Effects of coumestrol on lipid and glucose metabolism as a farnesoid X receptor ligand

Biochemical and Biophysical Research Communications

Volumn 372, Issue 3, 2008, Pages 395-399

  Takahashi, Miki ^a,d   Kanayama, Tomohiko ^b,d   Yashiro, Takuya ^b   Kondo, Hidehiko ^a   Murase, Takatoshi ^a   Hase, Tadashi ^a   Tokimitsu, Ichiro ^a   Nishikawa, Jun ichi ^c   Sato, Ryuichiro ^b,d  

^a KAO CORPORATION   (Japan)

^b UNIVERSITY OF TOKYO   (Japan)

^c MUKOGAWA WOMEN'S UNIVERSITY   (Japan)

^d Basic Research Activities for Innovative Biosciences   (Japan)

Author keywords

CoA BAP system; Coumestrol; Farnesoid X receptor; Glucose metabolism; Ligand; Lipid metabolism; Nuclear receptor; SHP

Indexed keywords

COUMESTROL; FARNESOID X RECEPTOR; GLUCOSE; HEPATOCYTE NUCLEAR FACTOR 4ALPHA; LIPID; LIVER X RECEPTOR;

ARTICLE; CONTROLLED STUDY; GENE ACTIVATION; GENE CONTROL; GENE TARGETING; GLUCOSE METABOLISM; HORMONE BINDING; HUMAN; HUMAN CELL; IN VITRO STUDY; LIPID METABOLISM; PRIORITY JOURNAL;

APOLIPOPROTEINS B; CELL LINE; COUMESTROL; DNA-BINDING PROTEINS; GLUCOSE; HUMANS; LIGANDS; LIPID METABOLISM; PHYTOESTROGENS; RECEPTORS, CYTOPLASMIC AND NUCLEAR; TRANSCRIPTION FACTORS; TRANSCRIPTION, GENETIC;

EID: 44749086172     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2008.04.136     Document Type: Article

References (27)

1. Chiang J.Y., Kimmel R., Weinberger C., and Stroup D. Farnesoid X receptor responds to bile acids and represses cholesterol 7α-hydroxylase gene (CYP7A1) transcription. J. Biol. Chem. 275 (2000) 10918-10924
2. Grober J., Zaghini I., Fujii H., Jones S.A., Kliewer S.A., Willson T.M., Ono T., and Besnard P. Identification of a bile acid-responsive element in the human ileal bile acid-binding protein gene. Involvement of the farnesoid X receptor/9-cis-retinoic acid receptor heterodimer. J. Biol. Chem. 274 (1999) 29749-29754
3. Urizar N.L., Dowhan D.H., and Moore D.D. The farnesoid X-activated receptor mediates bile acid activation of phospholipid transfer protein gene expression. J. Biol. Chem. 275 (2000) 39313-39317
4. Claudel T., Sturm E., Duez H., Torra I.P., Sirvent A., Kosykh V., Fruchart J.C., Dallongeville J., Hum D.W., Kuipers F., and Staels B. Bile acid-activated nuclear receptor FXR suppresses apolipoprotein A-I transcription via a negative FXR response element. J. Clin. Invest. 109 (2002) 961-971
5. Ma K., Saha P.K., Chan L., and Moore D.D. Farnesoid X receptor is essential for normal glucose homeostasis. J. Clin. Invest. 116 (2006) 1102-1109
6. Goodwin B., Jones S.A., Price R.R., Watson M.A., McKee D.D., Moore L.B., Galardi C., Wilson J.G., Lewis M.C., Roth M.E., Maloney P.R., Willson T.M., and Kliewer S.A. A regulatory cascade of the nuclear receptors FXR, SHP-1 and LRH-1 represses bile acid biosynthesis. Mol. Cell 6 (2000) 517-526
7. Lu T.T., Makishima M., Repa J.J., Schoonjans K., Kerr T.A., Auwerx J., and Mangelsdorf D.J. Molecular basis for feedback regulation of bile acid synthesis by nuclear receptors. Mol. Cell 6 (2000) 507-515
8. Lee Y.K., Dell H., Dowhan D.H., Hadzopoulou-Cladaras M., and Moore D.D. The orphan nuclear receptor SHP inhibits hepatocyte nuclear factor 4 and retinoid X receptor transactivation: two mechanisms for repression. Mol. Cell. Biol. 20 (2000) 187-195
9. Brendel C., Schoonjans K., Botrugno O.A., Treuter E., and Auwerx J. The small heterodimer partner interacts with the liver X receptor α and represses its transcriptional activity. Mol. Endocrinol. 16 (2002) 2065-2076
10. Repa J.J., Liang G., Ou J., Bashmakov Y., Lobaccaro J.M., Shimomura I., Shan B., Brown M.S., Goldstein J.L., and Mangelsdorf D.J. Regulation of mouse sterol regulatory element-binding protein-1c gene (SREBP-1c) by oxysterol receptors, LXRα and LXRβ. Genes Dev. 14 (2000) 2819-2830
11. Yoshikawa T., Shimano H., Amemiya-Kudo M., Yahagi N., Hasty A.H., Matsuzaka T., Okazaki H., Tamura Y., Iizuka Y., Ohashi K., Osuga J., Harada K., Gotoda T., Kimura S., Ishibashi S., and Yamada N. Identification of liver X receptor-retinoid X receptor as an activator of the sterol regulatory element-binding protein 1c gene promoter. Mol. Cell. Biol. 21 (2001) 2991-3000
12. McKenna N.J., Lanz R.B., and O'Malley B.W. Nuclear receptor coregulators: cellular and molecular biology. Endocr. Rev. 20 (1999) 321-344
13. Collingwood T.N., Urnov F.D., and Wolffe A.P. Nuclear receptors: coactivators, corepressors and chromatin remodeling in the control of transcription. J. Mol. Endocrinol. 23 (1999) 255-275
14. Robyr D., Wolffe A.P., and Wahli W. Nuclear hormone receptor coregulators in action: diversity for shared tasks. Mol. Endocrinol. 14 (2000) 329-347
15. Voegel J.J., Heine M.J., Zechel C., Chambon P., and Gronemeyer H. TIF2, a 160 kDa transcriptional mediator for the ligand-dependent activation function AF-2 of nuclear receptors. EMBO J. 15 (1996) 3667-3675
16. Chen J.D., and Evans R.M. A transcriptional co-repressor that interacts with nuclear hormone receptors. Nature 377 (1995) 454-457
17. Kanayama T., Mamiya S., Nishihara T., and Nishikawa J. Basis of a high-throughput method for nuclear receptor ligands. J. Biochem. (Tokyo) 133 (2003) 791-797
18. Kanayama T., Arito M., So K., Hachimura S., Inoue J., and Sato R. Interaction between sterol regulatory element-binding proteins and liver receptor homolog-1 reciprocally suppresses their transcriptional activities. J. Biol. Chem. 282 (2007) 10290-10298
19. Nakahara M., Furuya N., Takagaki K., Sugaya T., Hirota K., Fukamizu A., Kanda T., F ujii H., and Sato R. Ileal bile acid-binding protein, functionally associated with the farnesoid X receptor or the ileal bile acid transporter, regulates bile acid activity in the small intestine. J. Biol. Chem. 280 (2005) 42283-42289
20. Lai K., Harnish D.C., and Evans M.J. Estrogen receptor α regulates expression of the orphan receptor small heterodimer partner. J. Biol. Chem. 278 (2003) 36418-36429
21. Knuckles B.E., De Fremery D., and Kohler G.O. Coumestrol content of fractions obtained during wet processing of alfalfa. J. Agr. Food Chem. 24 (1976) 1177-1180
22. Kuiper G.G., Carlsson B., Grandien K., Enmark E., Haggblad J., Hilsson S., and Gustafsson J.A. Comparison of the ligand binding specificity and transcript tissue distribution of estrogen receptors α and β. Endocrinology 138 (1997) 863-870
23. Dodge J.A., Glasebrook A.L., Magee D.E., Phillips D.L., Sato M., Short L.L., and Bryant H.U. Environmental estrogens: effects on cholesterol lowering and bone in the ovariectomized rat. J. Steroid Biochem. Mol. Biol. 59 (1996) 155-161
24. Draper C.R., Edel M.J., Dick I.M., Randall A.G., Martin G.B., and Prince R.L. Phytoestrogens reduce bone loss and bone resorption in oophorectomized rats. J. Nutr. 127 (1997) 1795-1799
25. Watanabe M., Houten S.M., Wang L., Moschetta A., Mangelsdorf D.J., Heyman R.A., Moore D.D., and Auwerx J. Bile acids lower triglyceride levels via a pathway involving FXR, SHP, and SREBP-1c. J. Clin. Invest. 113 (2004) 1408-1418
26. Urizar N.L., Liverman A.B., Dodds D.T., Silva F.V., Ordentlich P., Yan Y.Z., Gonzalez F.J., Heyman R.A., Mangelsdorf D.J., and Moore D.D. A natural product that lowers cholesterol as an antagonist ligand for FXR. Science 296 (2002) 1703-1706
27. Wang H., Li H., Moore L.B., Johnson M.D., Maglich J.M., Goodwin B., Ittoop O.R., Wisely B., Creech K., Parks D.J., Collins J.L., Willson T.M., Kalpana G.V., Venkatesh M., Xie W., Cho S.Y., Roboz J., Redinbo M., Moore J.T., and Mani S. The phytoestrogen coumestrol is a naturally occurring antagonist of the human pregnane X receptor. Mol. Endocrinol. 22 (2008) 838-857