Two antiestrogens affect differently chromatin remodeling of trefoil factor 1 (pS2) gene and the fate of estrogen receptor in MCF7 cells

Biochimica et Biophysica Acta - Gene Structure and Expression

Volumn 1578, Issue 1-3, 2002, Pages 12-20

  Giamarchi, Claire ^a,b   Chailleux, Catherine ^a   Calligé, Mathide ^a   Rochaix, Philippe ^b   Trouche, Didier ^a   Richard Foy, Hélène ^a  

^a CNRS   (France)

^b INSERM   (France)

Author keywords

Antiestrogen; Breast cancer; Chromatin; Estrogen receptor ; pS2 gene

Indexed keywords

4 HYDROXYTAMOXIFEN; ANTIESTROGEN; DEOXYRIBONUCLEASE I; ESTROGEN RECEPTOR; ESTROGEN RECEPTOR ALPHA; ESTROGEN RECEPTOR BETA; FULVESTRANT; PROTEIN PS2; TREFOIL PEPTIDE;

ARTICLE; CELL NUCLEUS; CELL STRAIN MCF 7; CHROMATIN; CONTROLLED STUDY; DRUG EFFECT; DRUG MECHANISM; GENE STRUCTURE; GENETIC TRANSCRIPTION; HUMAN; HUMAN CELL; HUMAN TISSUE; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN TRANSPORT; TRANSCRIPTION REGULATION;

BLOTTING, WESTERN; CELL NUCLEUS; CHROMATIN; DEOXYRIBONUCLEASE I; ESTRADIOL; ESTROGEN ANTAGONISTS; ESTROGEN RECEPTOR ALPHA; GENE EXPRESSION REGULATION; HUMANS; IMMUNOHISTOCHEMISTRY; NEOPLASMS, HORMONE-DEPENDENT; PROMOTER REGIONS (GENETICS); PROTEINS; RECEPTORS, ESTROGEN; SELECTIVE ESTROGEN RECEPTOR MODULATORS; TAMOXIFEN; TIME FACTORS; TUMOR CELLS, CULTURED; TUMOR SUPPRESSOR PROTEINS;

LOTUS;

EID: 0037064199     PISSN: 01674781     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4781(02)00480-3     Document Type: Article

References (24)

1. Glass C.K., Rose D.W., Rosenfeld M.G. Nuclear receptor coactivators. Curr. Opin. Cell Biol. 9:1997;222-232.
2. Torchia J., Rose D.W., Inostroza J., Kamei Y., Westin S., Glass C.K., Rosenfeld M.G. The transcriptional co-activator p/CIP binds CBP and mediates nuclear-receptor function. Nature. 387:1997;677-684.
3. Jordan V.C. Biochemical pharmacology of antiestrogen action. Pharmacol. Rev. 36:1984;245-276.
4. Thompson E.W., Katz D., Shima T.B., Wakeling A.E., Lippman M.E., Dickson R.B. ICI 164 384, a pure antagonist of estrogen-stimulated MCF-7 cell proliferation and invasiveness. Cancer Res. 49:1989;6929-6934.
5. Wakeling A.E., Dukes M., Bowler J. A potent specific pure antiestrogen with clinical potential. Cancer Res. 51:1991;3867-3873.
6. Brzozowski A.M., Pike A.C., Dauter Z., Hubbard R.E., Bonn T., Engstrom O., Ohman L., Greene G.L., Gustafsson J.A., Carlquist M. Molecular basis of agonism and antagonism in the oestrogen receptor. Nature. 389:1997;753-758.
7. Berry M., Metzger D., Chambon P. Role of the two activating domains of the oestrogen receptor in the cell-type and promoter-context dependent agonistic activity of the anti-oestrogen 4-hydroxytamoxifen. EMBO J. 9:1990;2811-2818.
8. Dauvois S., Danielian P.S., White R., Parker M.G. Antiestrogen ICI 164 384 reduces cellular estrogen receptor content by increasing its turnover. Proc. Natl. Acad. Sci. U. S. A. 89:1992;4037-4041.
9. Dauvois S., White R., Parker M.G. The antiestrogen ICI 182 780 disrupts estrogen receptor nucleocytoplasmic shuttling. J. Cell Sci. 106:1993;1377-1388.
10. Berry M., Nunez A.M., Chambon P. Estrogen-responsive element of the human pS2 gene is an imperfectly palindromic sequence. Proc. Natl. Acad. Sci. U. S. A. 86:1989;1218-1222.
11. Sewack G.F., Hansen U. Nucleosome positioning and transcription-associated chromatin alterations on the human estrogen-responsive pS2 promoter. J. Biol. Chem. 272:1997;31118-31129.
12. Giamarchi C., Solanas M., Chailleux C., Augereau P., Vignon F., Rochefort H., Richard-Foy H. Chromatin structure of the regulatory regions of pS2 and cathepsin D genes in hormone-dependent and -independent breast cancer cell lines. Oncogene. 18:1999;533-541.
13. Wijayaratne A.L., Nagel S.C., Paige L.A., Christensen D.J., Norris J.D., Fowlkes D.M., McDonnell D.P. Comparative analyses of mechanistic differences among antiestrogens. Endocrinology. 140:1999;5828-5840.
14. Richard-Foy H., Sistare F.D., Riegel A.T., Simons S.S. Jr., Hager G.L. Mechanism of dexamethasone 21-mesylate antiglucocorticoid action: II. Receptor-antiglucocorticoid complexes do not interact productively with mouse mammary tumor virus long-terminal repeat chromatin. Mol. Endocrinol. 1:1987;659-665.
15. Schaffner W., Weissmann C. A rapid, sensitive, and specific method for the determination of protein in dilute solution. Anal. Biochem. 56:1973;502-514.
16. Stenoien D.L., Mancini M.G., Patel K., Allegretto E.A., Smith C.L., Mancini M.A. Subnuclear trafficking of estrogen receptor-alpha and steroid receptor coactivator-1. Mol. Endocrinol. 14:2000;518-534.
17. Sabbah M., Gouilleux F., Sola B., Redeuilh G., Baulieu E.E. Structural differences between the hormone and antihormone estrogen receptor complexes bound to the hormone response element. Proc. Natl. Acad. Sci. U. S. A. 88:1991;390-394.
18. Nawaz Z., Lonard D.M., Dennis A.P., Smith C.L., O'Malley B.W. Proteasome-dependent degradation of the human estrogen receptor. Proc. Natl. Acad. Sci. U. S. A. 96:1999;1858-1862.
19. Chalbos D., Philips A., Galtier F., Rochefort H. Synthetic antiestrogens modulate induction of pS2 and cathepsin-D messenger ribonucleic acid by growth factors and adenosine 3′,5′-monophosphate in MCF7 cells. Endocrinology. 133:1993;571-576.
20. Chun T.Y., Gregg D., Sarkar D.K., Gorski J. Differential regulation by estrogens of growth and prolactin synthesis in pituitary cells suggests that only a small pool of estrogen receptors is required for growth. Proc. Natl. Acad. Sci. U. S. A. 95:1998;2325-2330.
21. Devin-Leclerc J., Meng X., Delahaye F., Leclerc P., Baulieu E.E., Catelli M.G. Interaction and dissociation by ligands of estrogen receptor and Hsp90: the antiestrogen RU 58668 induces a protein synthesis-dependent clustering of the receptor in the cytoplasm. Mol. Endocrinol. 12:1998;842-854.
22. Wijayaratne A.L., McDonnell D.P. The human estrogen receptor-alpha is a ubiquitinated protein whose stability is affected differentially by agonists, antagonists, and selective estrogen receptor modulators. J. Biol. Chem. 276:2001;35684-35692.
23. Lonard D.M., Nawaz Z., Smith C.L., O'Malley B.W. The 26S proteasome is required for estrogen receptor-alpha and coactivator turnover and for efficient estrogen receptor-alpha transactivation. Mol. Cell. 5:2000;939-948.
24. Lavinsky R.M., Jepsen K., Heinzel T., Torchia J., Mullen T.M., Schiff R., Del-Rio A.L., Ricote M., Ngo S., Gemsch J., Hilsenbeck S.G., Osborne C.K., Glass C.K., Rosenfeld M.G., Rose D.W. Diverse signaling pathways modulate nuclear receptor recruitment of N-CoR and SMRT complexes. Proc. Natl. Acad. Sci. U. S. A. 95:1998;2920-2925.