Modulation of adipogenesis-related gene expression by estrogen-related receptor γ during adipocytic differentiation

Biochimica et Biophysica Acta - Gene Regulatory Mechanisms

Volumn 1789, Issue 2, 2009, Pages 71-77

  Kubo, Mayumi ^a,b   Ijichi, Nobuhiro ^a   Ikeda, Kazuhiro ^a   Horie Inoue, Kuniko ^a   Takeda, Satoru ^b   Inoue, Satoshi ^a,c  

^a SAITAMA MEDICAL UNIVERSITY   (Japan)

^b JUNTENDO UNIVERSITY SCHOOL OF MEDICINE   (Japan)

^c UNIVERSITY OF TOKYO   (Japan)

Author keywords

3T3 L1; Adipocyte differentiation; Estrogen related receptor (ERR ); Pluripotent mesenchymal cell; Preadipocyte

Indexed keywords

CYCLIC AMP; ESTROGEN RELATED RECEPTOR GAMMA; FATTY ACID BINDING PROTEIN 4; GLUCOCORTICOID; INSULIN; MESSENGER RNA; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR GAMMA; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR GAMMA COACTIVATOR 1BETA; SMALL INTERFERING RNA; STEROID RECEPTOR; UNCLASSIFIED DRUG;

ADIPOCYTE; ADIPOGENESIS; ANIMAL CELL; ANIMAL EXPERIMENT; ANIMAL TISSUE; ARTICLE; BROWN ADIPOSE TISSUE; CELL DIFFERENTIATION; CELL STRAIN 3T3; CONTROLLED STUDY; DOWN REGULATION; GENE EXPRESSION; LIPID DIET; MARKER GENE; MESENCHYME CELL; MOUSE; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; UPREGULATION; WHITE ADIPOSE TISSUE;

3T3-L1 CELLS; ADIPOCYTES; ADIPOGENESIS; ANIMALS; CELL DIFFERENTIATION; CELL LINE; GENE EXPRESSION REGULATION; MALE; MICE; MICE, INBRED C57BL; RECEPTORS, ESTROGEN; REVERSE TRANSCRIPTASE POLYMERASE CHAIN REACTION; RNA INTERFERENCE;

MURINAE; MUS;

EID: 58149501124     PISSN: 18749399     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbagrm.2008.08.012     Document Type: Article

References (40)

1. Shi Y., and Burn P. Lipid metabolic enzymes: emerging drug targets for the treatment of obesity. Nat. Rev. Drug Discov. 3 (2004) 695-710
2. Shepherd P.R., Gnudi L., Tozzo E., Yang H., Leach F., and Kahn B.B. Adipose cell hyperplasia and enhanced glucose disposal in transgenic mice overexpressing GLUT4 selectively in adipose tissue. J. Biol. Chem. 268 (1993) 22243-22246
3. Kershaw E.E., and Flier J.S. Adipose tissue as an endocrine organ. J. Clin. Endocrinol. Metab. 89 (2004) 2548-2556
4. Frühbeck G., Gomez-Ambrosi J., Muruzabal F.J., and Burrell M.A. The adipocyte: a model for integration of endocrine and metabolic signaling in energy metabolism regulation. Am. J. Physiol. Endocrinol. Metab. 280 (2001) E827-E847
5. Giguère V., Yang N., Segui P., and Evans R.M. Identification of a new class of steroid hormone receptors. Nature 331 (1988) 91-94
6. Hong H., Yang L., and Stallcup M.R. Hormone-independent transcriptional activation and coactivator binding by novel orphan nuclear receptor ERR3. J. Biol. Chem. 274 (1999) 22618-22626
7. Heard D.J., Norby P.L., Holloway J., and Vissing H. Human ERRγ-related receptor (ERR) subfamily of orphan nuclear receptors: tissue-specific isoforms are expressed during development and in the adult. Mol. Endocrinol. 14 (2000) 382-392
8. Sladek R., Bader J.A., and Giguère V. The orphan nuclear receptor estrogen-related receptor α- is a transcriptional regulator of the human medium-chain acyl coenzyme A dehydrogenase gene. Mol. Cell. Biol. 17 (1997) 5400-5409
9. Vega R.B., and Kelly D.P. A role for estrogen-related receptor α in the control of mitochondrial fatty acid β-oxidation during brown adipocyte differentiation. J. Biol. Chem. 272 (1997) 31693-31699
10. Luo J., Sladek R., Carrier J., Bader J.A., Richard D., and Giguere V. Reduced fat mass in mice lacking orphan nuclear receptor estrogen-related receptor α. Mol. Cell. Biol. 23 (2003) 7947-7956
11. Ijichi N., Ikeda K., Horie-Inoue K., Yagi K., Okazaki Y., and Inoue S. Estrogen-related receptor α modulates the expression of adipogenesis-related genes during adipocyte differentiation. Biochem. Biophys. Res. Commun. 358 (2007) 813-818
12. Alaynick W.A., Kondo R.P., Xie W., He W., Dufour C.R., Downes M., Jonker J.W., Giles W., Naviaux R.K., Giguère V., and Evans R.M. ERRγ directs and maintains the transition to oxidative metabolism in the postnatal heart. Cell. Metab. 6 (2007) 13-24
13. Knutti D., and Kralli A. PGC-1, a versatile coactivator. Trends Endocrinol. Metab. 12 (2001) 360-365
14. Puigserver P., and Spiegelman B.M. Peroxisome proliferator-activated receptor-γ coactivator 1α (PGC-1α): transcriptional coactivator and metabolic regulator. Endocr. Rev. 24 (2003) 78-90
15. Lin J., Tarr P.T., Yang R., Rhee J., Puigserver P., Newgard C.B., and Spiegelman B.M. PGC-1β in the regulation of hepatic glucose and energy metabolism. J. Biol. Chem. 278 (2003) 30843-30848
16. St-Pierre J., Lin J., Krauss S., Tarr P.T., Yang R., Newgard C.B., and Spiegelman B.M. Bioenergetic analysis of peroxisome proliferator-activated receptor γ coactivators 1α and 1β (PGC-1α and PGC-1β) in muscle cells. J. Biol. Chem. 278 (2003) 26597-26603
17. Yagi K., Kondo D., Okazaki Y., and Kano K. A novel preadipocyte cell line established from mouse adult mature adipocytes. Biochem. Biophys. Res. Commun. 321 (2004) 967-974
18. Horie-Inoue K., Takayama K., Bono H.U., Ouchi Y., Okazaki Y., and Inoue S. Identification of novel steroid target genes through the combination of bioinformatics and functional analysis of hormone response elements. Biochem. Biophys. Res. Commun. 339 (2006) 99-106
19. Niwa H., Yamamura K., and Miyazaki J. Efficient selection for high-expression transfectants with a novel eukaryotic vector. Gene 108 (1991) 193-199
20. Green H., and Meuth M. An established pre-adipose cell line and its differentiation in culture. Cell 3 (1974) 127-133
21. Student A.K., Hsu R.Y., and Lane M.D. Induction of fatty acid synthetase synthesis in differentiating 3T3-L1 preadipocytes. J. Biol. Chem. 255 (1980) 4745-4750
22. Ding J., Nagai K., and Woo J.T. Insulin-dependent adipogenesis in stromal ST2 cells derived from murine bone marrow. Biosci. Biotechnol. Biochem. 67 (2003) 314-321
23. Taylor S.M., and Jones P.A. Multiple new phenotypes induced in 10T1/2 and 3T3 cells treated with 5-azacytidine. Cell 17 (1979) 771-779
24. Huss J.M., Kopp R.P., and Kelly D.P. Peroxisome proliferator-activated receptor coactivator-1α (PGC-1α) coactivates the cardiac-enriched nuclear receptors estrogen-related receptor-α and -γ. J. Biol. Chem. 277 (2002) 40265-40274
25. Zhang Y., Ma K., Sadana P., Chowdhury F., Gaillard S., Wang F., McDonnell D.P., Unterman T.G., Elam M.B., and Park E.A. Estrogen-related receptors stimulate pyruvate dehydrogenase kinase isoform 4 gene expression. J. Biol. Chem. 281 (2006) 39897-39906
26. Greschik H., Wurtz J.M., Sanglier S., Bourguet W., van Dorsselaer A., Moras D., and Renaud J.P. Structural and functional evidence for ligand-independent transcriptional activation by the estrogen-related receptor 3. Mol. Cell 9 (2002) 303-313
27. Kallen J., Schlaeppi J.M., Bitsch F., Filipuzzi I., Schilb A., Riou V., Graham A., Strauss A., Geiser M., and Fournier B. Evidence for ligand-independent transcriptional activation of the human estrogen-related receptor α (ERRα): crystal structure of ERRα ligand binding domain in complex with peroxisome proliferator-activated receptor coactivator-1α. J. Biol Chem. 279 (2004) 49330-49337
28. Wang L., Zuercher W.J., Consler T.G., Lambert M.H., Miller A.B., Orband-Miller L.A., McKee D.D., Willson T.M., and Nolte R.T. X-ray crystal structures of the estrogen-related receptor-γ ligand binding domain in three functional states reveal the molecular basis of small molecule regulation. J. Biol. Chem. 281 (2006) 37773-37781
29. Zhang Z., and Teng C.T. Estrogen receptor-related receptor α1 interacts with coactivator and constitutively activates the estrogen response elements of the human lactoferrin gene. J. Biol. Chem. 275 (2000) 20837-20846
30. Xie W., Hong H., Yang N.N., Lin R.J., Simon C.M., Stallcup M.R., and Evans R.M. Constitutive activation of transcription and binding of coactivator by estrogen-related receptors 1 and 2. Mol. Endocrinol. 13 (1999) 2151-2162
31. Hentschke M., Susens U., and Borgmeyer U. PGC-1 and PERC, coactivators of the estrogen receptor-related receptor γ. Biochem. Biophys. Res. Commun. 299 (2002) 872-879
32. Kamei Y., Ohizumi H., Fujitani Y., Nemoto T., Tanaka T., Takahashi N., Kawada T., Miyoshi M., Ezaki O., and Kakizuka A. PPARγ coactivator 1β/ERR ligand 1 is an ERR protein ligand, whose expression induces a high-energy expenditure and antagonizes obesity. Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 12378-12383
33. Schreiber S.N., Knutti D., Brogli K., Uhlmann T., and Kralli A. The transcriptional coactivator PGC-1 regulates the expression and activity of the orphan nuclear receptor estrogen-related receptor α (ERRα). J. Biol. Chem. 278 (2003) 9013-9018
34. Willy P.J., Murray I.R., Qian J., Busch B.B., Stevens Jr. W.C., Martin R., Mohan R., Zhou S., Ordentlich P., Wei P., Sapp D.W., Horlick R.A., Heyman R.A., and Schulman I.G. Regulation of PPARγ coactivator 1α (PGC-1α) signaling by an estrogen-related receptor α (ERRα) ligand. Proc. Natl. Acad. Sci. U. S. A. 101 (2004) 8912-8917
35. Huss J.M., Torra I.P., Staels B., Giguere V., and Kelly D.P. Estrogen-related receptor α directs peroxisome proliferator-activated receptor α signaling in the transcriptional control of energy metabolism in cardiac and skeletal muscle. Mol. Cell. Biol. 24 (2004) 9079-9091
36. Dufour C.R., Wilson B.J., Huss J.M., Kelly D.P., Alaynick W.A., Downes M., Evans R.M., Blanchette M., and Giguère V. Genome-wide orchestration of cardiac functions by the orphan nuclear receptors ERRα and γ. Cell Metab. 5 (2007) 345-356
37. Wang L., Liu J., Saha P., Huang J., Chan L., Spiegelman B., and Moore D.D. The orphan nuclear receptor SHP regulates PGC-1α expression and energy production in brown adipocytes. Cell Metab. 2 (2005) 227-238
38. Zhang Z., and Teng C.T. Interplay between estrogen-related receptor alpha (ERRα) and gamma (ERRγ) on the regulation of ERRα gene expression. Mol. Cell. Endocrinol. 264 (2007) 128-141
39. Luo J., Sladek R., Bader J.A., Matthyssen A., Rossant J., and Giguère V. Placental abnormalities in mouse embryos lacking the orphan nuclear receptor ERR-β. Nature 388 (1997) 778-782
40. Yu S., Wong Y.C., Wang X.H., Ling M.T., Ng C.F., Chen S., and Chan F.L. Orphan nuclear receptor estrogen-related recfseptor-beta suppresses in vitro and in vivo growth of prostrate cancer cells via p21 (WAF1/CIP1) induction and as a potential therapeutic target in prostate cancer. Oncogene (2007) 1-16