Skip to main content

Estrogenic Control of Spermidine/Spermine N1-Acetyltransferase Activity in Rat Uterus

  • Chapter
Progress in Polyamine Research

Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 250))

  • 150 Accesses

Abstract

It is widely accepted that specific intracellular receptor proteins are implicated in the estrogen regulation of gene expression, growth and differentiation in target cells. The unoccupied forms of these receptors, as suggested by Jensen and Jacobson1 and Gorski et al.,2 reside primarily in the cytoplasm and translocate to the nucleus after hormone interaction. A revision of this classical “two-step” model has recently indicated that both native and ligand-bound forms of the receptors are localized in the nucleus, as supported by biochemical3 and immunocytochemical4 data. The binding of estrogen with receptor leads to a change in the conformational state of the protein, which increases its affinity for nuclear components and DNA.3, 4 A number of nuclear acceptor sites have been proposed, including specific DNA sequences,5 ribonucleoprotein,6 basic nonhistone proteins, nuclear matrix,8 and acidic nonhistone protein DNA complexes.9 The binding of activated receptor with DNA or other nuclear components triggers the synthesis of specific proteins, growth, and differentiation in responsive tissues.

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

Access this chapter

eBook
USD 16.99
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. E. V. Jensen and H. I. Jacobson, Basic guides to the mechanism of estrogen action, Recent Prog. Horm. Res. 18: 387 (1962).

    CAS  Google Scholar 

  2. J. Gorski, D. Toft, G. Shyamala, D. Smith, and A. Notides, Hormone receptors: studies on the interaction of estrogen with the uterus, Recent Prog. Horm. Res. 24: 45 (1968).

    PubMed  CAS  Google Scholar 

  3. W. V. Welshons, M. E. Lieberman, and J. Gorski, Nuclear localization of unoccupied oestrogen receptors, Nature 307: 747 (1984).

    Article  PubMed  CAS  Google Scholar 

  4. W. J. King and G. L. Greene, Monoclonal antibodies localize oestrogen receptor in the nuclei of target cells, Nature 307: 745 (1984).

    Article  PubMed  CAS  Google Scholar 

  5. J. P. Jost, M. Geiser, and M. Seldran, Specific modulation of the transcription of cloned avian vitellogenin II gene by estradiolreceptor complex in vitro, Proc. Natl. Acad. Sci. USA 82: 988 (1985).

    Article  PubMed  CAS  Google Scholar 

  6. T. Ling and S. Liao, Association of the uterine 17β-estradiol receptor complex with ribonucleoprotein in vitro and in vivo, J. Biol. Chem. 249: 4671 (1974).

    Google Scholar 

  7. G. A. Puca, V. Sica, and E. Nola, Identification of a high affinity nuclear acceptor site for estrogen receptor of calf uterus, Proc. Natl. Acad. Sci. USA 71: 979 (1974).

    Article  PubMed  CAS  Google Scholar 

  8. 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 (1980).

    PubMed  CAS  Google Scholar 

  9. 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, Recent Prog. Hoxm. Res. 39: 463 (1983).

    CAS  Google Scholar 

  10. W. V. Vedeckis, Steroid hormone receptor structure in normal and neoplastic cells, in: “Hormonally Responsive Tumors”, V. P. Hollander, ed., Academic Press, New York (1985).

    Google Scholar 

  11. W. W. Grody, W. T. Schrader, and B. W. 0’Malley, Activation, transformation and subunit structure of steroid hormone receptors, Endocr. Rev. 3: 141 (1982).

    Article  PubMed  CAS  Google Scholar 

  12. P. R. Housley and W. B. Pratt, Direct demonstration of glucocorticoid-receptor phosphorylation by intact L cells, J. Biol. Chem. 258: 4630 (1983).

    PubMed  CAS  Google Scholar 

  13. N. L. Weigel, J. S. Tash, A. R. Means, W. T. Schrader, and B. W. O’Malley, Phosphorylation of hen progesterone receptor by cAMP dependent protein kinase, Biochem. Biophys. Res. Commun. 102: 513 (1981).

    Article  PubMed  CAS  Google Scholar 

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

    PubMed  CAS  Google Scholar 

  15. M. K. Dahmer, P. R. Housley, and W. B. Pratt, Effects of molybdate and endogenous inhibitors on steroid-receptor inactivation, transformation, and translocation, Annu. Rev. Physiol. 46: 67 (1984).

    Article  PubMed  CAS  Google Scholar 

  16. T. Thomas and D. T. Kiang, Structural alterations and stabilization of rabbit uterine estrogen receptors by natural polyamines, Cancer Res. 47: 1799 (1987).

    PubMed  CAS  Google Scholar 

  17. S. Cohen, B. W. O’Malley, and M. Stastny, Estrogenic induction of ornithine decarboxylase in vivo and in vitro, Science 170: 336 (1970).

    Article  PubMed  CAS  Google Scholar 

  18. K. Käpyaho, H. Pösö, and J. Jänne, Role of propylamine transferases in hormone-induced stimulation of polyamine biosynthesis, Biochem. J. 192: 59 (1980).

    PubMed  Google Scholar 

  19. A. M. Kaye, I. Icekson, and H. R. Lindner, Stimulation by estrogens of ornithine and S-adenosylmethionine decarboxylases in the immature rat uterus. Biochim. Biophys. Acta 252: 150 (1971).

    Article  PubMed  CAS  Google Scholar 

  20. D. H. Russell and R. L. Taylor, Polyamine synthesis and accumulation in the castrated rat uterus after estradiol-17β stimulation, Endocrinology 88: 1397 (1971).

    Article  PubMed  CAS  Google Scholar 

  21. D. W. Lundgren, P. M. Farrell, L. F. Cohen, and J. Hankins, Fluctuations of unbound whole blood polyamine levels during the menstrual cycle, Proc. Soc. Exp. Biol. Med. 152: 81 (1976).

    PubMed  CAS  Google Scholar 

  22. O. Hernandes, L. M. Ballesteros, D. Mendez, and A. Rosado, Polyamine synthesis and polysome patterns in the rat uterus during the estrous cycle, Endocrinology 92: 1107 (1973).

    Article  Google Scholar 

  23. H. Nawata, R. S. Yamamoto, and L. A. Poirier, An inverse linear correlation between uterine and ovarian levels of ornithine decarboxylase and S-adenosylmethionine decarboxylase in the rat, Proc. Soc. Exp. Biol. Med. 167: 563 (1981).

    PubMed  CAS  Google Scholar 

  24. M. S. Smith, M. E. Freeman, and J. D. Neill, The control of progesterone secretion during the estrous cycle and early pseudopregnancy in the rat: prolactin, gonadotropin and steroid levels associated with rescue of the corpus luteum of pseudo-pregnancy, Endocrinology 96: 219 (1975).

    Article  PubMed  CAS  Google Scholar 

  25. K. Yoshinaga, R. A. Hawkins, and J. F. Stocker, Estrogen secretion by the rat ovary in vivo during the estrous cycle and pregnancy, Endocrinology 85: 103 (1969).

    Article  PubMed  CAS  Google Scholar 

  26. R. L. Butcher, W. E. Collins, and N. W. Fugo, Plasma concentration of LH, FSH, prolactin, progesterone and estradiol-17β throughout the 4-day estrous cycle of the rat, Endocrinology 94: 1704 (1974).

    Article  PubMed  CAS  Google Scholar 

  27. Y. Kobayashi, J. Kupelian, and D. V. Maudsley, Ornithine decarboxylase stimulation in rat ovary by luteinizing hormone, Science 172: 379 (1971).

    Article  PubMed  CAS  Google Scholar 

  28. L. Persson, K. Isaksson, E. Rosengren, and F. Sundler, Distribution of ornithine decarboxylase in ovaries of rat and hamster during pro-oestrus, Acta Endocrinol. 113: 403 (1986).

    PubMed  CAS  Google Scholar 

  29. S. K. Guha and J. Jänne, Decarboxylation of ornithine and adenosyl-methionine in rat ovary during pregnancy, Acta Endocrinol. 81: 793 (1976).

    PubMed  CAS  Google Scholar 

  30. S. K. Guha and J. Jänne, The synthesis and accumulation of polyamines in reproductive organs of the rat during pregnancy, Biochim. Biophys. Acta 437: 244 (1976).

    Article  PubMed  CAS  Google Scholar 

  31. W. A. Fogel, Diamine oxidase (DAO) and female sex hormones, Agents Actions 18: 4 (1986).

    Article  Google Scholar 

  32. M. E. Lippman and G. Bolan, Oestrogen-responsive human breast cancer in long term tissue culture, Nature 256: 592 (1975).

    Article  PubMed  CAS  Google Scholar 

  33. M. Lippman, G. Bolan, and K. Huff, The effects of estrogens and antiestrogens on hormone-responsive human breast cancer in long-term tissue culture, Cancer Res. 36: 4595 (1976).

    PubMed  CAS  Google Scholar 

  34. R. R. Weichselbaum, S. Hellman, A. J. Piro, J. J. Nove, and J. B. Little, Proliferation kinetics of a human breast cancer line in vitro following treatment with 17β-estradiol and 1-β-D-arabinofuranosylcytosine, Cancer Res. 38: 2339 (1978).

    PubMed  CAS  Google Scholar 

  35. J. C. Allegra and M. E. Lippman, Growth of a human breast cancer cell line in serum-free hormone-supplemented medium, Cancer Res. 38: 3823 (1978).

    PubMed  CAS  Google Scholar 

  36. A. Manni and C. Wright, Polyamines as mediators of estrogen action on the growth of experimental breast cancer in rats, J. Natl. Cancer Inst. 73: 511 (1984).

    PubMed  CAS  Google Scholar 

  37. G. Lima and R. P. C. Shiu, Role of polyamines in estradiol-induced growth of human breast cancer cells, Cancer Res. 45: 2466 (1985).

    PubMed  CAS  Google Scholar 

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

    Article  PubMed  CAS  Google Scholar 

  39. F. Vignon, M. E. Lippman, H. Nawata, D. Derocq, and H. Rochefort, Induction of two estrogen-responsive proteins by antiestrogens in R27, a tamoxifen-resistant clone of MCF7 cells, Cancer Res. 44: 2084 (1984).

    PubMed  CAS  Google Scholar 

  40. A. Manni, C. Wright, P. Feil, L. Baranao, L. Demers, M. Garcia, and H. Rochefort, Autocrine stimulation by estradiol-regulated growth factors of rat hormone-responsive mammary cancer: interaction with the polyamine pathway, Cancer Res. 46: 1594 (1986).

    PubMed  CAS  Google Scholar 

  41. A. E. Pegg, Recent advances in the biochemistry of polyamines in eukaryotes, Biochem. J. 234: 249 (1986).

    PubMed  CAS  Google Scholar 

  42. N. Seiler, Functions of polyamine acetylation, Can. J. Physiol. Pharmacol. 65: 2024 (1987).

    Article  PubMed  CAS  Google Scholar 

  43. A. E. Pegg and G. Erwin, Induction of spermidine/spermine N1-acetyltransferase in rat tissues by polyamines, Biochem. J. 231: 285 (1985).

    PubMed  CAS  Google Scholar 

  44. P. R. Libby, Calf liver nuclear N-acetyltransferases: purification and properties of two enzymes with both spermidine acetyltrans-ferase and histone acetyltransferase activities, J. Biol. Chem. 253: 23 (1978).

    Google Scholar 

  45. I. Matsui and A. E. Pegg, Effect of thioacetamide, growth hormone or partial hepatectomy on spermidine acetylase activity of rat liver cytosol, Biochim. Biophys. Acta, 633: 87 (1980).

    Article  PubMed  CAS  Google Scholar 

  46. C. W. Tabor and H. Tabor, 1, 4-Diaminobutane (putrescine), spermidine, and spermine, Annu. Rev. Biochem. 45: 285 (1976).

    Article  PubMed  CAS  Google Scholar 

  47. J. Jänne, H. Pösö, and A. Raina, Polyamines in rapid growth and cancer, Biochim. Biophys. Acta 473: 241 (1978).

    PubMed  Google Scholar 

  48. C. W. Tabor and H. Tabor, Polyamines, Annu. Rev. Biochem. 53: 749 (1984).

    Article  PubMed  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Editor information

Editors and Affiliations

Rights and permissions

Reprints and permissions

Copyright information

© 1988 Plenum Press, New York

About this chapter

Cite this chapter

Perin, A., Sessa, A., Desiderio, M.A. (1988). Estrogenic Control of Spermidine/Spermine N1-Acetyltransferase Activity in Rat Uterus. In: Zappia, V., Pegg, A.E. (eds) Progress in Polyamine Research. Advances in Experimental Medicine and Biology, vol 250. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-5637-0_30

Download citation

  • DOI: https://doi.org/10.1007/978-1-4684-5637-0_30

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4684-5639-4

  • Online ISBN: 978-1-4684-5637-0

  • eBook Packages: Springer Book Archive

Publish with us

Policies and ethics