The roles of nuclear receptors CAR and PXR in hepatic energy metabolism

Drug Metabolism and Pharmacokinetics

Volumn 23, Issue 1, 2008, Pages 8-13

  Konno, Yoshihiro ^a   Negishi, Masahiko ^a   Kodama, Susumu ^a  

^a NATIONAL INSTITUTE OF ENVIRONMENTAL HEALTH SCIENCES   (United States)

Author keywords

Constitutive active androstane receptor (CAR); Cytochrome P450; Drug metabolism; Gluconeogenesis; Lipid metabolism; Pregnane X receptor (PXR); Thyroid hormone

Indexed keywords

CONSTITUTIVE ANDROSTANE RECEPTOR; CYCLIC AMP BINDING PROTEIN; GLUCAGON; GLUCOSE 6 PHOSPHATASE; HEPATOCYTE NUCLEAR FACTOR 3BETA; INSULIN; LIOTHYRONINE; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR GAMMA COACTIVATOR 1ALPHA; PHOSPHOENOLPYRUVATE CARBOXYKINASE (GTP); PREGNANE X RECEPTOR; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; SULFOTRANSFERASE 1A1; THYROID HORMONE; THYROTROPIN; THYROXINE; THYROXINE DEIODINASE; TRANSCRIPTION FACTOR FKHR; CELL RECEPTOR; STEROID RECEPTOR; TRANSCRIPTION FACTOR;

DOWN REGULATION; ENERGY METABOLISM; FATTY ACID OXIDATION; GENE EXPRESSION REGULATION; GLUCONEOGENESIS; GLUCOSE BLOOD LEVEL; HORMONE ACTION; HUMAN; INSULIN BLOOD LEVEL; INSULIN SENSITIVITY; KETOGENESIS; LIOTHYRONINE BLOOD LEVEL; LIPID METABOLISM; LIPOGENESIS; LIVER FUNCTION; MOLECULAR INTERACTION; NONHUMAN; PROTEIN BINDING; PROTEIN FUNCTION; REVIEW; THYROID HORMONE SYNTHESIS; THYROTROPIN BLOOD LEVEL; THYROXINE BLOOD LEVEL; TRANSCRIPTION REGULATION; UPREGULATION; ANIMAL; CELL NUCLEUS; GENETICS; LIVER; METABOLISM; PHYSIOLOGY; SIGNAL TRANSDUCTION;

ANIMALS; CELL NUCLEUS; ENERGY METABOLISM; HUMANS; LIVER; RECEPTOR CROSS-TALK; RECEPTORS, CYTOPLASMIC AND NUCLEAR; RECEPTORS, STEROID; TRANSCRIPTION FACTORS;

EID: 42249111748     PISSN: 13474367     EISSN: 18800920     Source Type: Journal    
DOI: 10.2133/dmpk.23.8     Document Type: Review

References (38)

1. Honkakonski, P., Zelko, I., Sueyoshi, T. and Negishi, M.: The nuclear orphan receptor CAR-retinoid X receptor heterodimer activates the phenobarbital-responsive enhancer module of the CYP2B gene. Mol. Cell. Biol., 18: 5652-5658 (1998).
2. Wei, P., Zhang, J., Egan-Hafley, M., Liang, S. and Moore, D. D.: The nuclear receptor CAR mediates specific xenobiotic induction of drug metabolism. Nature, 407: 920-923 (2000).
3. Kodama, S. and Negishi, M.: Phenobarbital confers its diverse effects by activating the orphan nuclear receptor CAR. Drug Metab. Rev., 38: 75-87 (2006).
4. Urquhart, B. L., Tirona, R. G. and Kim, R. B.:Nuclear receptors and the regulation of drug-metabolizing enzymes and drug transporters: implications for interindividual variability in response to drugs. J. Clin. Pharmacol., 47: 566-78 (2007).
5. Sugatani, J., Yamakawa, K., Yoshinari, K., Machida, T., Takagi, H., Mori, M., Kakizaki, S., Sueyoshi, T., Negishi, M. and Miwa, M.: Identification of a defect in the UGT1A1 gene promoter and its association with hyperbilirubinemia. Biochem. Biophys. Res. Commun., 292: 492-497 (2002).
6. Eloranta, J. J. and Kullak-Ublick, G. A.: Coordinate transcriptional regulation of bile acid homeostasis and drug metabolism. Arch. Biochem. Biophys., 433: 397-412 (2005).
7. Herzig, S., Long, F., Jhala, U. S., Hedrick, S., Quinn, R., Bauer, A., Rudolph, D., Schutz, G., Yoon, C., Puigserver, P., Spiegelman, B. and Montminy, M.: CREB regulates hepatic gluconeogenesis through the activator PGC-1. Nature, 413: 179-183 (2001).
8. Kurukulasuriya, R., Link, J. T., Madar, D. J., Pei, Z., Richards, S. J., Rohde, J. J., Souers, A. J. and Szczepankiewicz, B. G.: Potential drug targets and progress towards pharmacologic inhibition of hepatic glucose production. Curr. Med. Chem., 10: 123-153 (2003).
9. Nakae, J., Kitamura, T., Silver, D. L. and Accill, D.: The forkhead transcription factor FoxO1 (Fkhr) confers insulin sensitivity onto glucose-6-phosphatase expression. J. Clin. Investig., 108: 1359-1367 (2001).
10. Kodama, S., Moore, R., Yamamoto, Y. and Negishi, M.: Human nuclear pregnane X receptor cross-talk with CREB to repress cAMP activation of the glucose-6-phosphatase gene. Biochem. J., 407: 373-381 (2007).
11. Matsuzaki, H., Daitoku, H., Hatta, M., Tanaka, K. and Fukamizu, A.: Insulin-induced phosphorylation on FKHR (Foxo1) targets to proteosomal degradation. Proc. Natl. Acad. Sci. USA, 100: 11285-11290 (2003).
12. Lahtela, J. T., Arranto, A. J. and Sotanaient, E. A.: Enzyme inducers improve insulin sensitivity in non-insulin-dependent diabetic subjects. Diabetes, 34: 911-916 (1985).
13. Manenti, G., Dragani, T. A. and Della Porta, G.: Effects of phenobarbital and 1, 4-bis[2-(3, 5-dichloropyridyloxy)]benzene on differentiated functions in mouse liver. Chem. Biol. Interact., 64: 83-92 (1987).
14. Argaud, D., Halimi, S., Catelloni, F. and Leverve, X. M.: Inhibition of gluconeogenesis in isolated rat hepatocytes after chronic treatment with phenobarbital. Biochem. J., 280: 663-669 (1991).
15. Kodama, S., Koike, C., Negishi, M. and Yamamoto, Y.: Nuclear Receptors CAR and PXR cross talk with FOXO1 to regulate genes that encode drug-metabolizing and gluconeogenic enzymes. Mol. Cell. Biol., 24: 7931-7940 (2004).
16. Miao, J., Fang, S., Bae, Y. and Kemper J. K.: Functional inhibitory cross-talk between constitutive androstane receptor and hepatic nuclear factor-4 in hepatic lipid/glucose metabolism is mediated by competition for binding to the DR1 motif and to the common coactivators, GRIP-1 and PGC-1α. J. Biol. Chem., 281: 14537-14546 (2006).
17. Sidhu, J. S. and Omiecinski, C. J.: Insulin-mediated modulation of cytochrome P450 gene induction profiles on primary rat hepatocytes cultures. J. Biochem. Mol. Toxicol., 13: 1-9 (1999).
18. Yamazoe, Y., Murayama, N., Shimada, M., Yamauchi, K. and Kato, R.: Cytochrome P450 in livers of diabetic rats: regulation by growth hormone and insulin. Arch. Biochem. Biophys., 268: 567-575 (1989).
19. Zhang, W., Patil, S., Chauhan, B., Guo, S., Powell, D. R., Le, J., Klotsas, A., Matika, R., Xiao, X., Franks, R., Heidenreich, K. A., Sajan, M. P., Farese, R. V., Stolz, D. B., Tso, P., Koo, S. H., Montminy, M. and Unterman, T. G.: FoxO1 regulates multiple metabolic pathways in the liver: effects on gluconeogenic, glycolytic, and lipogenic gene expression. J. Biol. Chem., 281: 10105-10117 (2006).
20. Hegardt, F. G.: Mitochondrial 3-hydroxy-3-methylglutaryl-CoA synthase: a control enzyme in ketogenesis, Biochem. J., 338: 569-582 (1999).
21. Louet, J. F., LeMay, C., Pegorier, J. P., Decaux, J. F. and Girard, J.: Regulation of liver carnitine palmitoyltransferase I gene expression by hormones and fatty acids, Biochem. Soc. Trans., 29: 310-316 (2001).
22. Dobrzyn, A. and Ntambi, J. M.: The role of stearoyl-CoA desaturase in the control of metabolism. Prostaglandins Leukot. Essent. Fatty Acids, 73: 35-41 (2005).
23. Wolfrum, C., Asilmaz, E., Luca, E., Friedman, J. M. and Stoffel, M.: Foxa2 regulates lipid metabolism and ketogenesis in the liver during fasting and in diabetes. Nature, 432: 1027-1032 (2004).
24. Wolfrum, C., Besser, D., Luca, E. and Stoffel, M.: Insulin regulates the activity of forkhead transcription factor Hnf-3beta/Foxa-2 by Akt-mediated phosphorylation and nuclear/cytosolic localization, Proc. Natl. Acad. Sci. USA, 100: 11624-11629 (2003).
25. Tabor, D. E., Kim, J. B., Spiegelman, B. M. and Edwards, P. A.: Identification of conserved cis-elements and transcription factors required for sterol-regulated transcription of stearoyl-CoA desaturase 1 and 2. J. Biol. Chem., 274: 20603-20610 (1999).
26. Nakamura, K., Moore, R., Negishi, M. and Sueyoshi, T.: Nuclear pregnane X receptor cross-talk with FoxA2 to mediate drug-induced regulation of lipid metabolism in fasting mouse liver. J. Biol. Chem., 282: 9768-9776 (2007).
27. Zhou, J., Zhai, Y., Mu, Y., Gong, H., Uppal, H., Toma, D., Ren, S., Evans, R. M. and Xie, W.: A novel pregnane X receptor-mediated and sterol regulatory element-binding protein-independent lipogenic pathway. J. Biol. Chem., 281: 15013-15020 (2006).
28. Bianco, A. C., Salvatore, D., Gereben, B., Berry, M. J. and Larsen, P. R.: Biochemistry, cellular and molecular biology, and physiological roles of the iodothyronine selenodeiodinases. Endocr. Rev., 23: 38-89 (2002).
29. Sutija, M. and Joss, J. M.: Thyroid hormone deiodinases revisited: insights from lungfish: a review. J. Comp. Physiol[B]., 176: 87-92 (2006).
30. Mitchell, A. M., Manley, S.W., Rowan, K. A. and Mortimer, R. H.: Uptake of reverse T3 in the human choriocarcinoma cell line, JAr. Placenta, 20: 65-70 (1999).
31. Tien, E. S., Matsui, K., Moore, R. and Negishi, M.: The nuclear receptor constitutively active/androstane receptor regulates type 1 deiodinase and thyroid hormone activity in the regenerating mouse liver. J. Pharmacol. Exp. Ther., 320: 307-313 (2007).
32. Curran, P. G. and DeGroot, L. J.: The effect of hepatic enzymeinducing drugs on thyroid hormones and the thyroid gland. Endocr. Rev., 12: 135-150 (1991).
33. Diwan, B. A., Hennenman, J. R., Rice, J. M. and Nims, R. W.: Enhancement of thyroid and hepatocarcinogenesis by 1, 4-bis[2-(3, 5-dichloropyridyloxy)]benzene in rats at doses that cause maximal induction of CYP2B. Carcinogenesis, 17: 37-43 (1996).
34. Schneider, M. J., Fiering, S. N., Thai, B., Wu, S. Y., St. Germain, E., Parlow, A. F., St. Germain, D. L. and Galton, V. A.: Targeted disruption of the type 1 selenodeiodinase gene (Dio1) results in marked changes in thyroid hormone economy in mice. Endocrinology, 147: 580-589 (2006).
35. Maglich, J. M., Watson, J., McMillen, P. J., Goodwin, B., Willson, T. M. and Moore, J. T.: The nuclear receptor CAR is a regulator of thyroid hormone metabolism during caloric restriction. J. Biol. Chem., 279: 19832-19838 (2004).
36. Qatanani, M., Zhang, J. and Moore, D. D.: Role of the constitutive androstane receptor in xenobiotic-induced thyroid hormone metabolism. Endocrinology, 146: 995-1002 (2005).
37. Hegedus, L., Hansen, J. M., Luhdorf, K., Perrild, H., Feldt-Rasmussen, U. and Kampmann, J. P.: Increased frequency of goitre in epileptic patients on long-term phenytoin or carbamazepine treatment. Clin. Endocrinol. (Oxf), 23: 423-429 (1985).
38. Visser, T. J., Kaptein, E., Glatt, H., Bartsch, I., Hagen, M. and Coughtrie, M. W.: Characterization of thyroid hormone sulfotransferases. Chem. Biol. Interact., 109: 279-291 (1998).