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PPAR Research
Volume 2010, Article ID 341671, 6 pages
http://dx.doi.org/10.1155/2010/341671
Review Article

PPAR- Signaling Crosstalk in Mesenchymal Stem Cells

1Department of Microbiology and Immunology, School of Medicine, Keio University, 35 Shinano-machi, Shinjuku-ku, Tokyo, 160-8582, Japan
2College of Science & General Studies, Alfaisal University, P.O. Box 50927, Riyadh 11533, Saudi Arabia
3Institute of Molecular and Cellular Biosciences, University of Tokyo, Yayoi 1-1-1, Bunkyo-ku, Tokyo 113-0032, Japan

Received 30 April 2010; Accepted 25 June 2010

Academic Editor: Yaacov Barak

Copyright © 2010 Ichiro Takada 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. L. Michalik, J. Auwerx, J. P. Berger et al., “International union of pharmacology. LXI. Peroxisome proliferator-activated receptors,” Pharmacological Reviews, vol. 58, no. 4, pp. 726–741, 2006. View at Publisher · View at Google Scholar · View at Scopus
  2. 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
  3. 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
  4. T. Kouzarides, “Chromatin modifications and their function,” Cell, vol. 128, no. 4, pp. 693–705, 2007. View at Publisher · View at Google Scholar · View at Scopus
  5. C. D. Allis, S. L. Berger, J. Cote et al., “New nomenclature for chromatin-modifying enzymes,” Cell, vol. 131, no. 4, pp. 633–636, 2007. View at Publisher · View at Google Scholar · View at Scopus
  6. R. Fujiki, T. Chikanishi, W. Hashiba et al., “GlcNAcylation of a histone methyltransferase in retinoic-acid-induced granulopoiesis,” Nature, vol. 459, no. 7245, pp. 455–459, 2009. View at Publisher · View at Google Scholar · View at Scopus
  7. N. Huang, E. vom Baur, J.-M. Garnier et al., “Two distinct nuclear receptor interaction domains in NSD1, a novel SET protein that exhibits characteristics of both corepressors and coactivators,” EMBO Journal, vol. 17, no. 12, pp. 3398–3412, 1998. View at Publisher · View at Google Scholar · View at Scopus
  8. I. Garcia-Bassets, Y.-S. Kwon, F. Telese et al., “Histone methylation-dependent mechanisms impose ligand dependency for gene activation by nuclear receptors,” Cell, vol. 128, no. 3, pp. 505–518, 2007. View at Publisher · View at Google Scholar · View at Scopus
  9. H. Kitagawa, R. Fujiki, K. Yoshimura et al., “The chromatin-remodeling complex WINAC targets a nuclear receptor to promoters and is impaired in Williams syndrome,” Cell, vol. 113, no. 7, pp. 905–917, 2003. View at Publisher · View at Google Scholar · View at Scopus
  10. B. Lemon, C. Inouye, D. S. King, and R. Tjian, “Selectivity of chromatin-remodelling cofactors for ligand-activated transcription,” Nature, vol. 414, no. 6866, pp. 924–928, 2001. View at Publisher · View at Google Scholar · View at Scopus
  11. Y. Bao and X. Shen, “SnapShot: chromatin remodeling complexes,” Cell, vol. 129, no. 3, p. 632, 2007. View at Publisher · View at Google Scholar · View at Scopus
  12. M. Kishimoto, R. Fujiki, S. Takezawa et al., “Nuclear receptor mediated gene regulation through chromatin remodeling and histone modifications,” Endocrine Journal, vol. 53, no. 2, pp. 157–172, 2006. View at Publisher · View at Google Scholar · View at Scopus
  13. S. Kato, H. Endoh, Y. Masuhiro et al., “Activation of the estrogen receptor through phosphorylation by mitogen-activated protein kinase,” Science, vol. 270, no. 5241, pp. 1491–1494, 1995. View at Google Scholar · View at Scopus
  14. M. Suzawa, I. Takada, J. Yanagisawa et al., “Cytokines suppress adipogenesis and PPAR-γ function through the TAK1/TAB1/NIK cascade,” Nature Cell Biology, vol. 5, no. 3, pp. 224–230, 2003. View at Publisher · View at Google Scholar · View at Scopus
  15. E. Hu, J. B. Kim, P. Sarraf, and B. M. Spiegelman, “Inhibition of adipogenesis through MAP kinase-mediated phosphorylation of PPARγ,” Science, vol. 274, no. 5295, pp. 2100–2103, 1996. View at Publisher · View at Google Scholar · View at Scopus
  16. G. Pascual, A. L. Fong, S. Ogawa et al., “A SUMOylation-dependent pathway mediates transrepression of inflammatory response genes by PPAR-γ,” Nature, vol. 437, no. 7059, pp. 759–763, 2005. View at Publisher · View at Google Scholar · View at Scopus
  17. D. Shao, S. M. Rangwala, S. T. Bailey, S. L. Krakow, M. J. Reginato, and M. A. Lazar, “Interdomain communication regulating ligand binding by PPAR-γ,” Nature, vol. 396, no. 6709, pp. 377–380, 1998. View at Publisher · View at Google Scholar · View at Scopus
  18. O. van Beekum, V. Fleskens, and E. Kalkhoven, “Posttranslational modifications of PPAR-γ: fine-tuning the metabolic master regulator,” Obesity, vol. 17, no. 2, pp. 213–219, 2009. View at Publisher · View at Google Scholar · View at Scopus
  19. I. Takada, A. P. Kouzmenko, and S. Kato, “Wnt and PPARgamma signaling in osteoblastogenesis and adipogenesis,” Nature Reviews. Rheumatology, vol. 5, no. 8, pp. 442–447, 2009. View at Google Scholar · View at Scopus
  20. A. Arthur, A. Zannettino, and S. Gronthos, “The therapeutic applications of multipotential mesenchymal/stromal stem cells in skeletal tissue repair,” Journal of Cellular Physiology, vol. 218, no. 2, pp. 237–245, 2009. View at Publisher · View at Google Scholar · View at Scopus
  21. H. Hamada, M. Kobune, K. Nakamura et al., “Mesenchymal stem cells (MSC) as therapeutic cytoreagents for gene therapy,” Cancer Science, vol. 96, no. 3, pp. 149–156, 2005. View at Publisher · View at Google Scholar · View at Scopus
  22. S. Muruganandan, A. A. Roman, and C. J. Sinal, “Adipocyte differentiation of bone marrow-derived mesenchymal stem cells: cross talk with the osteoblastogenic program,” Cellular and Molecular Life Sciences, vol. 66, no. 2, pp. 236–253, 2009. View at Publisher · View at Google Scholar · View at Scopus
  23. J.-H. Hong, E. S. Hwang, M. T. McManus et al., “TAZ, a transcriptional modulator of mesenchymal stem cell differentiation,” Science, vol. 309, no. 5737, pp. 1074–1078, 2005. View at Publisher · View at Google Scholar · View at Scopus
  24. S. Spinella-Jaegle, G. Rawadi, S. Kawai et al., “Sonic hedgehog increases the commitment of pluripotent mesenchymal cells into the osteoblastic lineage and abolishes adipocytic differentiation,” Journal of Cell Science, vol. 114, no. 11, pp. 2085–2094, 2001. View at Google Scholar · View at Scopus
  25. C. A. Baumann, V. Ribon, M. Kanzaki et al., “CAP defines a second signalling pathway required for insulin-stimulated glucose transport,” Nature, vol. 407, no. 6801, pp. 202–207, 2000. View at Publisher · View at Google Scholar · View at Scopus
  26. V. Ribon, J. H. Johnson, H. S. Camp, and A. R. Saltiel, “Thiazolidinediones and insulin resistance: peroxisome proliferator-activated receptor γ activation stimulates expression of the CAP gene,” Proceedings of the National Academy of Sciences of the United States of America, vol. 95, no. 25, pp. 14751–14756, 1998. View at Google Scholar · View at Scopus
  27. M. Ricote, A. C. Li, T. M. Willson, C. J. Kelly, and C. K. Glass, “The peroxisome proliferator-activated receptor-γ is a negative regulator of macrophage activation,” Nature, vol. 391, no. 6662, pp. 79–82, 1998. View at Publisher · View at Google Scholar · View at Scopus
  28. I. Takada, M. Mihara, M. Suzawa et al., “A histone lysine methyltransferase activated by non-canonical Wnt signalling suppresses PPAR-γ transactivation,” Nature Cell Biology, vol. 9, no. 11, pp. 1273–1285, 2007. View at Publisher · View at Google Scholar · View at Scopus
  29. M. Kortenjann, M. Nehls, A. J. H. Smith et al., “Abnormal bone marrow stroma in mice deficient for nemo-like kinase, Nlk,” European Journal of Immunology, vol. 31, no. 12, pp. 3580–3587, 2001. View at Publisher · View at Google Scholar · View at Scopus
  30. J. Yanagisawa, H. Kitagawa, M. Yanagida et al., “Nuclear receptor function requires a TFTC-type histone acetyl transferase complex,” Molecular Cell, vol. 9, no. 3, pp. 553–562, 2002. View at Publisher · View at Google Scholar · View at Scopus
  31. L. E. L. M. Vissers, C. M. A. van Ravenswaaij, R. Admiraal et al., “Mutations in a new member of the chromodomain gene family cause CHARGE syndrome,” Nature Genetics, vol. 36, no. 9, pp. 955–957, 2004. View at Publisher · View at Google Scholar · View at Scopus
  32. H. Wang, W. An, R. Cao et al., “mAM facilitates conversion by ESET of dimethyl to trimethyl lysine 9 of histone H3 to cause transcriptional repression,” Molecular Cell, vol. 12, no. 2, pp. 475–487, 2003. View at Publisher · View at Google Scholar · View at Scopus
  33. D. C. Schultz, K. Ayyanathan, D. Negorev, G. G. Maul, and F. J. Rauscher III, “SETDB1: a novel KAP-1-associated histone H3, lysine 9-specific methyltransferase that contributes to HP1-mediated silencing of euchromatic genes by KRAB zinc-finger proteins,” Genes and Development, vol. 16, no. 8, pp. 919–932, 2002. View at Publisher · View at Google Scholar · View at Scopus
  34. 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 Google Scholar · View at Scopus
  35. T. Kurahashi, T. Nomura, C. Kanei-Ishii, Y. Shinkai, and S. Ishii, “The Wnt-NLK signaling pathway inhibits A-Myb activity by inhibiting the association with coactivator CBP and methylating histone H3,” Molecular Biology of the Cell, vol. 16, no. 10, pp. 4705–4713, 2005. View at Publisher · View at Google Scholar · View at Scopus
  36. D. A. Glass II, P. Bialek, J. D. Ahn et al., “Canonical Wnt signaling in differentiated osteoblasts controls osteoclast differentiation,” Developmental Cell, vol. 8, no. 5, pp. 751–764, 2005. View at Publisher · View at Google Scholar · View at Scopus
  37. Y. Gong, R. B. Slee, N. Fukai et al., “LDL receptor-related protein 5 (LRP5) affects bone accrual and eye development,” Cell, vol. 107, no. 4, pp. 513–523, 2001. View at Publisher · View at Google Scholar · View at Scopus
  38. S. E. Ross, N. Hemati, K. A. Longo et al., “Inhibition of adipogenesis by Wnt signaling,” Science, vol. 289, no. 5481, pp. 950–953, 2000. View at Publisher · View at Google Scholar · View at Scopus
  39. I. Takada, A. P. Kouzmenko, and S. Kato, “Molecular switching of osteoblastogenesis versus adipogenesis: implications for targeted therapies,” Expert Opinion on Therapeutic Targets, vol. 13, no. 5, pp. 593–603, 2009. View at Publisher · View at Google Scholar · View at Scopus
  40. Y. Wan, L.-W. Chong, and R. M. Evans, “PPAR-γ regulates osteoclastogenesis in mice,” Nature Medicine, vol. 13, no. 12, pp. 1496–1503, 2007. View at Publisher · View at Google Scholar · View at Scopus
  41. Y. Guan, C. Hao, D. R. Cha et al., “Thiazolidinediones expand body fluid volume through PPARγ stimulation of ENaC-mediated renal salt absorption,” Nature Medicine, vol. 11, no. 8, pp. 861–866, 2005. View at Publisher · View at Google Scholar · View at Scopus