Skip to main content

Advertisement

SpringerLink
Log in

Promoter- and cell-specific responses to sex steroids

  • Published:
Osteoporosis International Aims and scope Submit manuscript

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

References

  1. King WJ, Greene GL. Monoclonal antibodies localize oestrogen receptor in the nuclei of target cells. Nature 1984;307:745–7.

    Google Scholar 

  2. Perrot-Applanat M, Logeat F, Groyer-Picard MT, Milgrom E. Immunocytochemical study of mammalian progesterone receptor using monoclonal antibodies. Endocrinology 1985;116:1473–84.

    Google Scholar 

  3. Welshons WV, Lieberman ME, Gorski J. Nuclear localization of unoccupied oestrogen receptors. Nature 1984;307:747–9.

    Google Scholar 

  4. Guiochon-Mantel A, Loosfelt H, Lescop P, et al. Mechanisms of nuclear localization of the progesterone receptor: evidence for interaction between monomers. Cell 1989;57:1147–54.

    Google Scholar 

  5. Guiochon-Mantel A, Lescop P, Christin-Maitre S, Loosfelt H, Perrot-Applanat M, Milgrom E. Nucleocytoplasmic shuttling of the progesterone receptor. EMBO J 1991;10:3851–9.

    Google Scholar 

  6. Madan AP, DeFranco DB. Bidirectional transport of glucocorticoid receptors across the nuclear envelope. Proc Natl Acad Sci USA 1993;90:3588–92.

    Google Scholar 

  7. Dauvois S, White R, Parker MG. The antiestrogen ICI182780 disrupts estrogen receptor nucleocytoplasmic shuttling. J Cell Sci 1993;106:1377–88.

    Google Scholar 

  8. Perrot-Applanat M, Lescop P, Milgrom E. The cytoskeleton and the cellular traffic of the progesterone receptor. J Cell Biol 1992;119:337–38.

    Google Scholar 

  9. Mandell RB, Feldherr CM. Identification of two hsp70-relatedXenopus oocyte proteins that are capable of recycling across the nuclear envelope. J Cell Biol 1990;111:1775–83.

    Google Scholar 

  10. Guiochon-Mantel A, Delabre K, Lescop P, Milgrom E. Nuclear localization signals also mediate the outward movement of proteins from the nucleus, Proc Natl Acad Sci USA 1994;91:7179–83.

    Google Scholar 

  11. Klein-Hitpass L, Cato ACB, Henderson D, Ryffel GU. Two types of antiprogestins identified by their differential action in transcriptionally active extracts from T47D cells. Nucleic Acids Res 1991 ;19:1227–34.

    Google Scholar 

  12. Delabre K, Guiochon-Mantel A, Milgrom E. In vivo evidence against the existence of antiprogestins disrupting receptor binding to DNA. Proc Natl Acad Sci USA 1993;90:4421–5.

    Google Scholar 

  13. Guiochon-Mantel A, Loosfelt H, Ragot T, et al. Receptors bound to antiprogestin form abortive complexes with hormone responsive elements. Nature 1988;336:695–8.

    Google Scholar 

  14. Milgrom E, Luu Thi MT, Atger M, Baulieu EE. Mechanisms regulating the concentration and the conformation of progesterone receptor(s) in the uterus. J Biol Chem 1973;248:6366–74.

    Google Scholar 

  15. Vu Hai MT, Logeat F, Warembourg M, Milgrom E. Hormonal control of progesterone receptors. Ann NY Acad Sci 1977;286:199–209.

    Google Scholar 

  16. Mester J, Baulieu EE. Progesterone receptors in the chicken oviduct. Eur J Biochem 1977;72:403–14.

    Google Scholar 

  17. Horwitz KB, McGuire WL. Oestrogen control of progesterone receptor in human breast cancer. J Biol Chem 1978;253:2223–8.

    Google Scholar 

  18. Garcia E, Bouchard P, De Brux J, et al. Use of immunocytochemistry of progesterone and estrogen receptors for endometrial dating. J Clin Endocrinol Metab 1988;67:80–7.

    Google Scholar 

  19. Chalbos D, Vignon F, Keydar I, Rochefort H. Estrogens stimulate cell proliferation and induce secretory proteins in a human breast cancer cell line (T47D). J Clin Endocrinol Metab 1982;55:276–83.

    Google Scholar 

  20. Prud'homme JF, Fridlansky F, Le Cunff M, et al. Cloning of a gene expressed in human breast cancer and regulated by estrogen in MCF-7 cells. DNA 1985;4:11–21.

    Google Scholar 

  21. Savouret JF, Bailly A, Misrahi M, et al. Characterization of the hormone responsive element involved in the regulation of the progesterone receptor gene. EMBO J 1991;10:1875–83.

    Google Scholar 

  22. 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 1990;9:2811–8.

    Google Scholar 

  23. Savouret JF, Rauch M, Redeuilh G, et al. Interplay between estrogens, progestins, retinoic acid and AP-1 on a single regulatory site in the progesterone receptor gene. J Biol Chem 1994;269:28955–62.

    Google Scholar 

  24. Onate SA, Tsai SY, Tsai MJ, O'Malley BW. Sequence and characterization of a coactivator for the steroid hormone receptor superfamily. Science 1995;270:1354–7.

    Google Scholar 

  25. Cavaillès V, Dauvois S, Danielian PS, Parker MG. Interaction of proteins with transcriptionally active estrogen receptor. Proc Natl Acad Sci USA 1994;91:10009–13.

    Google Scholar 

  26. Voegel JJ, Heine MJS, Zechel C, Chambon P, Gronemeyer H. TIF2, a 160 kDa transcriptional mediator for the ligand-dependent activation function AF-2 of nuclear receptors. EMBO J 1996;15:3667–75.

    Google Scholar 

  27. Halachmi S, Marden E, Martin G, Mackay H, Abbondanza C, Brown M. Estrogen receptor-associated proteins: possible mediators of hormone-induced transcription. Science 1994, 264:1455–8

    Google Scholar 

  28. Kamei Y, Xu L, Heinzel T, et al. A CBP integrator complex mediates transcriptional activation and AP-1 inhibition by nuclear receptors. Cell 1996;85:403–14.

    Google Scholar 

  29. Hörlein AJ, Näär AM, Heinzel T, et al. Ligand-independent repression by the thyroid hormone receptor mediated by a nuclear receptor co-repressor. Nature 1995;377:397–404.

    Google Scholar 

  30. Chen JD, Evans RM. A transcriptional co-repressor that interacts with nuclear hormone receptors. Nature 1995;377:454–7.

    Google Scholar 

  31. Cavaillès V, Dauvois S, L'Horset F, et al. Nuclear factor RIP140 modulates transcriptional activation by the estrogen receptor. EMBO J 1995;14:3741–51.

    Google Scholar 

  32. Le Douarin B, Zechel C, Gamier JM, et al. The N-terminal, part of TIF1, a putative mediator of the ligand-dependent activation function (AF-2) of nuclear receptors, is fused to B-raf in the oncogenic protein T18. EMBO J 1995;14:2020–33.

    Google Scholar 

  33. vom Baur E, Zechel C, Heery D, et al. Differential ligand-dependent interactions between the AF-2 activating domain of nuclear receptors and the putative transcriptional intermediary factors mSUGl and TIF1. EMBO J 1996;15:110–24.

    Google Scholar 

  34. Lee JW, Ryan F, Swaffield JC, Johnston SA, Moore DD. Interaction of thyroid-hormone receptor with a conserved transcriptional mediator. Nature 1995;374:91–4.

    Google Scholar 

  35. Guiochon-Mantel A, Savouret JF, Quignon F, Delabre K, Milgrom E, de Thé H. Effect of PML and PML-RAR on the transactivation properties and subcellular distribution of steroid hormone receptors. Mol Endocrinol 1995;9:1791–803.

    Google Scholar 

  36. Imhof MO, McDonnell DP. Yeast RSP5 and its human homolog hRPFl potentiate hormone-dependent activation of transactivation by human progesterone and glucocorticoid receptors. Mol Cell Biol 1996;16:2594–605.

    Google Scholar 

  37. de Thé H, Chomienne C, Lanotte M, Degos L, Dejean A. The t(15;17) translocation of acute promyelocytic leukaemia fuses the retinoic acid receptor gene to a novel transcribed locus. Nature 1990;347:558–61.

    Google Scholar 

  38. Muchardt C, Yaniv M. A human homologue ofSaccharomyces cerevisiae SNF2/SWI2 andDrosophila brm genes potentiates transcriptional activation by the glucocorticoid receptor. EMBO J 1993;12:4279–90.

    Google Scholar 

  39. Yoshinaga SK, Peterson CL, Herskowitz I, Yamamoto KR. Roles of SWI1, SWI2, and SWI3. Proteins for transcriptional enhancement by steroid receptors. Science 1992;258:1598–604.

    Google Scholar 

  40. Struhl K. Chromatin structure and RNA polymerase II connection: implications for transcription. Cell 1996;84:179–82.

    Google Scholar 

Download references

Author information

Authors and Affiliations

  1. INSERM U135, Hôpital de Bicêtre, 78 rue du Général Leclerc, F-94295, Le Kremlin Bicetre, France

    E. Milgrom, J. F. Savouret, A. Mantel, M. Perrot-Applanat, K. Delabre & P. Lescop

Authors
  1. E. Milgrom
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. J. F. Savouret
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. A. Mantel
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. M. Perrot-Applanat
    View author publications

    You can also search for this author in PubMed Google Scholar

  5. K. Delabre
    View author publications

    You can also search for this author in PubMed Google Scholar

  6. P. Lescop
    View author publications

    You can also search for this author in PubMed Google Scholar

Rights and permissions

Reprints and permissions

About this article

Cite this article

Milgrom, E., Savouret, J.F., Mantel, A. et al. Promoter- and cell-specific responses to sex steroids. Osteoporosis Int 7 (Suppl 1), 23–28 (1997). https://doi.org/10.1007/BF01674809

Download citation

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF01674809

Keywords

Search

Navigation