Flavone and Isoflavone Phytoestrogens Are Agonists of Estrogen-Related Receptors

Molecular Cancer Research

Volumn 1, Issue 13, 2003, Pages 981-991

  Suetsugi, Masatomo ^a   Su, Leila ^a   Karlsberg, Kimberly ^a   Yuan, Yate Ching ^a   Chen, Shiuan ^a  

^a CITY OF HOPE NATIONAL MEDICAL CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

6,3',4' TRIHYDROXYFLAVONE; BIOCHANIN A; DAIDZEIN; ESTROGEN RECEPTOR ALPHA; ESTROGEN RECEPTOR BETA; FLAVONE DERIVATIVE; GENISTEIN; ISOFLAVONE DERIVATIVE; ISOPROTEIN; PHYTOESTROGEN; UNCLASSIFIED DRUG;

ARTICLE; CONTROLLED STUDY; DRUG EFFECT; DRUG STRUCTURE; FEMALE; GENETIC TRANSFECTION; HUMAN; HUMAN CELL; LABORATORY; MAMMAL CELL; NUCLEOTIDE SEQUENCE; PREDICTION; PRIORITY JOURNAL; TWO HYBRID SYSTEM;

BINDING, COMPETITIVE; COMPUTER SIMULATION; DATABASES, FACTUAL; FLAVONOIDS; GENISTEIN; HELA CELLS; HUMANS; ISOFLAVONES; LIGANDS; LUCIFERASES; MODELS, MOLECULAR; MOLECULAR STRUCTURE; PHYTOESTROGENS; PLANT PREPARATIONS; RECEPTORS, CYTOPLASMIC AND NUCLEAR; RECEPTORS, ESTROGEN; RECOMBINANT FUSION PROTEINS; STRUCTURE-ACTIVITY RELATIONSHIP; TRANSFECTION;

MAMMALIA;

EID: 0344011490     PISSN: 15417786     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (31)

1. Giguere, V., Yang, N., Segui, P., and Evans, R. M. Identification of a new class of steroid hormone receptors. Nature, 331: 91-94, 1988.
2. Eudy, J. D., Yao, S., Weston, M. D., Ma-Edmonds, M., Talmadge, C. B., Cheng, J. J., Kimberling, W. J., and Sumegi, J. Isolation of a gene encoding a novel member of the nuclear receptor superfamily from the critical region of Usher syndrome type IIa at Iq41. Genomics, 50: 382-384, 1998.
3. 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: 22618-22626, 1999.
4. Yang, N., Shigeta, H., Shi, H., and Teng, C. T. Estrogen-related receptor. hERR1, modulates estrogen receptor-mediated response of human lactoferrin gene promoter. J. Biol. Chem., 271: 5795-5804, 1996.
5. Chen, S., Zhou, D., Yang, C., and Sherman, M. Molecular basis for the constitutive activity of estrogen-related receptor α-1. J. Biol. Chem., 276: 28465-28470, 2001.
6. 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: 303-313, 2002.
7. Yang, C. and Chen, S. Two organochlorine pesticides, toxaphene and chlordane, are antagonists for estrogen-related receptor α-1 orphan receptor. Cancer Res., 59: 4519-4524, 1999.
8. Tremblay, G. B., Kunath, T., Bergeron, D., Lapointe, L., Champigny, C., Bader, J. A., Rossant, J., and Giguere, V. Diethylstilbestrol regulates trophoblast stem cell differentiation as a ligand of orphan nuclear receptor ERRβ. Genes Dev., 15: 833-838, 2001.
9. Coward, P., Lee, D., Hull, M. V., and Lehmann, J. M. 4-Hydroxytamoxifen binds to and deactivates the estrogen-related receptor γ. Proc. Natl. Acad. Sci. USA, 98: 8880-8884, 2001.
10. Pike, A. C., Brzozowski, A. M., Hubbard, R. E., Bonn, T., Thorsell, A. G., Engstrom, O., Ljunggren, J., Gustafsson, J. A., and Carlquist, M. Structure of the ligand-binding domain of oestrogen receptor β in the presence of a partial agonist and a full antagonist. EMBO J., 18: 4608-4618, 1999.
11. SYBYL. 6.9 edition. St. Louis, MO: Tripos, Inc.
12. Pike, A. C., Brzozowski, A. M., Walton, J., Hubbard, R. E., Thorsell, A. G., Li, Y. L., Gustafsson, J. A., and Carlquist, M. Structural insights into the mode of action of a pure antiestrogen. Structure (Camb), 9: 145-153, 2001.
13. Shiau, A. K., Barstad, D., Loria, P. M., Cheng, L., Kushner, P. J., Agard, D. A., and Greene, G. L. The structural basis of estrogen receptor/coactivator recognition and the antagonism of this interaction by tamoxifen. Cell, 95: 927-937, 1998.
14. Gangloff, M., Ruff, M., Eiler, S., Duclaud, S., Wurtz, J. M., and Moras, D. Crystal structure of a mutant hERα ligand-binding domain reveals key structural features for the mechanism of partial agonism. J. Biol. Chem., 276: 15059-15065, 2001.
15. Tanenbaum, D. M., Wang, Y., Williams, S. P., and Sigler, P. B. Crystallographic comparison of the estrogen and progesterone receptor's ligand binding domains. Proc. Natl. Acad. Sci. USA, 95: 5998-6003, 1998.
16. Tremblay, G. B., Bergeron, D., and Giguere, V. 4-Hydroxytamoxifen is an isoform-specific inhibitor of orphan estrogen-receptor-related (ERR) nuclear receptors β and γ. Endocrinology, 142: 4572-4575, 2001.
17. Kraichely, D. M., Sun, J., Katzenellenbogen, J. A., and Katzenellenbogen, B. S. Conformational changes and coactivator recruitment by novel ligands for estrogen receptor-α and estrogen receptor-β: correlations with biological character and distinct differences among SRC coactivator family members. Endocrinology, 141: 3534-3545, 2000.
18. Wong, C. W., Komm, B., and Cheskis, B. J. Structure-function evaluation of ER α and β interplay with SRC family coactivators. ER selective ligands. Biochemistry, 40: 6756-6765, 2001.
19. Margeat, E., Bourdoncle, A., Margueron, R., Poujol, N., Cavailles, V., and Royer, C. Ligands differentially modulate the protein interactions of the human estrogen receptors α and β. J. Mol. Biol., 326: 77-92, 2003.
20. Schapira M, Abagyan R, and Totrov M. Nuclear hormone receptor targeted virtual screening. J. Med. Chem., 46: 3045-3059, 2003.
21. Wang, Z., Benoit, G., Liu, J., Prasad, S., Aarnisalo, P., Liu, X., Xu, H., Walker, N. P. and Perlmann, T. Structure and function of Nurr1 identifies a class of ligand-independent nuclear receptors. Nature, 423: 555-560, 2003.
22. Brzozowski, A. M., Pike, A. C., Dauter, D., Hubbard, R. E., Bonn, T., Engstrom, O., Ohman, L., Greene, G. L., Gustafsson, J. A., and Carlquist, M. Molecular basis of agonism and antagonism in the oestrogen receptor. Nature, 389: 753-758, 1997.
23. Anstead, G. M., Carlson, K. E., and Katzenellenbogen, J. A. The estradiol pharmacophore: ligand strucrure-estrogen receptor binding affinity relationships and a model for the receptor binding site. Steroids, 62: 268-303, 1997.
24. Anazi, E. A., Clark, G. M., and Mertz, J. E. Estrogen-related receptor α and estrogen-related receptor γ associate with unfavorable and favorable biomarkers, respectively, in human breast cancer. Cancer Res., 62: 6510-6518, 2002.
25. Bonnelye, E. and Aubin, J. E. Differential expression of estrogen receptor-related receptor γ and estrogen receptors α and β in osteoblasts in vivo and in vitro. J. Bone Miner. Res., 17: 1392-1400, 2002.
26. Bonnelye, E., Merdad, L., Kung, V., and Aubin, J. E. The orphan nuclear estrogen receptor-related receptor α((ERRα) is expressed throughout osteoblast differentiation and regulates bone formation in vitro. J. Cell Biol., 153: 971-983, 2001.
27. Zhou, D., Quach, K. M., Yang, C., Lee, S. Y., Pohajdak, B., and Chen, S. PNRC: a proline-rich nuclear receptor co-regulatory protein that modulates transcriptional activation of multiple nuclear receptors including orphan receptors SF1 and ERR alpha 1. Mol. Endocrinol., 14: 986-998, 2000.
28. Bernstein, F. C., Koetzle, T. F., Williams, G. J. B., Meyer, E. F., Brice, M. D., Rodgers, J. R., Kennard, O., Shimanouchi, T., and Tasumi, M. The Protein Data Bank: a computer-based archival file for macromolecular structures. J. Mol. Biol., 112: 535-542, 1977.
29. Srinivasan, N. and Blundell, T. L. An evaluation of the performance of an automated procedure for comparative modelling of protein tertiary structure. Protein Eng., 6: 501-512, 1993.
30. Rarey, M., Kramer, B., Lengauer, T., and Klebe, G. A fast flexible docking method using an incremental construction algorithm. J. Mol. Biol., 261: 470-489, 1996.
31. Kramer, B., Rarey, M., and Lengauer, T. Evaluation of the FLEXX incremental construction algorithm for protein-ligand docking. Proteins, 37: 228-241, 1999.