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PPAR Research
Volume 2012, Article ID 362361, 9 pages
http://dx.doi.org/10.1155/2012/362361
Review Article

The Role of PPAR in the Transcriptional Control by Agonists and Antagonists

Department of Integrative Physiology and Bio-System Control, Shinshu University School of Medicine, 3-1-1 Asahi, Matsumoto, Nagano 390-8621, Japan

Received 18 January 2012; Accepted 2 April 2012

Academic Editor: Shigehiro Katayama

Copyright © 2012 Tamotsu Tsukahara. 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. I. Issemann and S. Green, “Activation of a member of the steroid hormone receptor superfamily by peroxisome proliferators,” Nature, vol. 347, no. 6294, pp. 645–650, 1990. View at Publisher · View at Google Scholar · View at Scopus
  2. J. P. Renaud and D. Moras, “Structural studies on nuclear receptors,” Cellular and Molecular Life Sciences, vol. 57, no. 12, pp. 1748–1769, 2000. View at Google Scholar · View at Scopus
  3. C. Dreyer, G. Krey, H. Keller, F. Givel, G. Helftenbein, and W. Wahli, “Control of the peroxisomal β-oxidation pathway by a novel family of nuclear hormone receptors,” Cell, vol. 68, no. 5, pp. 879–887, 1992. View at Publisher · View at Google Scholar · View at Scopus
  4. M. Robinson-Rechavi, A. S. Carpentier, M. Duffraisse, and V. Laudet, “How many nuclear hormone receptors are there in the human genome?” Trends in Genetics, vol. 17, no. 10, pp. 554–556, 2001. View at Publisher · View at Google Scholar · View at Scopus
  5. T. Gulick, S. Cresci, T. Caira, D. D. Moore, and D. P. Kelly, “The peroxisome proliferator-activated receptor regulates mitochondrial fatty acid oxidative enzyme gene expression,” Proceedings of the National Academy of Sciences of the United States of America, vol. 91, no. 23, pp. 11012–11016, 1994. View at Publisher · View at Google Scholar · View at Scopus
  6. S. Kersten, J. Seydoux, J. M. Peters, F. J. Gonzalez, B. Desvergne, and W. Wahli, “Peroxisome proliferator-activated receptor α mediates the adaptive response to fasting,” Journal of Clinical Investigation, vol. 103, no. 11, pp. 1489–1498, 1999. View at Google Scholar · View at Scopus
  7. C. N. Palmer, M. H. Hsu, K. J. Griffin, J. L. Raucy, and E. F. Johnson, “Peroxisome proliferator activated receptor-α expression in human liver,” Molecular Pharmacology, vol. 53, no. 1, pp. 14–22, 1998. View at Google Scholar · View at Scopus
  8. S. M. Reilly, P. Bhargava, S. Liu et al., “Nuclear receptor corepressor SMRT regulates mitochondrial oxidative metabolism and mediates aging-related metabolic deterioration,” Cell Metabolism, vol. 12, no. 6, pp. 643–653, 2010. View at Publisher · View at Google Scholar · View at Scopus
  9. P. Ferré, “The biology of peroxisome proliferator-activated receptors: relationship with Lipid metabolism and insulin sensitivity,” Diabetes, vol. 53, Supplement 1, pp. S43–S50, 2004. View at Google Scholar · View at Scopus
  10. G. Krey, H. Keller, A. Mahfoudi et al., “Xenopus peroxisome proliferator activated receptors: genomic organization, response element recognition, heterodimer formation with retinoid x receptor and activation by fatty acids,” Journal of Steroid Biochemistry and Molecular Biology, vol. 47, no. 1–6, pp. 65–73, 1993. View at Google Scholar · View at Scopus
  11. A. Elbrecht, Y. Chen, C. A. Cullinan et al., “Molecular cloning, expression and characterization of human peroxisome proliferator activated receptors γ1 and γ2,” Biochemical and Biophysical Research Communications, vol. 224, no. 2, pp. 431–437, 1996. View at Publisher · View at Google Scholar · View at Scopus
  12. J. M. Way, W. W. Harrington, K. K. Brown et al., “Comprehensive messenger ribonucleic acid profiling reveals that peroxisome proliferator-activated receptor γ activation has coordinate effects on gene expression in multiple insulin-sensitive tissues,” Endocrinology, vol. 142, no. 3, pp. 1269–1277, 2001. View at Publisher · View at Google Scholar · View at Scopus
  13. C. Zhang, D. L. Baker, S. Yasuda et al., “Lysophosphatidic acid induces neointima formation through PPARγ activation,” Journal of Experimental Medicine, vol. 199, no. 6, pp. 763–774, 2004. View at Publisher · View at Google Scholar · View at Scopus
  14. T. Tsukahara, R. Tsukahara, Y. Fujiwara et al., “Phospholipase D2-dependent inhibition of the nuclear hormone receptor PPARγ by cyclic phosphatidic acid,” Molecular Cell, vol. 39, no. 3, pp. 421–432, 2010. View at Publisher · View at Google Scholar · View at Scopus
  15. F. Zheng, F. Cornacchia, I. Schulman et al., “Development of albuminuria and glomerular lesions in normoglycemic B6 recipients of db/db mice bone marrow: the role of mesangial cell progenitors,” Diabetes, vol. 53, no. 9, pp. 2420–2427, 2004. View at Publisher · View at Google Scholar · View at Scopus
  16. E. Rother, R. Brandl, D. L. Baker et al., “Subtype-selective antagonists of lysophosphatidic acid receptors inhibit platelet activation triggered by the lipid core of atherosclerotic plaques,” Circulation, vol. 108, no. 6, pp. 741–747, 2003. View at Publisher · View at Google Scholar · View at Scopus
  17. Y. Oishi-Tanaka and C. K. Glass, “A new role for cyclic phosphatidic acid as a PPARγ antagonist,” Cell Metabolism, vol. 12, no. 3, pp. 207–208, 2010. View at Publisher · View at Google Scholar · View at Scopus
  18. A. M. Sharma and B. Staels, “Review: peroxisome proliferator-activated receptor γ and adipose tissue—Understanding obesity-related changes in regulation of lipid and glucose metabolism,” Journal of Clinical Endocrinology and Metabolism, vol. 92, no. 2, pp. 386–395, 2007. View at Publisher · View at Google Scholar · View at Scopus
  19. J. P. Whitehead, “Diabetes: new conductors for the peroxisome proliferator-activated receptor γ (PPARγ) orchestra,” International Journal of Biochemistry and Cell Biology, vol. 43, no. 8, pp. 1071–1074, 2011. View at Publisher · View at Google Scholar · View at Scopus
  20. P. Tontonoz, E. Hu, and B. M. Spiegelman, “Stimulation of adipogenesis in fibroblasts by PPARγ2, a lipid-activated transcription factor,” Cell, vol. 79, no. 7, pp. 1147–1156, 1994. View at Google Scholar · View at Scopus
  21. 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
  22. O. A. MacDougald and M. D. Lane, “Transcriptional regulation of gene expression during adipocyte differentiation,” Annual Review of Biochemistry, vol. 64, pp. 345–373, 1995. View at Google Scholar · View at Scopus
  23. L. Nagy, P. Tontonoz, J. G. Alvarez, H. Chen, and R. M. Evans, “Oxidized LDL regulates macrophage gene expression through ligand activation of PPARγ,” Cell, vol. 93, no. 2, pp. 229–240, 1998. View at Publisher · View at Google Scholar · View at Scopus
  24. C. Huin, L. Corriveau, A. Bianchi et al., “Differential expression of peroxisome proliferator-activated receptors (PPARs) in the developing human fetal digestive tract,” Journal of Histochemistry and Cytochemistry, vol. 48, no. 5, pp. 603–611, 2000. View at Google Scholar · View at Scopus
  25. C. W. Cheon, D. H. Kim, D. H. Kim, Y. H. Cho, and J. H. Kim, “Effects of ciglitazone and troglitazone on the proliferation of human stomach cancer cells,” World Journal of Gastroenterology, vol. 15, no. 3, pp. 310–320, 2009. View at Publisher · View at Google Scholar · View at Scopus
  26. P. Sarraf, E. Mueller, D. Jones et al., “Differentiation and reversal of malignant changes in colon cancer through PPARγ,” Nature Medicine, vol. 4, no. 9, pp. 1046–1052, 1998. View at Publisher · View at Google Scholar · View at Scopus
  27. E. Saez, P. Tontonoz, M. C. Nelson et al., “Activators of the nuclear receptor PPARγ enhance colon polyp formation,” Nature Medicine, vol. 4, no. 9, pp. 1058–1061, 1998. View at Publisher · View at Google Scholar · View at Scopus
  28. Y. Dai and W. H. Wang, “Peroxisome proliferator-activated receptor γ and colorectal cancer,” World Journal of Gastrointestinal Oncology, vol. 2, no. 3, pp. 159–164, 2010. View at Publisher · View at Google Scholar
  29. H. S. Camp, O. Li, S. C. Wise et al., “Differential activation of peroxisome proliferator-activated receptor-γ by troglitazone and rosiglitazone,” Diabetes, vol. 49, no. 4, pp. 539–547, 2000. View at Google Scholar · View at Scopus
  30. D. J. Mangelsdorf, C. Thummel, M. Beato et al., “The nuclear receptor super-family: the second decade,” Cell, vol. 83, no. 6, pp. 835–839, 1995. View at Google Scholar · View at Scopus
  31. A. H. Brivanlou and J. E. Darnell Jr., “Signal transduction and the control of gene expression,” Science, vol. 295, no. 5556, pp. 813–818, 2002. View at Publisher · View at Google Scholar · View at Scopus
  32. 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
  33. M. Schupp and M. A. Lazar, “Endogenous ligands for nuclear receptors: digging deeper,” Journal of Biological Chemistry, vol. 285, no. 52, pp. 40409–40415, 2010. View at Publisher · View at Google Scholar · View at Scopus
  34. 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 · View at Scopus
  35. B. J. Goldstein, “Rosiglitazone,” International Journal of Clinical Practice, vol. 54, no. 5, pp. 333–337, 2000. View at Google Scholar
  36. J. M. Lenhard, S. A. Kliewer, M. A. Paulik, K. D. Plunket, J. M. Lehmann, and J. E. Weiel, “Effects of troglitazone and metformin on glucose and lipid metabolism. Alterations of two distinct molecular pathways,” Biochemical Pharmacology, vol. 54, no. 7, pp. 801–808, 1997. View at Publisher · View at Google Scholar · View at Scopus
  37. M. Wang, S. C. Wise, T. Leff, and T. Z. Su, “Troglitazone, an antidiabetic agent, inhibits cholesterol biosynthesis through a mechanism independent of peroxisome proliferator-activated receptor-γ,” Diabetes, vol. 48, no. 2, pp. 254–260, 1999. View at Publisher · View at Google Scholar · View at Scopus
  38. J. M. Lawrence and J. Reckless, “Pioglitazone,” International Journal of Clinical Practice, vol. 54, no. 9, pp. 614–618, 2000. View at Google Scholar · View at Scopus
  39. P. S. Gillies and C. J. Dunn, “Pioglitazone,” Drugs, vol. 60, no. 2, pp. 333–343, 2000. View at Google Scholar · View at Scopus
  40. S. W. Park, J. H. Yi, G. Miranpuri et al., “Thiazolidinedione class of peroxisome proliferator-activated receptor γ agonists prevents neuronal damage, motor dysfunction, myelin loss, neuropathic pain, and inflammation after spinal cord injury in adult rats,” Journal of Pharmacology and Experimental Therapeutics, vol. 320, no. 3, pp. 1002–1012, 2007. View at Publisher · View at Google Scholar · View at Scopus
  41. M. A. Peraza, A. D. Burdick, H. E. Marin, F. J. Gonzalez, and J. M. Peters, “The toxicology of ligands for peroxisome proliferator-activated receptors (PPAR),” Toxicological Sciences, vol. 90, no. 2, pp. 269–295, 2006. View at Publisher · View at Google Scholar · View at Scopus
  42. C. E. Clay, A. M. Namen, G. I. Atsumi et al., “Magnitude of peroxisome proliferator-activated receptor-γ activation is associated with important and seemingly opposite biological responses in breast cancer cells,” Journal of Investigative Medicine, vol. 49, no. 5, pp. 413–420, 2001. View at Google Scholar · View at Scopus
  43. D. Panigrahy, S. Huang, M. W. Kieran, and A. Kaipainen, “PPARγ as a therapeutic target for tumor angiogenesis and metastasis,” Cancer Biology and Therapy, vol. 4, no. 7, pp. 687–693, 2005. View at Google Scholar · View at Scopus
  44. C. D. Allred, D. R. Talbert, R. C. Southard, X. Wang, and M. W. Kilgore, “PPARγ1 as a molecular target of eicosapentaenoic acid in human colon cancer (HT-29) cells,” Journal of Nutrition, vol. 138, no. 2, pp. 250–256, 2008. View at Google Scholar · View at Scopus
  45. E. Capobianco, V. White, R. Higa, N. Martínez, and A. Jawerbaum, “Effects of natural ligands of PPARγ on lipid metabolism in placental tissues from healthy and diabetic rats,” Molecular Human Reproduction, vol. 14, no. 8, pp. 491–499, 2008. View at Publisher · View at Google Scholar · View at Scopus
  46. B. M. Forman, P. Tontonoz, J. Chen, R. P. Brun, B. M. Spiegelman, and R. M. Evans, “15-deoxy-Δ12, 14-prostaglandin J2 is a ligand for the adipocyte determination factor PPARγ,” Cell, vol. 83, no. 5, pp. 803–812, 1995. View at Google Scholar · View at Scopus
  47. K. Yu, W. Bayona, C. B. Kallen et al., “Differential activation of peroxisome proliferator-activated receptors by eicosanoids,” Journal of Biological Chemistry, vol. 270, no. 41, pp. 23975–23983, 1995. View at Publisher · View at Google Scholar · View at Scopus
  48. S. A. Kliewer, J. M. Lenhard, T. M. Willson, I. Patel, D. C. Morris, and J. M. Lehmann, “A prostaglandin J2 metabolite binds peroxisome proliferator-activated receptor γ and promotes adipocyte differentiation,” Cell, vol. 83, no. 5, pp. 813–819, 1995. View at Google Scholar · View at Scopus
  49. Y. Kobayashi, S. Ueki, G. Mahemuti et al., “Physiological levels of 15-deoxy-Δ12,14-prostaglandin J2 prime eotaxin-induced chemotaxis on human eosinophils through peroxisome proliferator-activated receptor-γ ligation,” Journal of Immunology, vol. 175, no. 9, pp. 5744–5750, 2005. View at Google Scholar · View at Scopus
  50. E. H. Kim, H. K. Na, D. H. Kim et al., “15-Deoxy-Δ12,14-prostaglandin J2 induces COX-2 expression through Akt-driven AP-1 activation in human breast cancer cells: a potential role of ROS,” Carcinogenesis, vol. 29, no. 4, pp. 688–695, 2008. View at Publisher · View at Google Scholar · View at Scopus
  51. S. J. Lee, M. S. Kim, J. Y. Park, J. S. Woo, and Y. K. Kim, “15-Deoxy-Δ12,14-prostaglandin J2 induces apoptosis via JNK-mediated mitochondrial pathway in osteoblastic cells,” Toxicology, vol. 248, no. 2-3, pp. 121–129, 2008. View at Publisher · View at Google Scholar · View at Scopus
  52. T. M. McIntyre, A. V. Pontsler, A. R. Silva et al., “Identification of an intracellular receptor for lysophosphatidic acid (LPA): LPA is a transcellular PPARγ agonist,” Proceedings of the National Academy of Sciences of the United States of America, vol. 100, no. 1, pp. 131–136, 2003. View at Publisher · View at Google Scholar · View at Scopus
  53. T. Tsukahara, R. Tsukahara, S. Yasuda et al., “Different residues mediate recognition of 1-O-oleyl-lysophosphatidic acid and rosiglitazone in the ligand binding domain of peroxisome proliferator-activated receptor γ,” Journal of Biological Chemistry, vol. 281, no. 6, pp. 3398–3407, 2006. View at Publisher · View at Google Scholar · View at Scopus
  54. S. S. Davies, A. V. Pontsler, G. K. Marathe et al., “Oxidized alkyl phospholipids are specific, high affinity peroxisome proliferator-activated receptor γ ligands and agonists,” Journal of Biological Chemistry, vol. 276, no. 19, pp. 16015–16023, 2001. View at Publisher · View at Google Scholar · View at Scopus
  55. Y. Li, J. Zhang, F. J. Schopfer et al., “Molecular recognition of nitrated fatty acids by PPARγ,” Nature Structural and Molecular Biology, vol. 15, no. 8, pp. 865–867, 2008. View at Publisher · View at Google Scholar · View at Scopus
  56. W. H. Moolenaar, K. Jalink, and E. J. van Corven, “Lysophosphatidic acid: a bioactive phospholipid with growth factor-like properties,” Reviews of Physiology Biochemistry and Pharmacology, vol. 119, pp. 47–65, 1992. View at Google Scholar · View at Scopus
  57. G. Tigyi, D. L. Dyer, and R. Miledi, “Lysophosphatidic acid possesses dual action in cell proliferation,” Proceedings of the National Academy of Sciences of the United States of America, vol. 91, no. 5, pp. 1908–1912, 1994. View at Google Scholar · View at Scopus
  58. G. Tigyi and A. L. Parrill, “Molecular mechanisms of lysophosphatidic acid action,” Progress in Lipid Research, vol. 42, no. 6, pp. 498–526, 2003. View at Publisher · View at Google Scholar · View at Scopus
  59. C. M. Stapleton, D. G. Mashek, S. Wang et al., “Lysophosphatidic acid activates peroxisome proliferator activated receptor-γ in CHO cells that over-express glycerol 3-phosphate acyltransferase-1,” PLoS ONE, vol. 6, no. 4, Article ID e18932, 2011. View at Publisher · View at Google Scholar · View at Scopus
  60. C. M. Mendel and D. B. Mendel, ““Non-specific” binding. The problem, and a solution,” Biochemical Journal, vol. 228, no. 1, pp. 269–272, 1985. View at Google Scholar · View at Scopus
  61. H. E. Xu, M. H. Lambert, V. G. Montana et al., “Structural determinants of ligand binding selectivity between the peroxisome proliferator-activated receptors,” Proceedings of the National Academy of Sciences of the United States of America, vol. 98, no. 24, pp. 13919–13924, 2001. View at Publisher · View at Google Scholar · View at Scopus
  62. B. Staels and J. C. Fruchart, “Therapeutic roles of peroxisome proliferator-activated receptor agonists,” Diabetes, vol. 54, no. 8, pp. 2460–2470, 2005. View at Publisher · View at Google Scholar · View at Scopus
  63. M. K. Racke, A. R. Gocke, M. Muir, A. Diab, P. D. Drew, and A. E. Lovett-Racke, “Nuclear receptors and autoimmune disease: the potential of PPAR agonists to treat multiple sclerosis,” Journal of Nutrition, vol. 136, no. 3, pp. 700–703, 2006. View at Google Scholar · View at Scopus
  64. M. G. Belvisi and D. J. Hele, “Peroxisome proliferator-activated receptors as novel targets in lung disease,” Chest, vol. 134, no. 1, pp. 152–157, 2008. View at Publisher · View at Google Scholar · View at Scopus
  65. T. Sato, H. Hanyu, K. Hirao, H. Kanetaka, H. Sakurai, and T. Iwamoto, “Efficacy of PPAR-γ agonist pioglitazone in mild Alzheimer disease,” Neurobiology of Aging, vol. 32, no. 9, pp. 1626–1633, 2011. View at Publisher · View at Google Scholar · View at Scopus
  66. H. M. Wright, C. B. Clish, T. Mikami et al., “A synthetic antagonist for the peroxisome proliferator-activated receptor γ inhibits adipocyte differentiation,” Journal of Biological Chemistry, vol. 275, no. 3, pp. 1873–1877, 2000. View at Publisher · View at Google Scholar · View at Scopus
  67. D. Bishop-Bailey, T. Hla, and T. D. Warner, “Bisphenol A diglycidyl ether (BADGE) is a PPARγ agonist in an ECV304 cell line,” British Journal of Pharmacology, vol. 131, no. 4, pp. 651–654, 2000. View at Google Scholar · View at Scopus
  68. M. Nakamuta, M. Enjoji, K. Uchimura et al., “Bisphenol A diglycidyl ether (BADGE) suppresses tumor necrosis factor-α production as a PPARγ agonist in the murine macrophage-like cell line, RAW 264.7,” Cell Biology International, vol. 26, no. 3, pp. 235–241, 2002. View at Publisher · View at Google Scholar · View at Scopus
  69. J. Rieusset, F. Touri, L. Michalik et al., “A new selective peroxisome proliferator-activated receptor γ antagonist with antiobesity and antidiabetic activity,” Molecular Endocrinology, vol. 16, no. 11, pp. 2628–2644, 2002. View at Publisher · View at Google Scholar · View at Scopus
  70. H. S. Camp, A. Chaudhry, and T. Leff, “A novel potent antagonist of peroxisome proliferator-activated receptor γ blocks adipocyte differentiation but does not revert the phenotype of terminally differentiated adipocytes,” Endocrinology, vol. 142, no. 7, pp. 3207–3213, 2001. View at Publisher · View at Google Scholar · View at Scopus
  71. L. M. Leesnitzer, D. J. Parks, R. K. Bledsoe et al., “Functional consequences of cysteine modification in the ligand binding sites of peroxisome proliferator activated receptors by GW9662,” Biochemistry, vol. 41, no. 21, pp. 6640–6650, 2002. View at Publisher · View at Google Scholar · View at Scopus
  72. L. Al-Alem, R. C. Southard, M. W. Kilgore, and T. E. Curry, “Specific thiazolidinediones inhibit ovarian cancer cell line proliferation and cause cell cycle arrest in a PPARγ independent manner,” PLoS ONE, vol. 6, no. 1, Article ID e16179, 2011. View at Publisher · View at Google Scholar · View at Scopus
  73. G. Lee, F. Elwood, J. McNally et al., “T0070907, a selective ligand for peroxisome proliferator-activated receptor γ, functions as an antagonist of biochemical and cellular activities,” Journal of Biological Chemistry, vol. 277, no. 22, pp. 19649–19657, 2002. View at Publisher · View at Google Scholar · View at Scopus
  74. A. J. Horlein, A. M. Naar, T. Heinzel et al., “Ligand-independent repression by the thyroid hormone receptor mediated by a nuclear receptor co-repressor,” Nature, vol. 377, no. 6548, pp. 397–404, 1995. View at Google Scholar · View at Scopus
  75. M. J. Reginato, S. L. Krakow, S. T. Bailey, and M. A. Lazar, “Prostaglandins promote and block adipogenesis through opposing effects on peroxisome proliferator-activated receptor γ,” Journal of Biological Chemistry, vol. 273, no. 4, pp. 1855–1858, 1998. View at Publisher · View at Google Scholar · View at Scopus
  76. S. J. Vane, “Differential inhibition of cyclooxygenase isoforms: an explanation of the action of NSAIDs,” Journal of Clinical Rheumatology, vol. 4, supplement 5, pp. S3–S10, 1998. View at Google Scholar · View at Scopus
  77. K. Murakami-Murofushi, M. Mukai, S. Kobayashi, T. Kobayashi, G. Tigyi, and H. Murofushi, “A novel lipid mediator, cyclic phosphatidic acid (cPA), and its biological functions,” Annals of the New York Academy of Sciences, vol. 905, pp. 319–321, 2000. View at Google Scholar · View at Scopus
  78. Y. Fujiwara, “Cyclic phosphatidic acid—a unique bioactive phospholipid,” Biochimica et Biophysica Acta, vol. 1781, no. 9, pp. 519–524, 2008. View at Publisher · View at Google Scholar · View at Scopus
  79. K. Murakami-Murofushi, A. Uchiyama, Y. Fujiwara et al., “Biological functions of a novel lipid mediator, cyclic phosphatidic acid,” Biochimica et Biophysica Acta, vol. 1582, no. 1–3, pp. 1–7, 2002. View at Publisher · View at Google Scholar · View at Scopus
  80. D. L. Bakera, Y. Fujiwara, K. R. Pigg et al., “Carba analogs of cyclic phosphatidic acid are selective inhibitors of autotaxin and cancer cell invasion and metastasis,” Journal of Biological Chemistry, vol. 281, no. 32, pp. 22786–22793, 2006. View at Publisher · View at Google Scholar · View at Scopus
  81. A. Uchiyama, M. Mukai, Y. Fujiwara et al., “Inhibition of transcellular tumor cell migration and metastasis by novel carba-derivatives of cyclic phosphatidic acid,” Biochimica et Biophysica Acta, vol. 1771, no. 1, pp. 103–112, 2007. View at Publisher · View at Google Scholar · View at Scopus
  82. S. Sugii and R. M. Evans, “Epigenetic codes of PPARγ in metabolic disease,” FEBS Letters, vol. 585, no. 13, pp. 2121–2128, 2011. View at Publisher · View at Google Scholar · View at Scopus
  83. M. Esteller, “Cancer epigenomics: DNA methylomes and histone-modification maps,” Nature Reviews Genetics, vol. 8, no. 4, pp. 286–298, 2007. View at Publisher · View at Google Scholar · View at Scopus
  84. J. P. Hamilton, “Epigenetics: principles and practice,” Digestive Diseases, vol. 29, no. 2, pp. 130–135, 2011. View at Publisher · View at Google Scholar · View at Scopus
  85. A. P. Bird and A. P. Wolffe, “Methylation-induced repression-belts, braces, and chromatin,” Cell, vol. 99, no. 5, pp. 451–454, 1999. View at Google Scholar · View at Scopus
  86. M. M. Musri, R. Gomis, and M. Párrizas, “Chromatin and chromatin-modifying proteins in adipogenesis,” Biochemistry and Cell Biology, vol. 85, no. 4, pp. 397–410, 2007. View at Publisher · View at Google Scholar · View at Scopus
  87. K. Fujiki, F. Kano, K. Shiota, and M. Murata, “Expression of the peroxisome proliferator activated receptor γ gene is repressed by DNA methylation in visceral adipose tissue of mouse models of diabetes,” BMC Biology, vol. 7, article 38, 2009. View at Publisher · View at Google Scholar · View at Scopus
  88. C. D. Green and J. D. J. Han, “Epigenetic regulation by nuclear receptors,” Epigenomics, vol. 3, no. 1, pp. 59–72, 2011. View at Publisher · View at Google Scholar · View at Scopus
  89. M. Grunstein, “Histone acetylation in chromatin structure and transcription,” Nature, vol. 389, no. 6649, pp. 349–352, 1997. View at Publisher · View at Google Scholar · View at Scopus
  90. J. Zhang, T. M. Henagan, Z. Gao, and J. Ye, “Inhibition of glyceroneogenesis by histone deacetylase 3 contributes to lipodystrophy in mice with adipose tissue inflammation,” Endocrinology, vol. 152, no. 5, pp. 1829–1838, 2011. View at Publisher · View at Google Scholar · View at Scopus
  91. O. Hermanson, C. K. Glass, and M. G. Rosenfeld, “Nuclear receptor coregulators: multiple modes of modification,” Trends in Endocrinology and Metabolism, vol. 13, no. 2, pp. 55–60, 2002. View at Publisher · View at Google Scholar · View at Scopus
  92. A. Baniahmad, “Nuclear hormone receptor co-repressors,” Journal of Steroid Biochemistry and Molecular Biology, vol. 93, no. 2–5, pp. 89–97, 2005. View at Publisher · View at Google Scholar · View at Scopus
  93. N. Heldring, T. Pawson, D. McDonnell, E. Treuter, J. Å. Gustafsson, and A. C. Pike, “Structural insights into corepressor recognition by antagonist-bound estrogen receptors,” Journal of Biological Chemistry, vol. 282, no. 14, pp. 10449–10455, 2007. View at Publisher · View at Google Scholar · View at Scopus
  94. M. G. Rosenfeld, V. V. Lunyak, and C. K. Glass, “Sensors and signals: a coactivator/corepressor/epigenetic code for integrating signal-dependent programs of transcriptional response,” Genes and Development, vol. 20, no. 11, pp. 1405–1428, 2006. View at Publisher · View at Google Scholar · View at Scopus
  95. P. Karagianni and J. Wong, “HDAC3: taking the SMRT-N-CoRrect road to repression,” Oncogene, vol. 26, no. 37, pp. 5439–5449, 2007. View at Publisher · View at Google Scholar · View at Scopus
  96. J. Li, J. Wang, J. Wang et al., “Both corepressor proteins SMRT and N-CoR exist in large protein complexes containing HDAC3,” EMBO Journal, vol. 19, no. 16, pp. 4342–4350, 2000. View at Google Scholar · View at Scopus
  97. V. Perissi and M. G. Rosenfeld, “Controlling nuclear receptors: the circular logic of cofactor cycles,” Nature Reviews Molecular Cell Biology, vol. 6, no. 7, pp. 542–554, 2005. View at Publisher · View at Google Scholar · View at Scopus
  98. A. Aranda and A. Pascual, “Nuclear hormone receptors and gene expression,” Physiological Reviews, vol. 81, no. 3, pp. 1269–1304, 2001. View at Google Scholar · View at Scopus
  99. K. Yoshida, W. Nishida, K. Hayashi et al., “Vascular remodeling induced by naturally occurring unsaturated lysophosphatidic acid in vivo,” Circulation, vol. 108, no. 14, pp. 1746–1752, 2003. View at Publisher · View at Google Scholar · View at Scopus
  100. T. Tsukahara, S. Hanazawa, T. Kobayashi, Y. Iwamoto, and K. Murakami-Murofushi, “Cyclic phosphatidic acid decreases proliferation and survival of colon cancer cells by inhibiting peroxisome proliferator-activated receptor γ,” Prostaglandins and Other Lipid Mediators, vol. 93, no. 3-4, pp. 126–133, 2010. View at Publisher · View at Google Scholar · View at Scopus
  101. T. Tsukahara, S. Hanazawa, and K. Murakami-Murofushi, “Cyclic phosphatidic acid influences the expression and regulation of cyclic nucleotide phosphodiesterase 3B and lipolysis in 3T3-L1 cells,” Biochemical and Biophysical Research Communications, vol. 404, no. 1, pp. 109–114, 2011. View at Publisher · View at Google Scholar · View at Scopus