vol. 6, no. 1, pp. 73–81, 2000. View at Google Scholar · View at Scopus
  5. L. Fajas, D. Auboeuf, E. Raspé et al., “The organization, promoter analysis, and expression of the human PPARγ gene,” Journal of Biological Chemistry, vol. 272, no. 30, pp. 18779–18789, 1997. View at Publisher · View at Google Scholar · View at Scopus
  6. A. IJpenberg, E. Jeannin, W. Wahli, and B. Desvergne, “Polarity and specific sequence requirements of peroxisome proliferator-activated receptor (PPAR)/retinoid X receptor heterodimer binding to DNA. A functional analysis of the malic enzyme gene PPAR response element,” Journal of Biological Chemistry, vol. 272, no. 32, pp. 20108–20117, 1997. View at Publisher · View at Google Scholar · View at Scopus
  7. S. A. Kliewer, K. Umesono, D. J. Noonan, R. A. Heyman, and R. M. Evans, “Convergence of 9-cis retinoic acid and peroxisome proliferator signalling pathways through heterodimer formation of their receptors,” Nature, vol. 358, no. 6389, pp. 771–774, 1992. View at Publisher · View at Google Scholar · View at Scopus
  8. 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 · View at Scopus
  9. 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 · View at Scopus
  10. R. T. Nolte, G. B. Wisely, S. Westin et al., “Ligand binding and co-activator assembly of the peroxisome proliferator-activated receptor-γ,” Nature, vol. 395, no. 6698, pp. 137–143, 1998. View at Publisher · View at Google Scholar · View at Scopus
  11. I. G. Schulman, G. Shao, and R. A. Heyman, “Transactivation by retinoid X receptor-peroxisome proliferator-activated receptor γ (PPARγ) heterodimers: intermolecular synergy requires only the PPRAγ hormone-dependent activation function,” Molecular and Cellular Biology, vol. 18, no. 6, pp. 3483–3494, 1998. View at Google Scholar · View at Scopus
  12. T. Heinzel, R. M. Lavinsky, T.-M. Mullen et al., “A complex containing N-CoR, mSin3 and histone deacetylase mediates transcriptional repression,” Nature, vol. 387, no. 6628, pp. 43–48, 1997. View at Google Scholar · View at Scopus
  13. V. Cavailles, S. Dauvois, F. L'Horset et al., “Nuclear factor RIP140 modulates transcriptional activation by the estrogen receptor,” EMBO Journal, vol. 14, no. 15, pp. 3741–3751, 1995. View at Google Scholar · View at Scopus
  14. J. D. Chen, K. Umesono, and R. M. Evans, “SMRT isoforms mediate repression and anti-repression of nuclear receptor heterodimers,” Proceedings of the National Academy of Sciences of the United States of America, vol. 93, no. 15, pp. 7567–7571, 1996. View at Publisher · View at Google Scholar · View at Scopus
  15. S. A. Onate, S. Y. Tsai, M.-J. Tsai, and B. W. O'Malley, “Sequence and characterization of a coactivator for the steroid hormone receptor superfamily,” Science, vol. 270, no. 5240, pp. 1354–1357, 1995. View at Google Scholar · View at Scopus
  16. L. Gelman, G. Zhou, L. Fajas, E. Raspé, J.-C. Fruchart, and J. Auwerx, “p300 Interacts with the N- and C-terminal part of PPARγ2 in a ligand-independent and -dependent manner, respectively,” Journal of Biological Chemistry, vol. 274, no. 12, pp. 7681–7688, 1999. View at Publisher · View at Google Scholar · View at Scopus
  17. C. A. Heinlein, H.-J. Ting, S. Yeh, and C. Chang, “Identification of ARA70 as a ligand-enhanced coactivator for the peroxisome proliferator-activated receptor γ,” Journal of Biological Chemistry, vol. 274, no. 23, pp. 16147–16152, 1999. View at Publisher · View at Google Scholar · View at Scopus
  18. C. Lu and S.-Y. Cheng, “Thyroid hormone receptors regulate adipogenesis and carcinogenesis via crosstalk signaling with peroxisome proliferator-activated receptors,” Journal of Molecular Endocrinology, vol. 44, no. 3, pp. 143–154, 2010. View at Publisher · View at Google Scholar · View at Scopus
  19. F. Cioffi, R. Senese, P. de Lange, F. Goglia, A. Lanni, and A. Lombardi, “Uncoupling protection: a complex journey to function discovery,” BioFactors, vol. 35, no. 5, pp. 417–428, 2009. View at Publisher · View at Google Scholar · View at Scopus
  20. P. de Lange, A. Feola, M. Ragni et al., “Differential 3,5,3′-triiodothyronine-mediated regulation of uncoupling protein 3 transcription: role of fatty acids,” Endocrinology, vol. 148, no. 8, pp. 4064–4072, 2007. View at Publisher · View at Google Scholar · View at Scopus
  21. G. Solanes, N. Pedraza, R. Iglesias, M. Giralt, and F. Villarroya, “Functional relationship between MyoD and peroxisome proliferator-activated receptor-dependent regulatory pathways in the control of the human uncoupling protein-3 gene transcription,” Molecular Endocrinology, vol. 17, no. 10, pp. 1944–1958, 2003. View at Publisher · View at Google Scholar · View at Scopus
  22. W. He, Y. Barak, A. Hevener et al., “Adipose-specific peroxisome proliferator-activated receptor γ knockout causes insulin resistance in fat and liver but not in muscle,” Proceedings of the National Academy of Sciences of the United States of America, vol. 100, no. 26, pp. 15712–15717, 2003. View at Publisher · View at Google Scholar · View at Scopus
  23. J. Berger and D. E. Moller, “The mechanisms of action of PPARs,” Annual Review of Medicine, vol. 53, no. 1, pp. 409–435, 2002. View at Publisher · View at Google Scholar · View at Scopus
  24. J. Friedman, “Fat in all the wrong places,” Nature, vol. 415, no. 6869, pp. 268–269, 2002. View at Publisher · View at Google Scholar · View at Scopus
  25. J.-M. Ye, P. J. Doyle, M. A. Iglesias, D. G. Watson, G. J. Cooney, and E. W. Kraegen, “Peroxisome proliferator-activated receptor (PPAR)-α activation lowers muscle lipids and improves insulin sensitivity in high fat-fed rats. Comparison with PPAR-γ activation,” Diabetes, vol. 50, no. 2, pp. 411–417, 2001. View at Google Scholar · View at Scopus
  26. P. Escher, O. Braissant, S. Basu-Modak, L. Michalik, W. Wahli, and B. Desvergne, “Rat PPARs: quantitative analysis in adult rat tissues and regulation in fasting and refeeding,” Endocrinology, vol. 142, no. 10, pp. 4195–4202, 2001. View at Publisher · View at Google Scholar · View at Scopus
  27. P. de Lange, A. Lombardi, E. Silvestri, F. Goglia, A. Lanni, and M. Moreno, “Peroxisome proliferator-activated receptor delta: a conserved director of lipid homeostasis through regulation of the oxidative capacity of muscle,” PPAR Research, vol. 2008, Article ID 172676, 7 pages, 2008. View at Publisher · View at Google Scholar · View at Scopus
  28. B. D. Abbot, “Review of the expression of peroxisome proliferators-activated receptors alpha (PPARalpha), beta (PPARbeta), and gamma (PPARgamma) in rodent and human development,” Reproductive Toxicology, vol. 75, no. 1, pp. 72–77, 2009. View at Google Scholar
  29. Y. Shi, M. Hon, and R. M. Evans, “The peroxisome proliferator-activated receptor δ, an integrator of transcriptional repression and nuclear receptor signaling,” Proceedings of the National Academy of Sciences of the United States of America, vol. 99, no. 5, pp. 2613–2618, 2002. View at Publisher · View at Google Scholar · View at Scopus
  30. M. C. U. Gustafsson, D. Knight, and C. N. A. Palmer, “Ligand modulated antagonism of PPARγ by genomic and non-genomic actions of PPARδ,” PLoS ONE, vol. 4, no. 9, Article ID e7046, 2009. View at Publisher · View at Google Scholar · View at Scopus
  31. T. Ide, H. Shimano, T. Yoshikawa et al., “Cross-talk between peroxisome proliferator-activated receptor (PPAR) α and liver X receptor (LXR) in nutritional regulation of fatty acid metabolism. II. LXRs suppress lipid degradation gene promoters through inhibition of PPAR signaling,” Molecular Endocrinology, vol. 17, no. 7, pp. 1255–1267, 2003. View at Publisher · View at Google Scholar · View at Scopus
  32. T. Yoshikawa, T. Ide, H. Shimano et al., “Cross-talk between peroxisome proliferator-activated receptor (PPAR) α and liver X receptor (LXR) in nutritional regulation of fatty acid metabolism. I. PPARS suppress sterol regulatory element binding protein-1c promoter through inhibition of LXR signaling,” Molecular Endocrinology, vol. 17, no. 7, pp. 1240–1254, 2003. View at Publisher · View at Google Scholar · View at Scopus
  33. K. Matsusue, A. Miyoshi, S. Yamano, and F. J. Gonzalez, “Ligand-activated PPARβ efficiently represses the induction of LXR-dependent promoter activity through competition with RXR,” Molecular and Cellular Endocrinology, vol. 256, no. 1-2, pp. 23–33, 2006. View at Publisher · View at Google Scholar · View at Scopus
  34. R. Chu, L. D. Madison, Y. Lin et al., “Thyroid hormone (T3) inhibits ciprofibrate-induced transcription of genes encoding β-oxidation enzymes: cross talk between peroxisome proliferator and T3 signaling pathways,” Proceedings of the National Academy of Sciences of the United States of America, vol. 92, no. 25, pp. 11593–11597, 1995. View at Publisher · View at Google Scholar · View at Scopus
  35. H. Ying, O. Araki, F. Furuya, Y. Kato, and S.-Y. Cheng, “Impaired adipogenesis caused by a mutated thyroid hormone α1 receptor,” Molecular and Cellular Biology, vol. 27, no. 6, pp. 2359–2371, 2007. View at Publisher · View at Google Scholar · View at Scopus
  36. G. Krey, O. Braissant, F. L'Horset et al., “Fatty acids, eicosanoids, and hypolipidemic agents identified as ligands of peroxisome proliferator-activated receptors by coactivator-dependent receptor ligand assay,” Molecular Endocrinology, vol. 11, no. 6, pp. 779–791, 1997. View at Publisher · View at Google Scholar · View at Scopus
  37. T. Itoh, L. Fairall, K. Amin et al., “Structural basis for the activation of PPARγ by oxidized fatty acids,” Nature Structural and Molecular Biology, vol. 15, no. 9, pp. 924–931, 2008. View at Publisher · View at Google Scholar · View at Scopus
  38. 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 · View at Scopus
  39. D. Cavalieri, E. Calura, C. Romualdi et al., “Filling gaps in PPAR-alpha signaling through comparative nutrigenomics analysis,” BMC Genomics, vol. 10, no. 1, pp. 596–612, 2009. View at Publisher · View at Google Scholar · View at Scopus
  40. L. M. Sanderson, P. J. de Groot, G. J. E. J. Hooiveld et al., “Effect of synthetic dietary triglycerides: a novel research paradigm for nutrigenomics,” PLoS ONE, vol. 27, no. 2, Article ID e1681, 2008. View at Publisher · View at Google Scholar · View at Scopus
  41. S. Surapureddi, S. Yu, H. Bu et al., “Identification of a transcriptionally active peroxisome proliferator-activated receptor α-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 · View at Scopus
  42. R. Nielsen, L. Grøntved, H. G. Stunnenberg, and S. Mandrup, “Peroxisome proliferator-activated receptor subtype- and cell-type-specific activation of genomic target genes upon adenoviral transgene delivery,” Molecular and Cellular Biology, vol. 26, no. 15, pp. 5698–5714, 2006. View at Publisher · View at Google Scholar · View at Scopus
  43. J. C. Yoon, P. Puigserver, G. Chen et al., “Control of hepatic gluconeogenesis through the transcriptional coaotivator PGC-1,” Nature, vol. 413, no. 6852, pp. 131–138, 2001. View at Publisher · View at Google Scholar · View at Scopus
  44. L. M. Sanderson, T. Degenhardt, A. Koppen et al., “Peroxisome proliferator-activated receptor β/δ (PPARβ/δ) but not PPARα serves as a plasma free fatty acid sensor in liver,” Molecular and Cellular Biology, vol. 29, no. 23, pp. 6257–6267, 2009. View at Publisher · View at Google Scholar · View at Scopus
  45. P. de Lange, P. Farina, M. Moreno et al., “Sequential changes in the signal transduction responses of skeletal muscle following food deprivation,” The FASEB Journal, vol. 20, no. 14, pp. 2579–2581, 2006. View at Publisher · View at Google Scholar · View at Scopus
  46. Y.-X. Wang, C.-H. Lee, S. Tiep et al., “Peroxisome-proliferator-activated receptor δ activates fat metabolism to prevent obesity,” Cell, vol. 113, no. 2, pp. 159–170, 2003. View at Publisher · View at Google Scholar · View at Scopus
  47. M. A. Stavinoha, J. W. Ray Spellicy, M. F. Essop et al., “Evidence for mitochondrial thioesterase 1 as a peroxisome proliferator-activated receptor-α-regulated gene in cardiac and skeletal muscle,” American Journal of Physiology, vol. 287, no. 5, pp. E888–E895, 2004. View at Publisher · View at Google Scholar · View at Scopus
  48. Y.-X. Wang, C.-L. Zhang, R. T. Yu et al., “Regulation of muscle fiber type and running endurance by PPARδ,” PLoS Biology, vol. 2, no. 10, article e294, 2004. View at Publisher · View at Google Scholar · View at Scopus
  49. T. Tanaka, J. Yamamoto, S. Iwasaki et al., “Activation of peroxisome proliferator-activated receptor δ induces fatty acid β-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 · View at Scopus
  50. 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 · View at Scopus
  51. K. Tsintzas, K. Jewell, M. Kamran et al., “Differential regulation of metabolic genes in skeletal muscle during starvation and refeeding in humans,” Journal of Physiology, vol. 575, no. 1, pp. 291–303, 2006. View at Publisher · View at Google Scholar · View at Scopus
  52. N. Kubota, Y. Terauchi, H. Miki et al., “PPARγ mediates high-fat diet-induced adipocyte hypertrophy and insulin resistance,” Molecular Cell, vol. 4, no. 4, pp. 597–609, 1999. View at Publisher · View at Google Scholar · View at Scopus
  53. F. Picard, M. Kurtev, N. Chung et al., “Sirt1 promotes fat mobilization in white adipocytes by repressing PPAR-γ,” Nature, vol. 429, no. 6993, pp. 771–776, 2004. View at Publisher · View at Google Scholar · View at Scopus
  54. Y.-K. Koh, M.-Y. Lee, J.-W. Kim et al., “Lipin1 is a key factor for the maturation and maintenance of adipocytes in the regulatory network with CCAAT/enhancer-binding protein α and peroxisome proliferator-activated receptor γ2,” Journal of Biological Chemistry, vol. 283, no. 50, pp. 34896–34906, 2008. View at Publisher · View at Google Scholar · View at Scopus
  55. P. A. Grimaldi, “The roles of PPARs in adipocyte differentiation,” Progress in Lipid Research, vol. 40, no. 4, pp. 269–281, 2001. View at Publisher · View at Google Scholar · View at Scopus
  56. L. M. Sanderson, M. V. Boekschoten, B. Desvergne, M. Müller, and S. Kersten, “Transcriptional profiling reveals divergent roles of PPARα and PPARβ/δ in regulation of gene expression in mouse liver,” Physiological Genomics, vol. 41, no. 1, pp. 42–52, 2010. View at Publisher · View at Google Scholar · View at Scopus
  57. A. Shalev, C. A. Siegrist-Kaiser, P. M. Yen et al., “The peroxisome proliferator-activated receptor α is a phosphoprotein: regulation by insulin,” Endocrinology, vol. 137, no. 10, pp. 4499–4502, 1996. View at Publisher · View at Google Scholar · View at Scopus
  58. P. Fuentes, M. J. Acuña, M. Cifuentes, and C. V. Rojas, “The anti-adipogenic effect of angiotensin II on human preadipose cells involves ERK1,2 activation and PPARG phosphorylation,” Journal of Endocrinology, vol. 206, no. 1, pp. 75–83, 2010. View at Publisher · View at Google Scholar · View at Scopus
  59. C. L. Yun and J. R. Zierath, “AMP-activated protein kinase signaling in metabolic regulation,” Journal of Clinical Investigation, vol. 116, no. 7, pp. 1776–1783, 2006. View at Publisher · View at Google Scholar · View at Scopus
  60. T. Leff, “AMP-activated protein kinase regulates gene expression by direct phosphorylation of nuclear proteins,” Biochemical Society Transactions, vol. 31, no. 1, pp. 224–226, 2003. View at Google Scholar · View at Scopus
  61. M. C. Sugden, P. W. Caton, and M. J. Holness, “PPAR control: it's SIRTainly as easy as PGC,” Journal of Endocrinology, vol. 204, no. 2, pp. 93–104, 2010. View at Publisher · View at Google Scholar · View at Scopus
  62. P. Puigserver and B. M. Spiegelman, “Peroxisome proliferator-activated receptor-γ coactivator 1α (PGC-1α): transcriptional coactivator and metabolic regulator,” Endocrine Reviews, vol. 24, no. 1, pp. 78–90, 2003. View at Publisher · View at Google Scholar · View at Scopus
  63. Y. Nagai, S. Yonemitsu, D. M. Erion et al., “The role of peroxisome proliferator-activated receptor γ coactivator-1 β in the pathogenesis of fructose-induced insulin resistance,” Cell Metabolism, vol. 9, no. 3, pp. 252–264, 2009. View at Publisher · View at Google Scholar · View at Scopus
  64. J. Yang, R. Sanders Williams, and D. P. Kelly, “Bcl3 interacts cooperatively with peroxisome proliferator-activated receptor gamma (PPARγ) coactivator 1α to coactivate nuclear receptors estrogen-related receptor α and PPAR,” Molecular and Cellular Biology, vol. 29, no. 15, pp. 4091–4102, 2009. View at Publisher · View at Google Scholar · View at Scopus
  65. K. Yamagata, H. Furuta, N. Oda et al., “Mutations in the hepatocyte nuclear factor-4α gene in maturity-onset diabetes of the young (MODY1),” Nature, vol. 384, no. 6608, pp. 458–460, 1996. View at Publisher · View at Google Scholar · View at Scopus
  66. J. Nakae, W. H. Biggs III, T. Kitamura et al., “Regulation of insulin action and pancreatic β-cell function by mutated alleles of the gene encoding forkhead transcription factor Foxo1,” Nature Genetics, vol. 32, no. 2, pp. 245–253, 2002. View at Publisher · View at Google Scholar · View at Scopus
  67. P. Puigserver, J. Rhee, J. Donovan et al., “Insulin-regulated hepatic gluconeogenesis through FOXO1-PGC-1α interaction,” Nature, vol. 423, no. 6939, pp. 550–555, 2003. View at Publisher · View at Google Scholar · View at Scopus
  68. R. K. Gupta, M. Z. Vatamaniuk, C. S. Lee et al., “The MODY1 gene HNF-4α regulates selected genes involved in insulin secretion,” Journal of Clinical Investigation, vol. 115, no. 4, pp. 1006–1015, 2005. View at Publisher · View at Google Scholar · View at Scopus
  69. J. Ek, G. Andersen, S. A. Urhammer et al., “Mutation analysis of peroxisome proliferator-activated receptor-γ coactivator-1 (PGC-1) and relationships of identified amino acid polymorphisms to Type II diabetes mellitus,” Diabetologia, vol. 44, no. 12, pp. 2220–2226, 2001. View at Publisher · View at Google Scholar · View at Scopus
  70. K. Hara, K. Tobe, T. Okada et al., “A genetic variation in the PGC-1 gene could confer insulin resistance and susceptibility to type II diabetes,” Diabetologia, vol. 45, no. 5, pp. 740–743, 2002. View at Publisher · View at Google Scholar · View at Scopus
  71. O. H. Mortensen, L. Frandsen, P. Schjerling, E. Nishimura, and N. Grunnet, “PGC-1α and PGC-1β have both similar and distinct effects on myofiber switching toward an oxidative phenotype,” American Journal of Physiology, vol. 291, no. 4, pp. E807–E816, 2006. View at Publisher · View at Google Scholar · View at Scopus
  72. T. C. Leone, J. J. Lehman, B. N. Finck et al., “PGC-1alpha deficiency causes multi-system energy metabolic derangements: muscle dysfunction, abnormal weight control and hepatic steatosis,” PLoS Biology, vol. 3, no. 4, article e101, 2005. View at Google Scholar · View at Scopus
  73. P. P. Roux and J. Blenis, “ERK and p38 MAPK-activated protein kinases: a family of protein kinases with diverse biological functions,” Microbiology and Molecular Biology Reviews, vol. 68, no. 2, pp. 320–344, 2004. View at Publisher · View at Google Scholar · View at Scopus
  74. P. Puigserver, J. Rhee, J. Lin et al., “Cytokine stimulation of energy expenditure through p38 MAP kinase activation of PPARγ coactivator-1,” Molecular Cell, vol. 8, no. 5, pp. 971–982, 2001. View at Publisher · View at Google Scholar · View at Scopus
  75. I. Irrcher, V. Ljubicic, and D. A. Hood, “Interactions between ROS and AMP kinase activity in the regulation of PGC-1α transcription in skeletal muscle cells,” American Journal of Physiology, vol. 296, no. 1, pp. C116–C123, 2009. View at Publisher · View at Google Scholar · View at Scopus
  76. X. Li, B. Monks, Q. Ge, and M. J. Birnbaum, “Akt/PKB regulates hepatic metabolism by directly inhibiting PGC-1α transcription coactivator,” Nature, vol. 447, no. 7147, pp. 1012–1016, 2007. View at Publisher · View at Google Scholar · View at Scopus
  77. V. A. Narkar, M. Downes, R. T. Yu et al., “AMPK and PPARδ agonists are exercise mimetics,” Cell, vol. 134, no. 3, pp. 405–415, 2008. View at Publisher · View at Google Scholar · View at Scopus
  78. D. Kitz Krämer, L. Al-Khalili, S. Perrini et al., “Direct activation of glucose transport in primary human myotubes after activation of peroxisome proliferator—activated receptor δ,” Diabetes, vol. 54, no. 4, pp. 1157–1163, 2005. View at Publisher · View at Google Scholar · View at Scopus
  79. D. K. Krämer, L. Al-Khalili, B. Guigas, Y. Leng, P. M. Garcia-Roves, and A. Krook, “Role of AMP kinase and PPARδ in the regulation of lipid and glucose metabolism in human skeletal muscle,” Journal of Biological Chemistry, vol. 282, no. 27, pp. 19313–19320, 2007. View at Publisher · View at Google Scholar · View at Scopus
  80. C. Lerin, J. T. Rodgers, D. E. Kalume, S.-H. Kim, A. Pandey, and P. Puigserver, “GCN5 acetyltransferase complex controls glucose metabolism through transcriptional repression of PGC-1α,” Cell Metabolism, vol. 3, no. 6, pp. 429–438, 2006. View at Publisher · View at Google Scholar · View at Scopus
  81. Z. Gerhart-Hines, J. T. Rodgers, O. Bare et al., “Metabolic control of muscle mitochondrial function and fatty acid oxidation through SIRT1/PGC-1α,” EMBO Journal, vol. 26, no. 7, pp. 1913–1923, 2007. View at Publisher · View at Google Scholar · View at Scopus
  82. J. T. Rodgers, C. Lerin, W. Haas, S. P. Gygi, B. M. Spiegelman, and P. Puigserver, “Nutrient control of glucose homeostasis through a complex of PGC-1α and SIRT1,” Nature, vol. 434, no. 7029, pp. 113–118, 2005. View at Publisher · View at Google Scholar · View at Scopus
  83. T. J. Kelly, C. Lerin, W. Haas, S. P. Gygi, and P. Puigserver, “GCN5-mediated transcriptional control of the metabolic coactivator PGC-1β through lysine acetylation,” Journal of Biological Chemistry, vol. 284, no. 30, pp. 19945–19952, 2009. View at Publisher · View at Google Scholar · View at Scopus
  84. A. Purushotham, T. T. Schug, Q. Xu, S. Surapureddi, X. Guo, and X. Li, “Hepatocyte-specific deletion of SIRT1 alters fatty acid metabolism and results in hepatic steatosis and inflammation,” Cell Metabolism, vol. 9, no. 4, pp. 327–338, 2009. View at Publisher · View at Google Scholar · View at Scopus
  85. J. T. Rodgers, C. Lerin, Z. Gerhart-Hines, and P. Puigserver, “Metabolic adaptations through the PGC-1α and SIRT1 pathways,” FEBS Letters, vol. 582, no. 1, pp. 46–53, 2008. View at Publisher · View at Google Scholar · View at Scopus
  86. A. S. Banks, N. Kon, C. Knight et al., “SirT1 gain of function increases energy efficiency and prevents diabetes in mice,” Cell Metabolism, vol. 8, no. 4, pp. 333–341, 2008. View at Publisher · View at Google Scholar · View at Scopus
  87. P. T. Pfluger, D. Herranz, S. Velasco-Miguel, M. Serrano, and M. H. Tschöp, “Sirt1 protects against high-fat diet-induced metabolic damage,” Proceedings of the National Academy of Sciences of the United States of America, vol. 105, no. 28, pp. 9793–9798, 2008. View at Publisher · View at Google Scholar · View at Scopus
  88. D. M. Erion, S. Yonemitsu, Y. Nie et al., “SirT1 knockdown in liver decreases basal hepatic glucose production and increases hepatic insulin responsiveness in diabetic rats,” Proceedings of the National Academy of Sciences of the United States of America, vol. 106, no. 27, pp. 11288–11293, 2009. View at Publisher · View at Google Scholar · View at Scopus
  89. C. Teyssier, H. Ma, R. Emter, A. Kralli, and M. R. Stallcup, “Activation of nuclear receptor coactivator PGC-1α by arginine methylation,” Genes and Development, vol. 19, no. 12, pp. 1466–1473, 2005. View at Publisher · View at Google Scholar · View at Scopus
  90. H. Iwasaki, “Impaired PRMT1 activity in the liver and pancreas of type 2 diabetic Goto-Kakizaki rats,” Life Sciences, vol. 85, no. 3-4, pp. 161–166, 2009. View at Publisher · View at Google Scholar · View at Scopus