Skip to main content
SpringerLink
Log in

Progesterone-Modulation of Estrogen Action: Rapid Down Regulation of Nuclear Acceptor Sites for the Estrogen Receptor

  • Chapter
Cell and Molecular Biology of the Uterus

Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 230))

Summary

Our previous studies demonstrated that progesterone down regulates the occupied form of nuclear estrogen receptor (Re). Using the density shift method, we discovered that progestins stimulate the turnover of nuclear Re within 3 h of treatment, and Re synthesis is suppressed subsequently. Thus, the primary site of progestin action in down-regulating Re is the stimulation of nuclear Re turnover followed by the inhibition of Re replenishment. A major breakthrough in our understanding of how progestin controls Re turnover was made by studying nuclear acceptor sites for Re that were found to decrease markedly within 2 h of progestin treatment. These and other results indicate that progestin induces a factor called the Re regulatory factor (ReRF) which acts to block nuclear Re acceptor sites, and this in turn decreases nuclear Re retention on chromatin acceptor sites, leading to an enhanced turnover (or processing) of nuclear Re.

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

Access this chapter

Log in via an institution
Chapter
USD 29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 84.99
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD 109.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. W. W. Leavitt, R. G. MacDonald, and W. C. Okulicz, Hormonal regulation of estrogen and progesterone receptor systems, in: “Biochemical Actions of Hormones,” Vol. 10, G. Litwack, ed., Academic Press, New York, pp. 323–356 (1983).

    Google Scholar 

  2. W. W. Leavitt, Progesterone regulation of nuclear estrogen receptors: Evidence for a receptor regulatory factor, in: “Molecular Mechanism of Steroid Hormone Action,” V. K. Moudgil, ed., Walter de Gruyter & Co., Berlin, pp. 437–470 (1985).

    Chapter  Google Scholar 

  3. K. H. Horwitz, L. L. Wei, S. M. Selacek, and C. N. D’Arville, Progestin action and progesterone receptor structure in human breast cancer: A review,Rec. Prog. Horm. Res. 41: 249–316 (1985).

    PubMed  CAS  Google Scholar 

  4. G. L. Greene, Application of immunochemical techniques to the analysis of estrogen receptor structure and function, in: “Biochemical Actions of Hormones,” Vol. 11, G. Litwack, ed., Academic Press, New York, pp. 207–239 (1984).

    Google Scholar 

  5. W. W. Leavitt, R. W. Evans, and W. J. Hendry III, Etiology of DES-induced uterine tumors in the Syrian hamster, in: “Hormones and Cancer,” W. W. Leavitt, ed., Plenum Publ. Corp., New York, pp. 63–86 (1982).

    Google Scholar 

  6. W. W. Leavitt, R. W. Evans, W. J. Hendry III, and K. I, H. Williams, Antiestrogen and progestin action in DES-induced endometrial abnormalities in the Syrian hamster, in: “Nonsteroidal Antioestrogens. Molecular Pharmacology and Antitumour Activity,” R. L. Sutherland and V. C. Jordan, eds., Academic Press, Sydney, pp. 167–176 (1981).

    Google Scholar 

  7. J. Gorski, W. Welshons, and D. Sakai, Remodeling the estrogen receptor model, Mol. Cell. Endocrinol. 36: 11–15 (1984).

    Article  CAS  Google Scholar 

  8. W. W. Grody, W. T. Schrader, and B. W. O’Malley, Activation, transformation, and subunit structure of steroid hormone receptors, Endocrine Rev. 3: 141–163 (1982).

    Article  CAS  Google Scholar 

  9. M. R. Sherman and J. Stevens, Structure of mammalian steroid receptors: evolving concepts and methodological developments, Physiol. Rev. 46: 83–105 (1984).

    Article  CAS  Google Scholar 

  10. T. C. Spelsberg, B. A. Littlefield, R. Seelke, G. Martin-Dani, H. Toyoda, P. Boyd-Leinen, C. Thrall, and O. L. Kon, Role of specific chromosomal proteins and DNA sequences in the nuclear binding sites for steroid receptors, Rec. Prog. Horm. Res. 39: 463–517 (1983).

    Google Scholar 

  11. W. C. Okulicz, R. A. Boomsma, R. G. MacDonald, and W. W. Leavitt, Conditions for the measurement of nuclear estrogen receptor at low temperature, Biochim. Biophys. Acta 757: 128–136 (1983).

    Article  PubMed  CAS  Google Scholar 

  12. T. J. Chen and W. W. Leavitt, Nuclear progesterone receptor in the hamster uterus: Measurement by [3H]-progesterone exchange during the estrous cycle, Endocrinology104: 1588–1597 (1979).

    Article  PubMed  CAS  Google Scholar 

  13. J. N. Anderson, E. J. Peck, Jr., and J. H. Clark, Nuclear receptor-estradiol complex: a requirement for uterotrophic responses, Endocrinology95: 174–178 (1974).

    Article  PubMed  CAS  Google Scholar 

  14. J. N. Anderson, E. J. Peck, Jr., and J. H. Clark, Estrogen-induced uterine responses and growth: relationship to receptor estrogen binding by uterine nuclei, Endocrinology 96: 160–167 (1975).

    Article  PubMed  CAS  Google Scholar 

  15. B. W. O’Mailey, D. R. Roop, E. C. Lai, J. L. Nordstrom, J, F. Catterall, G. E. Swaneck, D. A. Colbert, M. J. Tsai, A. Dugaiczyk, and S. L. C. Woo, The ovalbumin gene: Organization, structure, transcription, and regulation, Rec. Prog. Horm. Res. 35: 1–46 (1979).

    Google Scholar 

  16. W. W. Leavitt, J. M. Burns, and A. Alecozay, Oxytocin receptors: An overview, in: “Peptide Hormone Receptors,” M. Kalimi and C. Hubbard, eds., Walter de Gruyter and Co., Berlin, pp. 615–638 (1987).

    Google Scholar 

  17. R. S. Chuknyiska and G. S. Roth, Decreased estrogenic stimulation of RNA polymerase II in aged rat uteri is apparently due to reduced nuclear binding of receptor-estradiol complexes, J. Biol. Chem. 260: 8661–8663 (1985).

    PubMed  CAS  Google Scholar 

  18. W. W. Leavitt, Gene regulation by progesterone, in: “Handbook on Receptor Research,” F. Auricchio, ed., Field Educational Italia Acta Medica, Rome, pp. 179–209 (1985).

    Google Scholar 

  19. R. W. Evans, T. J. Chen, W. J. Hendry III, and W. W. Leavitt, Progesterone regulation of estrogen receptor in the hamster uterus during the estrous cycle, Endocrinology107: 383–390 (1980).

    Article  PubMed  CAS  Google Scholar 

  20. W. C. Okulicz, R. W. Evans, and W. W. Leavitt, Progesterone regulation of the occupied nuclear estrogen receptor, Science 213: 1503–1505 (1981).

    Article  PubMed  CAS  Google Scholar 

  21. W. W. Leavitt and W. C. Okulicz, Occupied and unoccupied estrogen receptor during the estrous cycle and pregnancy, Am. J. Physiol. 249: E589–E594 (1985).

    PubMed  CAS  Google Scholar 

  22. R. W. Evans and W. W. Leavitt, Progesterone inhibition of uterine nuclear estrogen receptor: dependence on RNA and protein synthesis, Proc. Natl. Acad. Sci. (USA) 77: 5856–5860 (1980).

    Article  CAS  Google Scholar 

  23. W. W. Leavitt, Hormonal regulation of myometrial estrogen, progesterone and oxytocin receptors in the pregnant and pseudopregnant hamster, Endocrinology116: 1079–1084 (1985).

    Article  PubMed  CAS  Google Scholar 

  24. W. W. Leavitt, R. G. MacDonald, and G. T. Shwaery, Characterization of deciduoma marker proteins in hamster uterus: Detection in decidual cell cultures, Biol. Reprod. 32: 631–643 (1985).

    Article  PubMed  CAS  Google Scholar 

  25. W. W. Leavitt and A. Takeda, Hormonal regulation of estrogen and progesterone receptors in hamster decidual cells, Biol. Reprod. 35: 475–484 (1986).

    Article  PubMed  CAS  Google Scholar 

  26. W. W. Leavitt, A. Takeda, and R. G. MacDonald, Progesterone regulation of protein synthesis and steroid receptor levels in decidual cells, Ann. N. Y. Acad. Sci. 476: 136–157 (1986).

    Article  PubMed  CAS  Google Scholar 

  27. A. Bachmoir, D. Finley, and A. Varshovsky, In vivo half life of a protein is a function of its amino-terminal residue, Science 234:179–186 (1986).

    Google Scholar 

  28. S. Rogers, R. Wells, and M. Rechsteiner, Amino acid sequences common to rapidly degraded proteins: the PEST hypothesis, Science 234: 364–368 (1986).

    Article  PubMed  CAS  Google Scholar 

  29. G. L. Greene, P. Gilna, M. Waterfield, A. Baker, Y. Hort, and J. Shine, Sequence and expression of human estrogen receptor complementary DNA, Science 231: 1150–1154 (1986).

    Article  PubMed  CAS  Google Scholar 

  30. S. Green, P. Walter, V. Kumar, A. Krust, J. M. Barnert, P. Argus, and P. Chambon, Human oestrogen receptor cDNA: sequence, expression and homology of v-erb-A, Nature 320: 134–139 (1986).

    Article  PubMed  CAS  Google Scholar 

  31. J. H. Clark, A. J. W. Hseuh, and E. J. Peck, Jr., Regulation of estrogen receptor replenishment by progesterone, Ann. N. Y. Acad. Sci. 286: 161–178 (1977).

    Article  PubMed  CAS  Google Scholar 

  32. W. W. Leavitt, W. C. Okulicz, J. A. McCracken, W. Schramm, and W. F. Robidoux, Rapid recovery of nuclear estrogen receptor and oxytocin receptor in the ovine uterus following progesterone withdrawal, J. Steroid Biochem. 22: 687–691 (1985).

    Article  PubMed  CAS  Google Scholar 

  33. W. C. Okulicz, R. W. Evans, and W. W. Leavitt, Progesterone regulation of estrogen receptor in the rat uterus. A primary inhibitory influence on the nuclear fraction, Steroids 37: 463–470 (1981).

    Article  PubMed  CAS  Google Scholar 

  34. A. Takeda and W. W. Leavitt, Progestin-induced down regulation of nuclear estrogen receptor in uterine decidual cells: Analysis of receptor synthesis and turnover by the density-shift method, Biochem. Biophys. Res. Comm. 135: 98–104 (1986).

    Article  PubMed  CAS  Google Scholar 

  35. A. Takeda and W. W. Leavitt, Progestin antagonizes estrogen action in T47D human breast cancer cells by shortening the half life of nuclear estrogen receptor, J. Cell Biol. 101: 347a (abstr.) (1985).

    Google Scholar 

  36. A. Takeda and W. W. Leavitt, Temporal effects of progesterone domination on estrogen and oxytocin receptors in hamster uterus, J. Steroid Biochem. 25: 219–224 (1986).

    Article  PubMed  CAS  Google Scholar 

  37. T. G. Muldoon, Regulation of steroid hormone receptor activity, Endocrine Rev. 1: 339–364 (1980).

    Article  CAS  Google Scholar 

  38. E. J. Smanick, H. K. Young, T. G. Muldoon, and V. B. Mahesh, Analysis of the effect of progesterone in vivo on estrogen receptor distribution in the rat anterior pituitary and hypothalamus, Endocrinology113: 15–22 (1983).

    Article  Google Scholar 

  39. J. J. Calderon, T. G. Muldoon, and V. B. Mahesh, Receptor-mediated interrelationships between progesterone and estradiol action on the anterior pituitary-hypothalamic axis of the ovariectomized immature rat, Endocrinology120: 2428–2435 (1987).

    Article  PubMed  CAS  Google Scholar 

  40. P. M. Wise and P. Camp, Changes in concentrations of estradiol nuclear receptors in the preoptic area, medial basal hypothalamus, amygdala, and pituitary gland of middle-aged and old cycling rats, Endocrinology114: 92–98 (1984).

    Article  PubMed  CAS  Google Scholar 

  41. M. McClellan, N. B. West, and R. M. Brenner, Immunocytochemical localization of estrogen receptors in the macaque endometrium during the luteal-follicular transition, Endocrinology119: 2467–2475 (1986).

    Article  PubMed  CAS  Google Scholar 

  42. E. R. Mulvihill and R. D. Palmiter, Relationship of nuclear estrogen receptor levels to induction of ovalbumin and conalbumin mRNA in chick oviduct, J. Biol. Chem. 252: 2060–2068 (1977).

    PubMed  CAS  Google Scholar 

  43. B. W. O’Mailey, M. J. Tsai, and W. T. Schrader, Structural considerations for the action of steroid hormones in eucaryotic cells, in: “Steroid Hormone Receptors,” H. Ericksson and J. Gustafsson, eds., Elsevier Sci. Pub., New York, pp. 307–328 (1983).

    Google Scholar 

  44. K. Yamamoto and B. M. Alberts, Steroid receptors: Elements for modulation of eukaryotic transcription, Ann. Rev. Biochem. 43: 721–746 (1976).

    Article  Google Scholar 

  45. K. B. Horwitz and W. L. McGuire, Nuclear mechanisms of estrogen action: Effects of estradiol and anti-estrogens on estrogen receptors in nuclear processing, J. Biol. Chem. 253: 8185–8191 (1978).

    PubMed  CAS  Google Scholar 

  46. R. L. Eckert, A. Mullick, E. A. Rorke, and B. S. Katzenellenbogen, Estrogen receptor synthesis and turnover in MCF-7 breast cancer cells measured by a density shift technique, Endocrinology114: 629–637 (1984).

    Article  PubMed  CAS  Google Scholar 

  47. W. C. Okulicz, R. G. MacDonald, and W. W. Leavitt, Progesterone-induced estrogen receptor-regulatory factor in hamster uterine nuclei: Preliminary characterization in a cell-free system, Endocrinology109: 2273–2275 (1981).

    Article  PubMed  CAS  Google Scholar 

  48. R. G. MacDonald, W. C. Okulicz, and W. W. Leavitt, Progesterone-induced inactivation of nuclear estrogen receptor in hamster uterus is mediated by acid phosphatase, Biochem. Biophy. Res. Comm. 104: 570–576 (1982).

    Article  CAS  Google Scholar 

  49. R. G. MacDonald, S. P. Rosenberg, arid W. W. Leavitt, Localization of estrogen receptor-regulatory factor in the uterine nucleus, Mol. Cell. Endocrinol. 32: 301–313 (1983).

    Article  CAS  Google Scholar 

  50. A. Cobb and W. W. Leavitt, Progesterone rapidly decreases the number of chromatin binding sites for nuclear estrogen receptor in the mammalian uterus, J. Cell. Biol. 101: 202a (abstr.) (1985).

    Google Scholar 

  51. K. B. Horwitz and W. L. McGuire, Actinomyocin D prevents nuclear processing of estrogen receptor, J. Biol. Chem. 253: 6319–6322 (1978).

    PubMed  CAS  Google Scholar 

  52. K. B. Horwitz and W. L. McGuire, Nuclear estrogen receptors. Effects of inhibitors on processing and steady state levels, J. Biol. Chem. 255: 9699–9705 (1980).

    PubMed  CAS  Google Scholar 

  53. V. G. Jordan, L. Rowsby, C. J. Dix, and G. Prestwick, Dose-related effects of nonsteroidal antiestrogens and oestrogens on the measurement of cytoplasmic estrogen receptors in the rat and mouse uterus, J. Endocrinol. 78: 71–81 (1978).

    Article  PubMed  CAS  Google Scholar 

  54. B. S. Katzenellenbogen, J. A. Katzenellenbogen, E. R. Ferguson, and N. Krauthammer, Antiestrogen interaction with uterine estrogen receptors. Studies with a radiolabeled antiestrogen (CI628), J. Biol. Chem. 253: 697–707 (1978).

    PubMed  CAS  Google Scholar 

  55. B. M. Raaka, M. Finnerty, E. Sun, and H. H. Samuels, Effects of molybdate on steroid receptors in intact GH1 cells: Evidence for dissociation of an intracellular 10S receptor oligomer prior to nuclear accumulation, J. Biol. Chem. 260: 14009–14015 (1985).

    PubMed  CAS  Google Scholar 

  56. M. F. Ruh and T. S. Ruh, Analysis of two forms of the molybdate-stabilized estrogen receptor, Endocrinology115: 1341–1349 (1984).

    Article  PubMed  CAS  Google Scholar 

  57. R. E. Muller, A. M. Traish, and H. H. Wotiz, Estrogen receptor activation precedes transformation, J. Biol. Chem. 258: 9227–9236 (1983).

    PubMed  CAS  Google Scholar 

  58. E. Milgrom, Activation of steroid receptor complexes, in: “Biochemical Actions of Hormones,” G. Litwack, ed., Academic Press, New York, Vol. 8, pp. 465–492 (1981).

    Google Scholar 

  59. A. Migliaccio, S. Lastoria, B. Moncharmont, A. Rotondi, and F. Auricchio, Phosphorylation of calf uterus, estradiol receptor by endogenous Ca-H— stimulated kinase activating the hormone binding of the receptor, Biochem. Biophys. Res. Comm. 109: 1002–1010 (1982).

    Article  CAS  Google Scholar 

  60. A. Migliaccio, A. Rotondi, and F. Auricchio, Calmodulin-stimulated phosphorylation of 176-estradiol receptor on tyrosine, Proc. Natl. Acad. Sci. (USA) 81: 5921–5925 (1984).

    Article  CAS  Google Scholar 

  61. F. Auricchio, A. Migliaccio, and A. Rotondi, Inactivation of oestrogen receptor in vitro by nuclear dephosphorylation, Biochem. J. 194: 569–574 (1981).

    PubMed  CAS  Google Scholar 

  62. F. Auricchio, A. Migliaccio, G. Castoria, S. Lastoria, and E, Schiavone, ATP-dependent enzyme activating hormone binding of estradiol receptor, Biochem. Biophys. Res. Comm. 101: 1171–1178 (1981).

    CAS  Google Scholar 

  63. V. K. Moudgil and T. E. Eessalu, Activation of estradiol-receptor complex by ATP in vitro, FEES Letters 122: 189–192 (1980).

    Article  CAS  Google Scholar 

  64. H. Fleming, R. Blumenthal, and E. Gurpide, Effects of cyclic nucleotides on estradiol binding in human endometrium, Endocrinology111: 1671–1677 (1982).

    Article  PubMed  CAS  Google Scholar 

  65. F. J. Monsma, Jr., B. S. Katzenellenbogen, M. A. Miller, Y. S. Ziegler, and J. A. Katzenellenbogen, Characterization of the estrogen receptor and its dynamics in MCF-7 human breast cancer cells using a covalently attaching antiestrogen, Endocrinology115: 143–153 (1984).

    Article  PubMed  CAS  Google Scholar 

  66. A. Kasid, K. Huff, G. L. Greene, and M. E. Lippman, A novel nuclear form of estradiol receptor in MCF-7 human breast cancer cells, Science 225: 1162–1165 (1984).

    Article  PubMed  CAS  Google Scholar 

  67. R. Jakesz, A. Kasid, G. Greene, and M. E. Lippman, Characteristics of different cytoplasmic and nuclear estrogen receptors appearing with continuous hormonal exposure, J. Biol. Chem. 258: 11807–11813 (1983).

    PubMed  CAS  Google Scholar 

  68. D. Sakai and J. Gorski, Estrogen receptor transformation to a high-affinity state without subunit-subunit interactions, J. Biochemistry 23: 3541–3547 (1984).

    Article  CAS  Google Scholar 

  69. A. C. Notides, S. Susson, and S. Callison, An allosteric regulatory mechanism for estrogen receptor activation, in: “Molecular Mechanisms of Steroid Hormone Action,” V. K. Moudgil, ed., Walter de Gruyter & Co., New York, pp. 173–197 (1985).

    Google Scholar 

  70. T. S. Ruh and T. C. Spelsberg, Acceptor sites for the oestrogen receptor in hen oviduct chromatin, Biochem. J. 210: 905–912 (1983).

    PubMed  CAS  Google Scholar 

  71. C. A. Campen and J. Gorski, Anomalous behavior of protein synthesis inhibitors on the turnover of the estrogen receptor as measured by density labeling, Endocrinology119: 1454–1461 (1986).

    Article  PubMed  CAS  Google Scholar 

  72. J. R. Pasqualini, C. Cosquer-Clavreul, G. Vidali, and V. G. Allfrcy, Effects of estradiol on the acetylation of histones in the fetal uterus of the guinea pig, Biol. Reprod. 25: 1035–1039 (1981).

    Article  PubMed  CAS  Google Scholar 

  73. P. R. Libby, Histone acetylation and hormone action: Early effects of oestradiol 173 on histone acetylation in rat uterus, Biochem. J. 130: 663–669 (1972).

    PubMed  CAS  Google Scholar 

  74. M. E. Cohen and T. H. Hamilton, Effect of estradiol-17g on the synthesis of specific uterine nonhistone chromosomal proteins, Proc. Natl. Acad. Sci. USA 72: 4346–4350 (1975).

    Article  PubMed  CAS  Google Scholar 

  75. K. L. Barker, Estrogen-induced synthesis of histones and a specific nonhistone protein in the uterus, Biochemistry 10: 284–291 (1981).

    Article  Google Scholar 

  76. M. J. Horton and C. M. Szego, Chromatin proteins of rat preputial-gland: Acute changes in response to estrogen, Int. J. Biochem. 16: 447–460 (1984).

    Article  PubMed  CAS  Google Scholar 

  77. S. Gilmour, The role of acidic proteins in gene regulation, in: “Acidic Proteins of the Nucleus,” I. L. Cameron and J. R. Jeter, Jr., eds., Academic Press, New York, pp. 297–316 (1981).

    Google Scholar 

  78. R. K. Keller, S. H. Socher, J. F. Krall, T. Chandra, and B. W. O’Malley, Fractionation of chick oviduct chromatin:IV. Association of protein kinase with transcriptionally active chromatin, Biochem. Biophys. Res. Comm. 66: 453–459 (1975).

    Article  PubMed  CAS  Google Scholar 

  79. P. Chambon, A. Dierich, M. Gaub, S. Jokowler, J. Jongstra, A. Krust, J. LePennec, P. Oudet, and T. Reudelhuber, Promoter elements of genes coding for proteins and modulation of transcription by estrogen and progesterone, Rec. Prog. Horm. Res. 40: 1–42 (1984).

    Google Scholar 

  80. E. R. Barrack and D. S. Coffey, The specific binding of estrogens and androgens to the nuclear matrix of sex hormone responsive tissues, J. Biol. Chem. 255: 7265–7275 (1980).

    PubMed  CAS  Google Scholar 

  81. J. B. E. Burch and H. Weintraub, Temporal order of chromatin structural changes associated with activation of the major chicken vitellogenin gene, Cell 33: 65–76 (1983).

    Article  PubMed  CAS  Google Scholar 

  82. R. Renkawitz, G. Schutz, D. von der Ahe, and M. Beato, Sequences in the promoter region of the chicken lysozyme gene required for steroid regulation and receptor binding, Cell 37: 503–510 (1984).

    Article  PubMed  CAS  Google Scholar 

  83. D. von der Ahe, J. M. Renoir, T. Buchou, E. E. Baulieu, and M. Beato, Receptors for glucocorticoid and progesterone recognize distinct features of a DNA regulatory element, Proc. Natl. Acad. Sci. USA 83: 2817–2821 (1986).

    Article  PubMed  Google Scholar 

  84. D. F. Skafar and A. C. Notides, Modulation of the estrogen receptor’s affinity for DNA by estradiol, J. Biol. Chem. 260: 12208–12213 (1985).

    PubMed  CAS  Google Scholar 

  85. P. Walter, S. Green, G. Greene, A Krust, J. Bornert, J. Jeltsch, A. Strub, E. Jensen, G. Scrace, M. Waterfield, and P. Chambon, Cloning of the human estrogen receptor cDNA, Proc. Natl. Acad., Sci. USA 82: 7889–7893 (1985).

    Article  CAS  Google Scholar 

  86. H. W. Dickerman and S. Kumar, The polynucleotide binding sites of estradiol receptor complexes, in: “Hormones and Cancer,” W. W. Leavitt, ed., Plenum Press, New York, pp. 1–18 (1982).

    Google Scholar 

  87. E. R. Mulvihill, J. P. LePennec, and P. Chambon, Chicken oviduct progesterone receptor: Location of specific regions of high-affinity binding in cloned DNA fragments of hormone-responsive genes, Cell 28: 621–632 (1982).

    Article  PubMed  CAS  Google Scholar 

  88. E. C. Lai, M. E. Riser, and B. W. O’Malley, Regulated expression of the chicken ovalbumin gene in a human estrogen-responsive cell line, J. Biol. Chem. 258: 12693–12701 (1983).

    PubMed  CAS  Google Scholar 

  89. G. A. Puca, E. Nola, V. Hibner, G. Cicala, and V. Sica, Interaction of the estradiol receptor from calf uterus with its nuclear acceptor sites, J. Biol. Chem. 250: 6452–6459 (1975).

    PubMed  CAS  Google Scholar 

  90. O. L. Kon and T. C. Spelsberg, Nuclear binding of estrogen receptor complex: Receptor specific nuclear acceptor sites, Endocrinology111: 1925–1934 (1982).

    Article  PubMed  CAS  Google Scholar 

  91. H. Toyoda, R. W. Seelke, B. A. Littlefield, and T. C. Spelsberg, Evidence for specific DNA sequences in the nuclear acceptor sites of the avian oviduct progesterone receptor, Proc. Natl. Acad. Sci. USA 82: 4722–4726 (1985).

    Article  PubMed  CAS  Google Scholar 

  92. R. K. Singh, M. F. Ruh, W. B. Butler, and T. S. Ruh, Acceptor sites on chromatin for receptor-bound by estrogen versus antiestrogen in antiestrogen-sensitive and -resistant MCF-7 cells, Endocrinology118: 1087–1095 (1986).

    Article  PubMed  CAS  Google Scholar 

  93. P. Ross, Jr., and T. S. Ruh, Binding of the estradiol-receptor complex to reconstituted nucleoacidic protein from calf uterus, Biochem. Biophys. Acta 782: 18–25 (1984).

    PubMed  CAS  Google Scholar 

  94. M. Lebeau, N. Massol, and E. Baulieu, Oestrogen and progesterone receptors in chick oviduct chromatin after administration of oestradiol, progesterone or anti-oestrogen, Biochem. J 204: 653–662 (1982).

    PubMed  CAS  Google Scholar 

  95. C. L. Cushing, R. A. Bambara, and R. Hilf, Interactions of estrogen-receptor and antiestrogen-receptor complexes with nuclei in vitro, Endocrinology116: 2419–2430 (1985).

    Article  PubMed  CAS  Google Scholar 

  96. R. N. Taylor and R. G. Smith, Effects of highly purified estrogen receptors on gene transcription in isolated nuclei, Biochemistry 21: 1781–1787 (1981).

    Article  Google Scholar 

  97. J. Jost, M. Seldran, and M. Geiser, Preferential binding of the estrogen-receptor complex to a region containing the estrogen- dependent hypomethylation site preceding the chicken vitellogenin II gene, Proc. Natl. Acad. Sci. USA 81: 429–433 (1984).

    Article  PubMed  CAS  Google Scholar 

  98. J. Jost, M. Geiser, and M. Seldran, Specific modulation of the transcription of cloned avian vitellogenin II gene by estradiol- receptor complex in vitro, Proc. Natl. Acad. Sci. USA 82: 988–991 (1985).

    Article  PubMed  CAS  Google Scholar 

  99. L. A. Zwelling, D. Kerrigan, and M. E. Lippman, Protein-associated intercalator-induced DNA scission is enhanced by estrogen stimulation in human breast cancer cells, Proc. Natl. Acad. Sci. USA 80: 6182 - 6186 (1983).

    Article  PubMed  CAS  Google Scholar 

  100. B. L. Maxwell, D. P. McDonnell, O. M. Conneely, T. Z. Schulz, G. L. Greene, and B. W. O’Malley, Structural organization and regulation of the chicken estrogen receptor, Mol. Endocrinol. 1: 25–35 (1987).

    Article  PubMed  CAS  Google Scholar 

  101. K. S. Bloom and J. N. Anderson, Conformation of ovalbumin and globin genes in chromatin during differential gene expression, J. Biol. Chem. 254: 10532–10539 (1979).

    PubMed  CAS  Google Scholar 

  102. K. Pratt, J. V. Wierowski, R. Hilf, and R. A. Bambarn, Bovine estrogen receptor binds chromatin at pre-existing nuclease hypersensitive sites, Mol. Cell. Endocrinol. 35: 205–20014 (1984).

    Article  CAS  Google Scholar 

  103. A. Geier, M. Haimsohn, R. Beeny, and B. Lunenfeld, Physical-chemical properties of the estrogen receptor solubilized by micrococcal nuclease, J. Steroid Biochem. 23: 137–143 (1985).

    Article  PubMed  CAS  Google Scholar 

  104. T. Thomas and B. S. Leung, Characterization of nuclear estradiol receptors released by micrococcal nuclease and deoxyribonuclease I, J. Steroid Biochem. 21: 35–42 (1984).

    Article  PubMed  CAS  Google Scholar 

  105. A. L. Goldberg and A. C. St. John, Intracellular protein degradation in mammalian and bacterial cells: Part 2, Ann. Rev. Biochem. 45: 747–803 (1976).

    Article  PubMed  CAS  Google Scholar 

  106. P. N. Cockerill and W. T. Garrard, Chromosomal loop anchorage of the kappa immunoglobulin gene occurs next to the enhancer in a region containing topoisomerase II sites, Cell 44: 273–282 (1986).

    Article  PubMed  CAS  Google Scholar 

  107. J. J. Dougherty, R. K. Puri, and D. O. Toft, Phosphorylation in vivo of chicken oviduct progesterone receptor, J. Biol. Chem. 257: 14226–14230 (1982).

    PubMed  CAS  Google Scholar 

  108. T. Garcia, P. Tuohima, J. Mester, T. Buchon, J. Renoir, and E. Baulieu, Protein kinase activity of purified components of the chicken oviduct progesterone receptor, Biochem. Biophys. Res. Comm. 113: 960–966 (1983).

    Article  CAS  Google Scholar 

  109. W. P. Sullivan, T. G. Beito, J. Proper, C. J. Krco, and D. O. Toft, Preparation of monoclonal antibodies to the avian progesterone receptor, Endocrinology119: 1549–1557 (1986).

    Article  PubMed  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Department of Biochemistry, Texas Tech University Health Sciences Center, Lubbock, TX, USA

    Wendell W. Leavitt, Andrea D. Cobb & Akihiro Takeda

Authors
  1. Wendell W. Leavitt
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Andrea D. Cobb
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Akihiro Takeda
    View author publications

    You can also search for this author in PubMed Google Scholar

Editor information

Editors and Affiliations

  1. Texas Tech University Health Sciences Center, Lubbock, Texas, USA

    Wendell W. Leavitt

Rights and permissions

Reprints and permissions

Copyright information

© 1987 Plenum Press, New York

About this chapter

Cite this chapter

Leavitt, W.W., Cobb, A.D., Takeda, A. (1987). Progesterone-Modulation of Estrogen Action: Rapid Down Regulation of Nuclear Acceptor Sites for the Estrogen Receptor. In: Leavitt, W.W. (eds) Cell and Molecular Biology of the Uterus. Advances in Experimental Medicine and Biology, vol 230. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-1297-0_4

Download citation

  • DOI: https://doi.org/10.1007/978-1-4684-1297-0_4

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4684-1299-4

  • Online ISBN: 978-1-4684-1297-0

  • eBook Packages: Springer Book Archive

Publish with us

Policies and ethics

Search

Navigation