Abstract
The ligand-dependent recruitment of coactivators to peroxisome
proliferator-activated receptor-
The ligand-dependent recruitment of coactivators to peroxisome
proliferator-activated receptor-
C Dreyer, G Krey, H Keller, F Givel, G Helftenbein, and W Wahli, “Control of the peroxisomal -oxidation pathway by a novel family of nuclear hormone receptors,” Cell, vol. 68, no. 5, pp. 879–887, 1992.
View at: Google ScholarR A Roberts, N H James, N J Woodyatt, N Macdonald, and J D Tugwood, “Evidence for the suppression of apoptosis by the peroxisome proliferator activated receptor alpha (PPAR),” Carcinogenesis, vol. 19, no. 1, pp. 43–48, 1998.
View at: Google ScholarN H James, J H Gill, R Brindle et al., “Peroxisome proliferator-activated receptor (PPAR) alpha-regulated growth responses and their importance to hepatocarcinogenesis,” Toxicology Letters, vol. 102-103, pp. 91–96, 1998.
View at: Google ScholarM J Olson, “DNA strand breaks induced by hydrogen peroxide in isolated rat hepatocytes,” Journal of Toxicology and Environmental Health, vol. 23, no. 3, pp. 407–423, 1988.
View at: Google ScholarJ K Reddy and M S Rao, “Oxidative DNA damage caused by persistent peroxisome proliferation: its role in hepatocarcinogenesis,” Mutation Research, vol. 214, no. 1, pp. 63–68, 1989.
View at: Google ScholarY Yu, P H Correll, and J P Vanden Heuvel, “Conjugated linoleic acid decreases production of pro-inflammatory products in macrophages: evidence for a PPAR-dependent mechanism,” Biochimica et Biophysica Acta - Molecular and Cell Biology of Lipids, vol. 1581, no. 3, pp. 89–99, 2002.
View at: Google ScholarV H Coulthard, S Matsuda, and D M Heery, “An extended LXXLL motif sequence determines the nuclear receptor binding specificity of TRAP220,” Journal of Biological Chemistry, vol. 278, no. 13, pp. 10942–10951, 2003.
View at: Google ScholarD M Heery, S Hoare, S Hussain, M G Parker, and H Sheppard, “Core LXXLL motif sequences in CREB-binding protein, SRC1, and RIP140 define affinity and selectivity for steroid and retinoid receptors,” Journal of Biological Chemistry, vol. 276, no. 9, pp. 6695–6702, 2001.
View at: Google ScholarR B Lanz, N J McKenna, S A Onate et al., “A steroid receptor coactivator, SRA, functions as an RNA and is present in an SRC-1 complex,” Cell, vol. 97, no. 1, pp. 17–27, 1999.
View at: Google ScholarJ Bragança, T Swingler, F IR Marques et al., “Human CREB-binding protein/p300-interacting transactivator with ED-rich tail (CITED) 4, a new member of the CITED family, functions as a co-activator for transcription factor AP-2,” Journal of Biological Chemistry, vol. 277, no. 10, pp. 8559–8565, 2002.
View at: Google ScholarR T Nolte, G B Wisely, S Westin et al., “Ligand binding and co-activator assembly of the peroxisome proliferator- activated receptor-,” Nature, vol. 395, no. 6698, pp. 137–143, 1998.
View at: Google ScholarJ Uppenberg, C Svensson, M Jaki, G Bertilsson, L Jendeberg, and A Berkenstam, “Crystal structure of the ligand binding domain of the human nuclear receptor PPAR,” Journal of Biological Chemistry, vol. 273, no. 47, pp. 31108–31112, 1998.
View at: Google ScholarJ K Reddy, “Carcinogenicity of peroxisome proliferators: evaluation and mechanisms,” Biochemical Society Transactions, vol. 18, no. 1, pp. 92–94, 1990.
View at: Google ScholarC E Connor, J D Norris, G Broadwater et al., “Circumventing tamoxifen resistance in breast cancers using antiestrogens that induce unique conformational changes in the estrogen receptor,” Cancer Research, vol. 61, no. 7, pp. 2917–2922, 2001.
View at: Google ScholarP Dowell, V J Peterson, T M Zabriskie, and M Leid, “Ligand-induced peroxisome proliferator-activated receptor conformational change,” Journal of Biological Chemistry, vol. 272, no. 3, pp. 2013–2020, 1997.
View at: Google ScholarW K Sumanasekera, E S Tien, J W Davis, II, R Turpey, G H Perdew, and J P Vanden Heuvel, “Heat shock protein-90 (Hsp90) acts as a repressor of peroxisome proliferator-activated receptor- (PPAR) and PPAR activity,” Biochemistry, vol. 42, no. 36, pp. 10726–10735, 2003.
View at: Google ScholarJ D Tugwood, P R Holden, N H James, R A Prince, and R A Roberts, “A peroxisome proliferator-activated receptor-alpha (PPAR) cDNA cloned from guinea-pig liver encodes a protein with similar properties to the mouse PPAR: implications for species differences in responses to peroxisome proliferators,” Archives of Toxicology, vol. 72, no. 3, pp. 169–177, 1998.
View at: Google ScholarC-Y Chang, J D Norris, H Grøn et al., “Dissection of the LXXLL nuclear receptor-coactivator interaction motif using combinatorial peptide libraries: discovery of peptide antagonists of estrogen receptors and ,” Molecular and Cellular Biology, vol. 19, no. 12, pp. 8226–8239, 1999.
View at: Google ScholarE S Tien, J W Davis, and J P Vanden Heuvel, “Identification of the CREB-binding protein/p300-interacting protein CITED2 as a peroxisome proliferator-activated receptor coregulator,” Journal of Biological Chemistry, vol. 279, no. 23, pp. 24053–24063, 2004.
View at: Google ScholarY Kodera, K-I Takeyama, A Murayama, M Suzawa, Y Masuhiro, and S Kato, “Ligand type-specific interactions of peroxisome proliferator-activated receptor with transcriptional coactivators,” Journal of Biological Chemistry, vol. 275, no. 43, pp. 33201–33204, 2000.
View at: Google ScholarJ Xu, Y Qiu, F J DeMayo, S Y Tsai, M-J Tsai, and B W O'Malley, “Partial hormone resistance in mice with disruption of the steroid receptor coactivator-1 (SRC-1) gene,” Science, vol. 279, no. 5358, pp. 1922–1925, 1998.
View at: Google ScholarJ D Graham, D L Bain, J K Richer, T A Jackson, L Tung, and K B Horwitz, “Nuclear receptor conformation, coregulators, and tamoxifen-resistant breast cancer,” Steroids, vol. 65, no. 10-11, pp. 579–584, 2000.
View at: Google ScholarM Xu, K J Modarress, J EW Meeker, and S S Jr Simons, “Steroid-induced conformational changes of rat glucocorticoid receptor cause altered trypsin cleavage of the putative helix 6 in the ligand binding domain,” Molecular and Cellular Endocrinology, vol. 155, no. 1-2, pp. 85–100, 1999.
View at: Google ScholarR K Sharma, B G Lake, R Makowski et al., “Differential induction of peroxisomal and microsomal fatty-acid-oxidising enzymes by peroxisome proliferators in rat liver and kidney. Characterisation of a renal cytochrome P-450 and implications for peroxisome proliferation,” European Journal of Biochemistry, vol. 184, no. 1, pp. 69–78, 1989.
View at: Google ScholarS Haubenwallner, A D Essenburg, B C Barnett et al., “Hypolipidemic activity of select fibrates correlates to changes in hepatic apolipoprotein C-III expression: a potential physiologic basis for their mode of action,” Journal of Lipid Research, vol. 36, no. 12, pp. 2541–2551, 1995.
View at: Google ScholarT Takahashi, T Hirano, K Okada, and M Adachi, “Clinical and Experimental: apolipoprotein CIII deficiency prevents the development of hypertriglyceridemia in streptozotocin-induced diabetic mice,” Metabolism, vol. 52, no. 10, pp. 1354–1359, 2003.
View at: Google ScholarC Karagianni, S Stabouli, K Roumeliotou et al., “Severe hypertriglyceridaemia in diabetic ketoacidosis: clinical and genetic study,” Diabetic Medicine, vol. 21, no. 4, pp. 380–382, 2004.
View at: Google ScholarH Miyamoto, M Rahman, H Takatera et al., “A dominant-negative mutant of androgen receptor coregulator ARA54 inhibits androgen receptor-mediated prostate cancer growth,” Journal of Biological Chemistry, vol. 277, no. 7, pp. 4609–4617, 2002.
View at: Google ScholarY Wang and R J Miksicek, “Identification of a dominant negative form of the human estrogen receptor,” Molecular Endocrinology, vol. 5, no. 11, pp. 1707–1715, 1991.
View at: Google ScholarJ J Palvimo, P J Kallio, T Ikonen, M Mehto, and O A Janne, “Dominant negative regulation of trans-activation by the rat androgen receptor: roles of the N-terminal domain and heterodimer formation,” Molecular Endocrinology, vol. 7, no. 11, pp. 1399–1407, 1993.
View at: Google ScholarW Seol, H-S Choi, and D D Moore, “An orphan nuclear hormone receptor that lacks a DNA binding domain and heterodimerizes with other receptors,” Science, vol. 272, no. 5266, pp. 1336–1339, 1996.
View at: Google Scholar