Androgen Regulation of Ornithine Decarboxylase and S-Adenosylmethionine Decarboxylase Gene Expression

  • Olli A. Jänne
  • Anne Crozat
  • Mervi Julkunen
  • Noreen J. Hickok
  • Leonard Eisenberg
  • Evie Melanitou
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 250)

Abstract

The action of androgenic steroids in their target tissues occurs in a receptor-mediated fashion similar to that of other steroid hormones (1–3). Over the last several years, a number of gene products regulated by androgens have been characterized and their induction kinetics in vivo elucidated. The best defined genes fall, with regard to the tissues of their expression, into three main categories: (i) α2u-globulin and the major urinary protein genes are regulated by androgens in rodent liver; (ii) prostatein and seminal vesicle basic protein genes are controlled by androgens in rat accessory sex organs; and (iii) ornithine decarboxylase, β-glucuronidase, RP2, and kidney androgen-regulated protein genes exhibit androgen regulation in murine kidney.

Keywords

Ornithine Decarboxylase Mouse Kidney mRNA Accumulation Murine Kidney Androgen Regulation 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. 1.
    C. W. Bardin and J. F. Catterall, Testosterone, a major determinant of extragenital sexual dimorphism, Science 211: 1285 (1981).PubMedCrossRefGoogle Scholar
  2. 2.
    J. E. Griffin, M. Leishin, and J. D. Wilson, Androgen resistance syndromes, Am. J. Physiol. 243: E81 (1982).PubMedGoogle Scholar
  3. 3.
    K. K. Kontula, O. A. Jänne, and C. W. Bardin, Intracellular hormone receptor defects and disease, in: “Receptors IV”, P.M. Conn, ed., Academic Press, Orlando, pp. 37–74 (1986).Google Scholar
  4. 4.
    A. B. Kulkarni, R.M. Gubito, and P. Feigelson, Developmental and hormonal regulation of α2u-globulin gene transcription, Proc. Natl. Acad. Sci. USA 82: 2579 (1985).PubMedCrossRefGoogle Scholar
  5. 5.
    N. J. Kuhn, M. Woodworth-Gutai, K. W. Gross, and W. A. Held, Subfamilies of the mouse urinary protein (MUP) multi-gene family: Sequence analysis of cDNA clones and differential regulation in the liver, Nucleic Acids Res. 12: 6073 (1984).PubMedCrossRefGoogle Scholar
  6. 6.
    M. G. Parker, R. White, and J. G. Williams, Cloning and characterization of androgen-dependent mRNA from rat ventral prostate, J. Biol. Chem. 255: 6996 (1980).PubMedGoogle Scholar
  7. 7.
    M. K. Kistler, R. E. Taylor, Jr., J. C. Kandala, and W. S. Kistler, Isolation of recombinant plasmids containing structural gene sequences for rat seminal vesicle secretory proteins IV and V, Biochem. Biophys. Res. Commun. 99: 1161 (1981).PubMedCrossRefGoogle Scholar
  8. 8.
    J. F. Catterall, K. K. Kontula, C. S. Watson, P. J. Seppänen, B. Funkenstein, E. Melanitou, N. J. Hickok, C. W. Bardin, and O. A. Jänne, Regulation of gene expression by androgens in murine kidney, Recent Prog. Horm. Res. 42: 71 (1986).PubMedGoogle Scholar
  9. 9.
    C. S. Watson, D. Salomon, and J. F. Catterall, Structure and expression of androgen-regulated genes in mouse kidney, Ann. N.Y. Acad. Sci. 438: 101 (1984).PubMedCrossRefGoogle Scholar
  10. 10.
    K. K. Kontula, T. K. Torkkeli, C. W. Bardin, and O. A. Jänne, Androgen induction of ornithine decarboxylase mRNA in mouse kidney as studied by complementary DNA, Proc. Natl. Acad. Sci. USA 81: 731 (1984).PubMedCrossRefGoogle Scholar
  11. 11.
    A. E. Pegg and P. P. McCann, Polyamine metabolism and function, Am. J. Physiol. 243: C212 (1982).PubMedGoogle Scholar
  12. 12.
    J. E. Seely, H. Pösö, and A. E. Pegg, Purification of ornithine decarboxylase from kidneys of androgen treated mice, Biochemistry 21: 3394 (1982).PubMedCrossRefGoogle Scholar
  13. 13.
    V. V. Isomaa, A. E. I. Pajunen, C. W. Bardin, and O. A. Jänne, Ornithine decarboxylase in mouse kidney. Purification, characterization and radioimmunological determination of the enzyme protein, J. Biol. Chem. 258: 6735 (1983).PubMedGoogle Scholar
  14. 14.
    N. J. Hickok, P. J. Seppänen, G. L. Gunsalus, and O. A. Jänne, Complete amino acid sequence of human ornithine decarboxylase deduced from complementary DNA, DNA 6: 179 (1987).PubMedCrossRefGoogle Scholar
  15. 15.
    M. Gupta and P. Coffino, Mouse ornithine decarboxylase. Complete amino acid sequence deduced from cDNA, J. Biol. Chem. 260: 2941 (1985).PubMedGoogle Scholar
  16. 16.
    O. A. Jänne, K. K. Kontula, V. V. Isomaa, T. K. Torkkeli, and C. W. Bardin, Androgen-receptor dependent regulation of ornithine decarboxylase gene expression in mouse kidney, in: “Steroid Hormone Receptors: Structure and function”, H. Eriksson and J.-A. Gustafsson, eds., Elsevier Science Publishers BV, Amsterdam, pp. 461–476 (1983).Google Scholar
  17. 17.
    L. Persson, J. E. Seely, and A. E. Pegg, Investigation of structure and rate of synthesis of ornithine decarboxylase protein in mouse kidney, Biochemistry 23: 3777 (1984).PubMedCrossRefGoogle Scholar
  18. 18.
    A. Pulkka, T. Taskinen, H. Aaltonen, J. Ramberg, and A. E. I. Pajunen, Studies on the degradation of ornithine decarboxylase by the immunoblotting technique, Biochem. Int. 11: 845 (1985).PubMedGoogle Scholar
  19. 19.
    M. Macrae and P. Coffino, Complementation of a polyamine-deficient Escherichia coli mutant by expression of mouse ornithine decarboxylase, Mol. Cell. Biol. 7: 564 (1987).PubMedGoogle Scholar
  20. 20.
    J. E. Seely and A. E. Pegg, Changes in mouse kidney ornithine decarboxylase activity are brought about by changes in the amount of enzyme protein as measured by radioimmunoassay, J. Biol. Chem. 258: 2496 (1983).PubMedGoogle Scholar
  21. 21.
    S. Rogers, R. Wells, and M. Rechsteiner, Amino acid sequences common to rapidly degraded proteins: The PEST hypothesis, Science 234: 364 (1986).PubMedCrossRefGoogle Scholar
  22. 22.
    C. Kahana and D. Nathans, Translational regulation of mammalian ornithine decarboxylase by polyamines, J. Biol. Chem. 260: 15390 (1985).PubMedGoogle Scholar
  23. 23.
    E. Hölttä and P. Pohjanpelto, Control of ornithine decarboxylase in Chinese hamster ovary cells by polyamines. Translational inhibition of synthesis and acceleration of degradation of the enzyme by putrescine, spermidine, and spermine, J. Biol. Chem. 261: 9502 (1986).PubMedGoogle Scholar
  24. 24.
    A. E. I. Pajunen, V. V. Isomaa, O. A. Jänne, and C. W. Bardin, Androgenic regulation of ornithine decarboxylase activity and its relationship to changes in cytosol and nuclear androgen receptors, J. Biol. Chem. 257: 8190 (1982).PubMedGoogle Scholar
  25. 25.
    G. J. Sertich and A. E. Pegg, Polyamine administration reduces ornithine decarboxylase activity without affecting the mRNA content, Biochenu Biophys. Res. Commun. 143: 424 (1987).CrossRefGoogle Scholar
  26. 26.
    N. J. Hickok, P. J. Seppänen, K. K. Kontula, P. A. Jänne, C. W. Bardin, and O. A. Jänne, Two ornithine decarboxylase mRNA species in mouse kidney arise from size heterogeneity at their 3′ termini, Proc. Natl. Acad. Sci. USA 83: 594 (1986).PubMedCrossRefGoogle Scholar
  27. 27.
    C. Kahana and D. Nathans, Nucleotide sequence of murine ornithine decarboxylase mRNA, Proc. Natl. Acad. Sci. USA 82: 1673 (1985).PubMedCrossRefGoogle Scholar
  28. 28.
    A. Katz and C. Kahana, Isolation and characterization of the mouse ornithine decarboxylase gene, J. Biol. Chem. 263: 7604 (1988).PubMedGoogle Scholar
  29. 29.
    M. Brabant, L. McConlogue, T. van Daalen Wetters, and P. Coffino, Mouse ornithine decarboxylase gene: Cloning, structure, and expression, Proc. Natl. Acad. Sci. USA 85: 2200 (1988).PubMedCrossRefGoogle Scholar
  30. 30.
    R. Winqvist, T. P. Mäkelä, P. Seppänen, O. A. Jänne, L. Alhonen-Hongisto, J. Jänne, K.-H. Grzeschik, and K. Alitalo, Human ornithine decarboxylase sequences map to chromosome regions 2pter→p23 and 7cen→qter but are not co-amplified with the NMYC oncogene, Cytogenet. Cell. Genet. 42: 133 (1986).PubMedCrossRefGoogle Scholar
  31. 31.
    O. A. Jänne, K. K. Kontula, V. V. Isomaa, and C. W. Bardin, Ornithine decarboxylase mRNA in mouse kidney: A low abundancy gene product regulated by androgens with rapid kinetics, Ann. N.Y. Acad. Sci. 438: 72 (1984).PubMedCrossRefGoogle Scholar
  32. 32.
    F. G. Berger, D. Loose, H. Meisner, and G. Watson, Androgen induction of messenger RNA concentrations in mouse kidney is posttranscriptional, Biochemistry 25: 1170 (1986).PubMedCrossRefGoogle Scholar
  33. 33.
    M. J. Page and M. G. Parker, Effect of androgen on the transcription of rat prostatic binding protein genes, Mol. Cell. Endocrinol. 27: 343 (1982).PubMedCrossRefGoogle Scholar
  34. 34.
    E. Melanitou, D. A. Cohn, C. W. Bardin, and O. A. Jänne, Genetic variation in androgen regulation of ornithine decarboxylase gene expression in inbred strains of mice, Mol. Endocrinol. 1: 266 (1987).PubMedCrossRefGoogle Scholar
  35. 35.
    A. E. Pegg, D. H. Lockwood, and H. G. Williams-Ashman, Concentrations of putrescine and polyamines and their enzymic synthesis during androgeninduced prostatic growth, Biochem. J. 117: 17 (1970).PubMedGoogle Scholar
  36. 36.
    K. Käpyaho, A. Kallio, and J. Jänne, Differential effects of 2-difluoromethylornithine and methylglyoxal bis(guanylhydrazone) on the testosterone-induced growth of ventral prostate and seminal vesicles of castrated rats, Biochem. J. 219: 811 (1984).PubMedGoogle Scholar
  37. 37.
    A. Pajunen, A. Crozat, O. A. Jänne, R. Ihalainen, P. H. Laitinen, B. Stanley, R. Madhubala, and A. E. Pegg, Structure and regulation of mammalian S-adenosylmethionine decarboxylase, J. Biol. Chem., in press (1988).Google Scholar

Copyright information

© Plenum Press, New York 1988

Authors and Affiliations

  • Olli A. Jänne
    • 1
  • Anne Crozat
    • 1
  • Mervi Julkunen
    • 1
  • Noreen J. Hickok
    • 1
  • Leonard Eisenberg
    • 1
  • Evie Melanitou
    • 1
  1. 1.The Population CouncilThe Rockefeller UniversityNew YorkUSA

Personalised recommendations