Journal Menu
- About this Journal
- Abstracting and Indexing
- Aims and Scope
- Article Processing Charges
- Articles in Press
- Author Guidelines
- Bibliographic Information
- Citations to this Journal
- Contact Information
- Editorial Board
- Editorial Workflow
- Free eTOC Alerts
- Publication Ethics
- Reviewers Acknowledgment
- Submit a Manuscript
- Subscription Information
- Table of Contents
PPAR Research
Volume 2012 (2012), Article ID 641087, 15 pages
doi:10.1155/2012/641087
Review Article
PPAR and Oxidative Stress: Con() Catenating NRF2 and FOXO
Gastroenterology Unit, Department of Clinical Pathophysiology, University of Florence, Viale Pieraccini 6, 50139 Firenze, Italy
Received 1 September 2011; Revised 5 November 2011; Accepted 17 November 2011
Academic Editor: Paul Drew
Copyright © 2012 Simone Polvani 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
- G. Perry, A. Nunomura, K. Hirai, A. Takeda, G. Aliev, and M. A. Smith, “Oxidative damage in Alzheimer's disease: the metabolic dimension,” International Journal of Developmental Neuroscience, vol. 18, no. 4-5, pp. 417–421, 2000. View at Publisher · View at Google Scholar · View at Scopus
- V. Adam-Vizi and C. Chinopoulos, “Bioenergetics and the formation of mitochondrial reactive oxygen species,” Trends in Pharmacological Sciences, vol. 27, no. 12, pp. 639–645, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- J. T. Hancock, R. Desikan, and S. J. Neill, “Role of reactive oxygen species in cell signalling pathways,” Biochemical Society Transactions, vol. 29, no. 2, pp. 345–350, 2001. View at Publisher · View at Google Scholar · View at Scopus
- T. Jabs, “Reactive oxygen intermediates as mediators of programmed cell death in plants and animals,” Biochemical Pharmacology, vol. 57, no. 3, pp. 231–245, 1999. View at Publisher · View at Google Scholar · View at Scopus
- H. Jaeschke, “Reactive oxygen and mechanisms of inflammatory liver injury: present concepts,” Journal of Gastroenterology and Hepatology, vol. 26, supplement 1, pp. 173–179, 2011. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- S. Reuter, S. C. Gupta, M. M. Chaturvedi, and B. B. Aggarwal, “Oxidative stress, inflammation, and cancer: how are they linked?” Free Radical Biology and Medicine, vol. 49, no. 11, pp. 1603–1616, 2010. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- M. J. Morgan and Z. Liu, “Crosstalk of reactive oxygen species and NF-κB signaling,” Cell Research, vol. 21, no. 1, pp. 103–115, 2011. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- N. Ghosh, R. Chaki, V. Mandal, and S. C. Mandal, “Cox-2 as a target for cancer chemotherapy,” Pharmacological Reports, vol. 62, no. 2, pp. 233–244, 2010. View at Scopus
- A. Pautz, J. Art, S. Hahn, S. Nowag, C. Voss, and H. Kleinert, “Regulation of the expression of inducible nitric oxide synthase,” Nitric Oxide, vol. 23, no. 2, pp. 75–93, 2010. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- A. Galli, T. Mello, and S. Polvani, “Peroxisome proliferator-activated receptor and retinoic X receptor in alcoholic liver disease,” PPAR Research, vol. 2009, Article ID 748174, 11 pages, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- B. A. Neuschwander-Tetri, “Hepatic lipotoxicity and the pathogenesis of nonalcoholic steatohepatitis: the central role of nontriglyceride fatty acid metabolites,” Hepatology, vol. 52, no. 2, pp. 774–788, 2010. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- D. Zhu, J. Shi, S. Liu, Y. Liu, and D. Zheng, “HIV infection enhances TRAIL-induced cell death in macrophage by down-regulating decoy receptor expression and generation of reactive oxygen species,” Plos One, vol. 6, no. 4, Article ID e18291, 2011. View at Publisher · View at Google Scholar · View at PubMed
- W. Lin, G. Wu, S. Li, et al., “Hiv and hcv cooperatively promote hepatic fibrogenesis via induction of reactive oxygen species and nfkappab,” The Journal of Biological Chemistry, vol. 286, no. 4, pp. 2665–2674, 2011.
- L. Hu, L. Chen, G. Yang, et al., “Hbx sensitizes cells to oxidative stress-induced apoptosis by accelerating the loss of mcl-1 protein via caspase-3 cascade,” Molecular Cancer, vol. 10, p. 43, 2011.
- B. Desvergne and W. Wahli, “Peroxisome proliferator-activated receptors: nuclear control of metabolism,” Endocrine Reviews, vol. 20, no. 5, pp. 649–688, 1999. View at Scopus
- T. Varga, Z. Czimmerer, and L. Nagy, “PPARs are a unique set of fatty acid regulated transcription factors controlling both lipid metabolism and inflammation,” Biochimica et Biophysica Acta, vol. 1812, no. 8, pp. 1007–1022, 2011. View at Publisher · View at Google Scholar · View at PubMed
- B. R. Kwak, F. Mulhaupt, and F. Mach, “The role of PPARγ ligands as regulators of the immune response,” Drug News and Perspectives, vol. 15, no. 6, pp. 325–332, 2002. View at Publisher · View at Google Scholar · View at Scopus
- J. Auwerx, E. Baulieu, M. Beato et al., “A unified nomenclature system for the nuclear receptor superfamily,” Cell, vol. 97, no. 2, pp. 161–163, 1999. View at Scopus
- D. L. Bain, A. F. Heneghan, K. D. Connaghan-Jones, and M. T. Miura, “Nuclear receptor structure: implications for function,” Annual Review of Physiology, vol. 69, pp. 201–220, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- A. Galli, M. Stewart, R. Dorris, and D. Crabb, “High-level expression of RXRα and the presence of endogenous ligands contribute to expression of a peroxisome proliferator-activated receptor- responsive gene in hepatoma cells,” Archives of Biochemistry and Biophysics, vol. 354, no. 2, pp. 288–294, 1998. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- K. A. Burns and J. P. Vanden Heuvel, “Modulation of PPAR activity via phosphorylation,” Biochimica et Biophysica Acta, vol. 1771, no. 8, pp. 952–960, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- T. E. Akiyama, C. T. Baumann, S. Sakai, G. L. Hager, and F. J. Gonzalez, “Selective intranuclear redistribution of PPAR isoforms by RXRα,” Molecular Endocrinology, vol. 16, no. 4, pp. 707–721, 2002. View at Publisher · View at Google Scholar · View at Scopus
- E. Ceni, D. W. Crabb, M. Foschi et al., “Acetaldehyde inhibits PPARγ via H2O2-mediated c-Abl activation in human hepatic stellate cells,” Gastroenterology, vol. 131, no. 4, pp. 1235–1252, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- A. von Knethen, M. Soller, N. Tzieply et al., “PPARγ1 attenuates cytosol to membrane translocation of PKCα to desensitize monocytes/macrophages,” The Journal of Cell Biology, vol. 176, no. 5, pp. 681–694, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- A. von Knethen, N. Tzieply, C. Jennewein, and B. Brüne, “Casein-kinase-II-dependent phosphorylation of PPARγ provokes CRM1-mediated shuttling of PPARγ from the nucleus to the cytosol,” Journal of Cell Science, vol. 123, no. 2, pp. 192–201, 2010. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- Z. E. Floyd and J. M. Stephens, “Interferon-γ-mediated activation and ubiquitin-proteasome-dependent degradation of PPARγ in adipocytes,” Journal of Biological Chemistry, vol. 277, no. 6, pp. 4062–4068, 2002. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- P. Tontonoz and B. M. Spiegelman, “Fat and beyond: the diverse biology of PPARγ,” Annual Review of Biochemistry, vol. 77, pp. 289–312, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- M. Li, G. Pascual, and C. K. Glass, “Peroxisome proliferator-activated receptor γ-dependent repression of the inducible nitric oxide synthase gene,” Molecular and Cellular Biology, vol. 20, no. 13, pp. 4699–4707, 2000. View at Publisher · View at Google Scholar · View at Scopus
- B. Vandewalle, E. Moerman, B. Lefebvre et al., “PPARγ-dependent and -independent effects of Rosiglitazone on lipotoxic human pancreatic islets,” Biochemical and Biophysical Research Communications, vol. 366, no. 4, pp. 1096–1101, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- S. W. Chung, B. Y. Kang, S. H. Kim et al., “Oxidized low density lipoprotein inhibits interleukin-12 production in lipopolysaccharide-activated mouse macrophages via direct interactions between peroxisome proliferator-activated receptor-γ and nuclear factor-κB,” The Journal of Biological Chemistry, vol. 275, no. 42, pp. 32681–32687, 2000. View at Scopus
- S. T. Bailey and S. Ghosh, “‘PPAR’ting ways with inflammation,” Nature Immunology, vol. 6, no. 10, pp. 966–967, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- 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 Scopus
- J. M. Kleinhenz, D. J. Kleinhenz, S. You et al., “Disruption of endothelial peroxisome proliferator-activated receptor-γ reduces vascular nitric oxide production,” American Journal of Physiology, vol. 297, no. 5, pp. H1647–H1654, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- Z. Yousefipour, A. Oyekan, and M. Newaz, “Interaction of oxidative stress, nitric oxide and peroxisome proliferator activated receptor γ in acute renal failure,” Pharmacology and Therapeutics, vol. 125, no. 3, pp. 436–445, 2010. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- S. H. H. Chan, K. L. H. Wu, P. S. S. Kung, and J. Y. H. Chan, “Oral intake of rosiglitazone promotes a central antihypertensive effect via upregulation of peroxisome proliferator-activated receptor-γ and alleviation of oxidative stress in rostral ventrolateral medulla of spontaneously hypertensive rats,” Hypertension, vol. 55, no. 6, pp. 1444–1453, 2010. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- L. H. Randy and B. Guoying, “Agonism of peroxisome proliferator receptor-gamma may have therapeutic potential for neuroinflammation and Parkinson's disease,” Current Neuropharmacology, vol. 5, no. 1, pp. 35–46, 2007. View at Publisher · View at Google Scholar · View at Scopus
- Y. Lee, S. B. Han, S. Nam, K. Oh, and J. T. Hong, “Inflammation and Alzheimer's disease,” Archives of Pharmacal Research, vol. 33, no. 10, pp. 1539–1556, 2010. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- A. A. Gupte, J. Z. Liu, Y. Ren et al., “Rosiglitazone attenuates age- and diet-associated nonalcoholic steatohepatitis in male low-density lipoprotein receptor knockout mice,” Hepatology, vol. 52, no. 6, pp. 2001–2011, 2010. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- R. A. Quintanilla, Y. N. Jin, K. Fuenzalida, M. Bronfman, and G. V. W. Johnson, “Rosiglitazone treatment prevents mitochondrial dysfunction in mutant huntingtin-expressing cells: possible role of peroxisome proliferator-activated receptor-γ (PPARγ) in the pathogenesis of huntington disease,” Journal of Biological Chemistry, vol. 283, no. 37, pp. 25628–25637, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- A. Galli, E. Ceni, T. Mello et al., “Thiazolidinediones inhibit hepatocarcinogenesis in hepatitis B virus-transgenic mice by peroxisome proliferator-activated receptor γ-independent regulation of nucleophosmin,” Hepatology, vol. 52, no. 2, pp. 493–505, 2010. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- X. Wang, Z. Wang, J. Z. Liu et al., “Double antioxidant activities of rosiglitazone against high glucose-induced oxidative stress in hepatocyte,” Toxicology in Vitro, vol. 25, no. 4, pp. 839–847, 2011. View at Publisher · View at Google Scholar · View at PubMed
- H. E. Ferguson, T. H. Thatcher, K. C. Olsen et al., “Peroxisome proliferator-activated receptor-γ ligands induce heme oxygenase-1 in lung fibroblasts by a PPARγ-independent, glutathione-dependent mechanism,” American Journal of Physiology, vol. 297, no. 5, pp. L912–L919, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- R. Kapadia, J. Yi, and R. Vemuganti, “Mechanisms of anti-inflammatory and neuroprotective actions of PPAR-gamma agonists,” Frontiers in Bioscience, vol. 13, no. 5, pp. 1813–1826, 2008. View at Publisher · View at Google Scholar · View at Scopus
- A. Galli, E. Ceni, D. W. Crabb et al., “Antidiabetic thiazolidinediones inhibit invasiveness of pancreatic cancer cells via PPARγ independent mechanisms,” Gut, vol. 53, no. 11, pp. 1688–1697, 2004. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- Y. Okuno, M. Matsuda, Y. Miyata et al., “Human catalase gene is regulated by peroxisome proliferator activated receptor-gamma through a response element distinct from that of mouse,” Endocrine Journal, vol. 57, no. 4, pp. 303–309, 2010. View at Publisher · View at Google Scholar · View at Scopus
- G. D. Girnun, F. E. Domann, S. A. Moore, and M. E. C. Robbins, “Identification of a functional peroxisome proliferator-activated receptor response element in the rat catalase promoter,” Molecular Endocrinology, vol. 16, no. 12, pp. 2793–2801, 2002. View at Publisher · View at Google Scholar · View at Scopus
- Y. Ren, C. Sun, Y. Sun et al., “PPAR gamma protects cardiomyocytes against oxidative stress and apoptosis via Bcl-2 upregulation,” Vascular Pharmacology, vol. 51, no. 2-3, pp. 169–174, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- C. Blanquicett, B. Y. Kang, J. D. Ritzenthaler, D. P. Jones, and C. M. Hart, “Oxidative stress modulates PPARγ in vascular endothelial cells,” Free Radical Biology and Medicine, vol. 48, no. 12, pp. 1618–1625, 2010. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- K. Fuenzalida, R. Quintanilla, P. Ramos et al., “Peroxisome proliferator-activated receptor γ up-regulates the Bcl-2 anti-apoptotic protein in neurons and induces mitochondrial stabilization and protection against oxidative stress and apoptosis,” The Journal of Biological Chemistry, vol. 282, no. 51, pp. 37006–37015, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- X. Yu, X. Shao, H. Sun et al., “Activation of cerebral peroxisome proliferator-activated receptors gamma exerts neuroprotection by inhibiting oxidative stress following pilocarpine-induced status epilepticus,” Brain Research, vol. 1200, pp. 146–158, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- G. Ding, M. Fu, Q. Qin et al., “Cardiac peroxisome proliferator-activated receptor γ is essential in protecting cardiomyocytes from oxidative damage,” Cardiovascular Research, vol. 76, no. 2, pp. 269–279, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- S. S. Chung, M. Kim, B. Youn et al., “Glutathione peroxidase 3 mediates the antioxidant effect of peroxisome proliferator-activated receptor γ in human skeletal muscle cells,” Molecular and Cellular Biology, vol. 29, no. 1, pp. 20–30, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- 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
- T. Ishii, K. Itoh, E. Ruiz et al., “Role of Nrf2 in the regulation of CD36 and stress protein expression in murine macrophages: activation by oxidatively modified LDL and 4-hydroxynonenal,” Circulation Research, vol. 94, no. 5, pp. 609–616, 2004. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- G. Krönke, A. Kadl, E. Ikonomu et al., “Expression of heme oxygenase-1 in human vascular cells is regulated by peroxisome proliferator-activated receptors,” Arteriosclerosis, Thrombosis, and Vascular Biology, vol. 27, no. 6, pp. 1276–1282, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- A. A. Herzlich, X. Ding, D. Shen, et al., “Peroxisome proliferator-activated receptor expression in murine models and humans with age-related macular degeneration,” The Open Biology Journal, vol. 2, pp. 141–148, 2009.
- Y. Zhao, A. Patzer, T. Herdegen, P. Gohlke, and J. Culman, “Activation of cerebral peroxisome proliferator-activated receptors gamma promotes neuroprotection by attenuation of neuronal cyclooxygenase-2 overexpression after focal cerebral ischemia in rats,” The FASEB Journal, vol. 20, no. 8, pp. 1162–1175, 2006. View at Publisher · View at Google Scholar · View at PubMed
- M. Collino, M. Aragno, R. Mastrocola et al., “Modulation of the oxidative stress and inflammatory response by PPAR-γ agonists in the hippocampus of rats exposed to cerebral ischemia/reperfusion,” European Journal of Pharmacology, vol. 530, no. 1-2, pp. 70–80, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- 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 PubMed · View at Scopus
- E. Paradis, S. Clavel, F. Bouillaud, D. Ricquier, and D. Richard, “Uncoupling protein 2: a novel player in neuroprotection,” Trends in Molecular Medicine, vol. 9, no. 12, pp. 522–525, 2003. View at Publisher · View at Google Scholar · View at Scopus
- M. Febbraio, D. P. Hajjar, and R. L. Silverstein, “CD36: a class B scavenger receptor involved in angiogenesis, atherosclerosis, inflammation, and lipid metabolism,” Journal of Clinical Investigation, vol. 108, no. 6, pp. 785–791, 2001. View at Publisher · View at Google Scholar · View at Scopus
- F. Zhang, F. Liu, M. Yan et al., “Peroxisome proliferator-activated receptor-γ agonists suppress iNOS expression induced by LPS in rat primary Schwann cells,” Journal of Neuroimmunology, vol. 218, no. 1-2, pp. 36–47, 2010. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- S. Aleshin, S. Grabeklis, T. Hanck, M. Sergeeva, and G. Reiser, “Peroxisome proliferator-activated receptor (PPAR)-γ positively controls and PPARα negatively controls cyclooxygenase-2 expression in rat brain astrocytes through a convergence on PPARβ/δ via mutual control of PPAR expression levels,” Molecular Pharmacology, vol. 76, no. 2, pp. 414–424, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- H. Was, J. Dulak, and A. Jozkowicz, “Heme oxygenase-1 in tumor biology and therapy,” Current Drug Targets, vol. 11, no. 12, pp. 1551–1570, 2010.
- P. Gong, D. Stewart, B. Hu et al., “Activation of the mouse heme oxygenase-1 gene by 15-deoxy-Δ12, 14-prostaglandin J2 is mediated by the stress response elements and transcription factor Nrf2,” Antioxidants and Redox Signaling, vol. 4, no. 2, pp. 249–257, 2002. View at Scopus
- J. Liu, Q. Xia, Q. Zhang et al., “Peroxisome proliferator-activated receptor-γ ligands 15-deoxy-δ12,14-prostaglandin J2 and pioglitazone inhibit hydroxyl peroxide-induced TNF-α and lipopolysaccharide-induced CXC chemokine expression in neonatal rat cardiac myocytes,” Shock, vol. 32, no. 3, pp. 317–324, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- J. Ye, “Regulation of PPARγ function by TNF-α,” Biochemical and Biophysical Research Communications, vol. 374, no. 3, pp. 405–408, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- M. Napolitano, L. Costa, R. Palermo, A. Giovenco, A. Vacca, and A. Gulino, “Protective effect of pioglitazone, a PPARγ ligand, in a 3 nitropropionic acid model of Huntington's disease,” Brain Research Bulletin, vol. 85, no. 3-4, pp. 231–237, 2011. View at Publisher · View at Google Scholar · View at PubMed
- M. K. Ahsan, H. Okuyama, Y. Hoshino et al., “Thioredoxin-binding protein-2 deficiency enhances methionine-choline deficient diet-induced hepatic steatosis but inhibits steatohepatitis in mice,” Antioxidants & Redox Signaling, vol. 11, no. 10, pp. 2573–2584, 2009.
- W. O. Osburn and T. W. Kensler, “Nrf2 signaling: an adaptive response pathway for protection against environmental toxic insults,” Mutation Research, vol. 659, no. 1-2, pp. 31–39, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- K. Itoh, N. Wakabayashi, Y. Katoh et al., “Keap1 represses nuclear activation of antioxidant responsive elements by Nrf2 through binding to the amino-terminal Neh2 domain,” Genes and Development, vol. 13, no. 1, pp. 76–86, 1999. View at Scopus
- D. Lee, H. Kuo, M. Liu et al., “KEAP1 E3 ligase-mediated downregulation of NF-κB signaling by targeting IKKβ,” Molecular Cell, vol. 36, no. 1, pp. 131–140, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- A. R. Collins, C. J. Lyon, X. Xia et al., “Age-accelerated atherosclerosis correlates with failure to upregulate antioxidant genes,” Circulation Research, vol. 104, no. 6, pp. e42–e54, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- M. D'Archivio, B. Scazzocchio, C. Filesi et al., “Oxidised LDL up-regulate CD36 expression by the Nrf2 pathway in 3T3-L1 preadipocytes,” FEBS Letters, vol. 582, no. 15, pp. 2291–2298, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- K. Nakaso, H. Yano, Y. Fukuhara, T. Takeshima, K. Wada-Isoe, and K. Nakashima, “PI3K is a key molecule in the Nrf2-mediated regulation of antioxidative proteins by hemin in human neuroblastoma cells,” FEBS Letters, vol. 546, no. 2-3, pp. 181–184, 2003. View at Publisher · View at Google Scholar · View at Scopus
- J. Lee, M. J. Calkins, K. Chan, Y. W. Kan, and J. A. Johnson, “Identification of the NF-E2-related factor-2-dependent genes conferring protection against oxidative stress in primary cortical astrocytes using oligonucleotide microarray analysis,” The Journal of Biological Chemistry, vol. 278, no. 14, pp. 12029–12038, 2003. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- E. Y. Park, I. J. Cho, and S. G. Kim, “Transactivation of the PPAR-responsive enhancer module in chemopreventive glutathione S-transferase gene by the peroxisome proliferator-activated receptor-γ and retinoid X receptor heterodimer,” Cancer Research, vol. 64, no. 10, pp. 3701–3713, 2004. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- M. Kwak, K. Itoh, M. Yamamoto, and T. W. Kensler, “Enhanced expression of the transcription factor Nrf2 by cancer chemopreventive agents: role of antioxidant response element-like sequences in the nrf2 promoter,” Molecular and Cellular Biology, vol. 22, no. 9, pp. 2883–2892, 2002. View at Publisher · View at Google Scholar · View at Scopus
- H. Cho, S. P. Reddy, A. DeBiase, M. Yamamoto, and S. R. Kleeberger, “Gene expression profiling of NRF2-mediated protection against oxidative injury,” Free Radical Biology and Medicine, vol. 38, no. 3, pp. 325–343, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- H. Cho, W. Gladwell, X. Wang et al., “Nrf2-regulated PPARγ expression is critical to protection against acute lung injury in mice,” American Journal of Respiratory and Critical Care Medicine, vol. 182, no. 2, pp. 170–182, 2010. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- J. Huang, I. Tabbi-Anneni, V. Gunda, and L. Wang, “Transcription factor Nrf2 regulates SHP and lipogenic gene expression in hepatic lipid metabolism,” American Journal of Physiology, vol. 299, no. 6, pp. G1211–G1221, 2010. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- L. A. Faine, M. Rudnicki, F. A. César et al., “Anti-inflammatory and antioxidant properties of a new arylidene- thiazolidinedione in macrophages,” Current Medicinal Chemistry, vol. 18, no. 22, pp. 3351–3360, 2011. View at Publisher · View at Google Scholar
- R. K. Thimmulappa, H. Lee, T. Rangasamy et al., “Nrf2 is a critical regulator of the innate immune response and survival during experimental sepsis,” The Journal of Clinical Investigation, vol. 116, no. 4, pp. 984–995, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- S. Chowdhry, M. H. Nazmy, P. J. Meakin et al., “Loss of Nrf2 markedly exacerbates nonalcoholic steatohepatitis,” Free Radical Biology and Medicine, vol. 48, no. 2, pp. 357–371, 2010. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- H. Y. Kay, W. D. Kim, S. J. Hwang et al., “Nrf2 inhibits LXRα-dependent hepatic lipogenesis by competing with FXR for acetylase binding,” Antioxidants and Redox Signaling, vol. 15, no. 8, pp. 2135–2146, 2011. View at Publisher · View at Google Scholar · View at PubMed
- B. Rubinfeld, I. Albert, E. Porfiri, C. Fiol, S. Munemitsu, and P. Polakis, “Binding of GSK3β to the APC-β-catenin complex and regulation of complex assembly,” Science, vol. 272, no. 5264, pp. 1023–1026, 1996. View at Scopus
- H. Clevers, “Stem cells, asymmetric division and cancer,” Nature Genetics, vol. 37, no. 10, pp. 1027–1028, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- H. Clevers, “Wnt/β-catenin signaling in development and disease,” Cell, vol. 127, no. 3, pp. 469–480, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- B. T. MacDonald, K. Tamai, and X. He, “Wnt/β-catenin signaling: components, mechanisms, and diseases,” Developmental Cell, vol. 17, no. 1, pp. 9–26, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- M. Okamura, H. Kudo, K. Wakabayashi et al., “COUP-TFII acts downstream of Wnt/β-catenin signal to silence PPARγ gene expression and repress adipogenesis,” Proceedings of the National Academy of Sciences of the United States of America, vol. 106, no. 14, pp. 5819–5824, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- Y. Chen, Y. Hu, T. Zhou et al., “Activation of the wnt pathway plays a pathogenic role in diabetic retinopathy in humans and animal models,” The American Journal of Pathology, vol. 175, no. 6, pp. 2676–2685, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- A. J. Mikels and R. Nusse, “Wnts as ligands: processing, secretion and reception,” Oncogene, vol. 25, no. 57, pp. 7461–7468, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- A. J. Mikels and R. Nusse, “Purified Wnt5a protein activates or inhibits beta-catenin-TCF signaling depending on receptor context,” Plos Biology, vol. 4, no. 4, p. e115, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- K. Inoki, H. Ouyang, T. Zhu et al., “TSC2 integrates wnt and energy signals via a coordinated phosphorylation by AMPK and GSK3 to regulate cell growth,” Cell, vol. 126, no. 5, pp. 955–968, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- P. Ye, Q. Hu, H. Liu, Y. Yan, and A. J. D'Ercole, “β-catenin mediates insulin-like growth factor-I actions to promote cyclin D1 mRNA expression, cell proliferation and survival in oligodendroglial cultures,” GLIA, vol. 58, no. 9, pp. 1031–1041, 2010. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- C. Desbois-Mouthon, A. Cadoret, M. J. Blivet-Van Eggelpoël et al., “Insulin and IGF-1 stimulate the β-catenin pathway through two signalling cascades involving GSK-3β inhibition and Ras activation,” Oncogene, vol. 20, no. 2, pp. 252–259, 2001. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- T. Zhou, K. K. Zhou, K. Lee et al., “The role of lipid peroxidation products and oxidative stress in activation of the canonical wingless-type MMTV integration site (WNT) pathway in a rat model of diabetic retinopathy,” Diabetologia, vol. 54, no. 2, pp. 459–468, 2010. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- J. Chen, O. P. Lazarenko, K. Shankar, M. L. Blackburn, T. M. Badger, and M. J. Ronis, “A role for ethanol-induced oxidative stress in controlling lineage commitment of mesenchymal stromal cells through inhibition of Wnt/β-catenin signaling,” Journal of Bone and Mineral Research, vol. 25, no. 5, pp. 1117–1127, 2010. View at Publisher · View at Google Scholar · View at PubMed
- Y. Funato and H. Miki, “Redox regulation of Wnt signalling via nucleoredoxin,” Free Radical Research, vol. 44, no. 4, pp. 379–388, 2010. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- Y. Funato, T. Terabayashi, R. Sakamoto et al., “Nucleoredoxin sustains Wnt/β-catenin signaling by retaining a pool of inactive dishevelled protein,” Current Biology, vol. 20, no. 21, pp. 1945–1952, 2010. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- F. Al-Mulla, M. S. Bitar, M. Al-Maghrebi et al., “Raf kinase inhibitor protein RKIP enhances signaling by glycogen synthase kinase-3β,” Cancer Research, vol. 71, no. 4, pp. 1334–1343, 2011. View at Publisher · View at Google Scholar · View at PubMed
- C. Lin, J. Wang, J. Ko et al., “Superoxide destabilization of β-catenin augments apoptosis of high-glucose-stressed mesangial cells,” Endocrinology, vol. 149, no. 6, pp. 2934–2942, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- X. Tan, Y. Yuan, G. Zeng et al., “β-catenin deletion in hepatoblasts disrupts hepatic morphogenesis and survival during mouse development,” Hepatology, vol. 47, no. 5, pp. 1667–1679, 2008. View at Publisher · View at Google Scholar · View at PubMed
- X. Zhang, X. Tan, G. Zeng et al., “Conditional β-catenin loss in mice promotes chemical hepatocarcinogenesis: role of oxidative stress and platelet-derived growth factor receptor α/phosphoinositide 3-kinase signaling,” Hepatology, vol. 52, no. 3, pp. 954–965, 2010. View at Publisher · View at Google Scholar · View at PubMed
- S. Giera, A. Braeuning, C. Köhle et al., “Wnt/beta-catenin signaling activates and determines hepatic zonal expression of glutathione S-transferases in mouse liver,” Toxicological Sciences, vol. 115, no. 1, pp. 22–33, 2010. View at Scopus
- X. Tan, J. Behari, B. Cieply, G. K. Michalopoulos, and S. P. S. Monga, “Conditional deletion of β-catenin reveals its role in liver growth and regeneration,” Gastroenterology, vol. 131, no. 5, pp. 1561–1572, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- G. J. P. L. Kops, T. B. Dansen, P. E. Polderman et al., “Forkhead transcription factor FOXO3a protects quiescent cells from oxidative stress,” Nature, vol. 419, no. 6904, pp. 316–321, 2002. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- Y. Zhao, Y. Wang, and W. Zhu, “Applications of post-translational modifications of FoxO family proteins in biological functions,” Journal of Molecular Cell Biology, vol. 3, no. 5, pp. 276–282, 2011. View at Publisher · View at Google Scholar · View at PubMed
- M. A. G. Essers, S. Weijzen, A. M. M. de Vries-Smits et al., “FOXO transcription factor activation by oxidative stress mediated by the small GTPase Ral and JNK,” The EMBO Journal, vol. 23, no. 24, pp. 4802–4812, 2004. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- M. A. G. Essers, L. M. M. de Vries-Smits, N. Barker, P. E. Polderman, B. M. T. Burgering, and H. C. Korswagen, “Functional interaction between β-catenin and FOXO in oxidative stress signaling,” Science, vol. 308, no. 5725, pp. 1181–1184, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- S. Asada, H. Daitoku, H. Matsuzaki et al., “Mitogen-activated protein kinases, Erk and p38, phosphorylate and regulate Foxo1,” Cellular Signalling, vol. 19, no. 3, pp. 519–527, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- M. L. L. Leong, A. C. Maiyar, B. Kim, B. A. O'Keeffe, and G. L. Firestone, “Expression of the serum- and glucocorticoid-inducible protein kinase, Sgk, is a cell survival response to multiple types of environmental stress stimuli in mammary epithelial cells,” The Journal of Biological Chemistry, vol. 278, no. 8, pp. 5871–5882, 2003. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- M. C. Hu, D. Lee, W. Xia et al., “IκB kinase promotes tumorigenesis through inhibition of forkhead FOXO3a,” Cell, vol. 117, no. 2, pp. 225–237, 2004. View at Publisher · View at Google Scholar · View at Scopus
- M. K. Wilson, S. M. McWhirter, R. H. Amin, D. Huang, and M. S. Schlissel, “Abelson virus transformation prevents TRAIL expression by inhibiting FoxO3a and NF-κB,” Molecules and Cells, vol. 29, no. 4, pp. 333–341, 2010. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- M. Almeida, L. Han, M. Martin-Millan, C. A. O'Brien, and S. C. Manolagas, “Oxidative stress antagonizes Wnt signaling in osteoblast precursors by diverting β-catenin from T cell factor- to forkhead box O-mediated transcription,” The Journal of Biological Chemistry, vol. 282, no. 37, pp. 27298–27305, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- D. Hoogeboom, M. A. G. Essers, P. E. Polderman, E. Voets, L. M. M. Smits, and B. M. T. Burgering, “Interaction of FOXO with β-catenin inhibits β-catenin/T cell factor activity,” The Journal of Biological Chemistry, vol. 283, no. 14, pp. 9224–9230, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- 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
- M. Almeida, E. Ambrogini, L. Han, S. C. Manolagas, and R. L. Jilka, “Increased lipid oxidation causes oxidative stress, increased peroxisome proliferator-activated receptor-γ expression, and diminished pro-osteogenic Wnt signaling in the skeleton,” Journal of Biological Chemistry, vol. 284, no. 40, pp. 27438–27448, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- B. Gustafson, B. Eliasson, and U. Smith, “Thiazolidinediones increase the wingless-type MMTV integration site family (WNT) inhibitor Dickkopf-1 in adipocytes: a link with osteogenesis,” Diabetologia, vol. 53, no. 3, pp. 536–540, 2010. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- J. H. Cheng, H. She, Y. Han et al., “Wnt antagonism inhibits hepatic stellate cell activation and liver fibrosis,” American Journal of Physiology, vol. 294, no. 1, pp. G39–G49, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- R. K. Kaundal and S. S. Sharma, “Peroxisome proliferator-activated receptor γ agonists as neuroprotective agents,” Drug News and Perspectives, vol. 23, no. 4, pp. 241–256, 2010. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- D. Lu and D. A. Carson, “Repression of β-catenin signaling by PPARγ ligands,” European Journal of Pharmacology, vol. 636, no. 1–3, pp. 198–202, 2010. View at Publisher · View at Google Scholar · View at PubMed
- T. Fujisawa, A. Nakajima, N. Fujisawa, et al., “Peroxisome proliferator-activated receptor gamma (ppargamma) suppresses colonic epithelial cell turnover and colon carcinogenesis through inhibition of the beta-catenin/t cell factor (tcf) pathway,” Journal of Pharmacological Sciences, vol. 106, no. 4, pp. 627–638, 2008.
- C. Sharma, A. Pradeep, R. G. Pestell, and B. Rana, “Peroxisome proliferator-activated receptor gamma activation modulates cyclin d1 transcription via beta-catenin-independent and camp-response element-binding protein-dependent pathways in mouse hepatocytes,” The Journal of Biological Chemistry, vol. 279, no. 17, pp. 16927–16938, 2004.
- C. Sharma, A. Pradeep, L. Wong, A. Rana, and B. Rana, “Peroxisome proliferator-activated receptor γ activation can regulate β-catenin levels via a proteasome-mediated and adenomatous polyposis coli-independent pathway,” The Journal of Biological Chemistry, vol. 279, no. 34, pp. 35583–35594, 2004. View at Publisher · View at Google Scholar · View at PubMed
- N. Yamakawa-Karakida, K. Sugita, T. Inukai et al., “Ligand activation of peroxisome proliferator-activated receptor γ induces apoptosis of leukemia cells by down-regulating the c-myc gene expression via blockade of the Tcf-4 activity,” Cell Death and Differentiation, vol. 9, no. 5, pp. 513–526, 2002. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- T. Fujisawa, M. Sugiyama, A. Tomimoto, et al., “Inhibition of peroxisome proliferator-activated receptor gamma promotes tumorigenesis through activation of the beta-catenin / t cell factor (tcf) pathway in the mouse intestine,” Journal of Pharmacological Sciences, vol. 108, no. 4, pp. 535–544, 2008.
- J. Liu, H. Wang, Y. Zuo, and S. R. Farmer, “Functional interaction between peroxisome proliferator-activated receptor γ and β-catenin,” Molecular and Cellular Biology, vol. 26, no. 15, pp. 5827–5837, 2006. View at Publisher · View at Google Scholar · View at PubMed
- P. Dowell, T. C. Otto, S. Adi, and M. D. Lane, “Convergence of peroxisome proliferator-activated receptor γ and Foxo1 signaling pathways,” The Journal of Biological Chemistry, vol. 278, no. 46, pp. 45485–45491, 2003. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- M. Armoni, C. Harel, S. Karni et al., “FOXO1 represses peroxisome proliferator-activated receptor-γ1 and -γ2 gene promoters in primary adipocytes: a novel paradigm to increase insulin sensitivity,” The Journal of Biological Chemistry, vol. 281, no. 29, pp. 19881–19891, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- W. Fan, T. Imamura, N. Sonoda et al., “FOXO1 transrepresses peroxisome proliferator-activated receptor γ transactivation, coordinating an insulin-induced feed-forward response in adipocytes,” The Journal of Biological Chemistry, vol. 284, no. 18, pp. 12188–12197, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- F. Wang and Q. Tong, “SIRT2 suppresses adipocyte differentiation by deacetylating FOXO1 and enhancing FOXO1's repressive interaction with PPARγ,” Molecular Biology of the Cell, vol. 20, no. 3, pp. 801–808, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- F. Lin, J. Qin, K. Tang, S. Y. Tsai, and M.-J. Tsai, “Coup d'Etat: an orphan takes control,” Endocrine Reviews, vol. 32, no. 3, pp. 404–421, 2011. View at Publisher · View at Google Scholar · View at PubMed
- A. Nifuji, H. Ideno, Y. Ohyama et al., “Nemo-like kinase (NLK) expression in osteoblastic cells and suppression of osteoblastic differentiation,” Experimental Cell Research, vol. 316, no. 7, pp. 1127–1136, 2010. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- W. Guo, J. Flanagan, R. Jasuja, J. Kirkland, L. Jiang, and S. Bhasin, “The effects of myostatin on adipogenic differentiation of human bone marrow-derived mesenchymal stem cells are mediated through cross-communication between Smad3 and Wnt/β-catenin signaling pathways,” The Journal of Biological Chemistry, vol. 283, no. 14, pp. 9136–9145, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- W. P. Cawthorn, F. Heyd, K. Hegyi, and J. K. Sethi, “Tumour necrosis factor-α inhibits adipogenesis via a β-catenin/TCF4(TCF7L2)-dependent pathway,” Cell Death and Differentiation, vol. 14, no. 7, pp. 1361–1373, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- W. P. Cawthorn and J. K. Sethi, “TNF-α and adipocyte biology,” FEBS Letters, vol. 582, no. 1, pp. 117–131, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- T. Fujisawa, “Hydra peptide project 1993–2007,” Development Growth and Differentiation, vol. 50, no. 1, pp. S257–S268, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- D. Lu, H. B. Cottam, M. Corr, and D. A. Carson, “Repression of β-catenin function in malignant cells by nonsteroidal antiinflammatory drugs,” Proceedings of the National Academy of Sciences of the United States of America, vol. 102, no. 51, pp. 18567–18571, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- R. E. Teresi and K. A. Waite, “Ppargamma, pten, and the fight against cancer,” PPAR Research, vol. 2008, Article ID 932632, 2008.
- M. Sharma, W. W. Chuang, and Z. Sun, “Phosphatidylinositol 3-kinase/Akt stimulates androgen pathway through GSK3β inhibition and nuclear β-catenin accumulation,” The Journal of Biological Chemistry, vol. 277, no. 34, pp. 30935–30941, 2002. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- K. Sakamoto, K. Iwasaki, H. Sugiyama, and Y. Tsuji, “Role of the tumor suppressor PTEN in antioxidant responsive element-mediated transcription and associated histone modifications,” Molecular Biology of the Cell, vol. 20, no. 6, pp. 1606–1617, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- J. Yi, S. Park, N. Brooks, B. T. Lang, and R. Vemuganti, “PPARγ agonist rosiglitazone is neuroprotective after traumatic brain injury via anti-inflammatory and anti-oxidative mechanisms,” Brain Research, vol. 1244, pp. 164–172, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- C. Garrido, M. Brunet, C. Didelot, Y. Zermati, E. Schmitt, and G. Kroemer, “Heat shock proteins 27 and 70: anti-apoptotic proteins with tumorigenic properties,” Cell Cycle, vol. 5, no. 22, pp. 2592–2601, 2006. View at Scopus
- S. Dodd, B. Hain, and A. Judge, “Hsp70 prevents disuse muscle atrophy in senescent rats,” Biogerontology, vol. 10, no. 5, pp. 605–611, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- W. Cai, J. L. Rudolph, S. M. W. Harrison et al., “An evolutionarily conserved rit GTPase-p38 MAPK signaling pathway mediates oxidative stress resistance,” Molecular Biology of the Cell, vol. 22, no. 17, pp. 3231–3241, 2011. View at Publisher · View at Google Scholar · View at PubMed
- A. Brunet, L. B. Sweeney, J. F. Sturgill et al., “Stress-dependent regulation of FOXO transcription factors by the SIRT1 deacetylase,” Science, vol. 303, no. 5666, pp. 2011–2015, 2004. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- R. R. Alcendor, S. Gao, P. Zhai et al., “Sirt1 regulates aging and resistance to oxidative stress in the heart,” Circulation Research, vol. 100, no. 10, pp. 1512–1521, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- 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 PubMed · View at Scopus
- L. Han, R. Zhou, J. Niu, M. A. McNutt, P. Wang, and T. Tong, “SIRT1 is regulated by a PPARγ-SIRT1 negative feedback loop associated with senescence,” Nucleic Acids Research, vol. 38, no. 21, pp. 7458–7471, 2010. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- P. Tontonoz, S. Singer, B. M. Forman et al., “Terminal differentiation of human liposarcoma cells induced by ligands for peroxisome proliferator-activated receptor γ and the retinoid X receptor,” Proceedings of the National Academy of Sciences of the United States of America, vol. 94, no. 1, pp. 237–241, 1997. View at Publisher · View at Google Scholar · View at Scopus
- Q. Gan, J. Huang, R. Zhou et al., “PPARγ accelerates cellular senescence by inducing expression in human diploid fibroblasts,” Journal of Cell Science, vol. 121, no. 13, pp. 2235–2245, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus