Abstract
Tissue levels of ornithine decarboxylase (ODC) are under negative feedback regulation by polyamines. Thus, exogenously added polyamines cause a rapid decrease of ODC activity. Recent studies in various laboratories have indicated that the rapid decay of ODC activity caused by polyamines is due both to suppression of ODC synthesis (1–3) and to acceleration of ODC degradation (1, 2, 4) and that a new protein synthesis is needed for the latter effect (2). Antizyme was discovered in 1976 by Canellakis and his collaborators as a unique protein inhibitor of ODC induced by polyamines (5, 6). Since then, antizyme has been shown to be present in various tissues and cells as a free form and/or a complex with ODC (7). Previous studies in this and other laboratories have led to a hypothesis that antizyme not only inhibits ODC activity but also accelerates its degradation in a recycling manner (8–10). The strongest evidence for that hypothesis was the existence of a good correlation between ODC decay rate and antizyme/ODC ratio in HTC cells (9). In the present paper, we report the results of our recent studies that support the above hypothesis. We also present some of our results on the cloning of cDNAs for rat liver antizyme.
This is a preview of subscription content, log in via an institution.
Buying options
Tax calculation will be finalised at checkout
Purchases are for personal use only
Learn about institutional subscriptionsPreview
Unable to display preview. Download preview PDF.
References
R. Kanamoto, K. Utsunomiya, T. Kameji, and S. Hayashi, Effects of putrescine on synthesis and degradation of ornithine decarboxylase in primary cultured hepatocytes, Eur. J. Biochem., 154: 539 (1986)
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)
L. Persson, I. Holm., and O. Heby, Translational regulation of ornithine decarboxylase by polyamines, FEBS Lett., 205: 175 (1986)
J. R. Glass and E. W. Gerner, Polyamine-mediated turnover of ornithine decarboxylase in Chinese hamster ovary cells, Biochem. J., 236
W. F. Fong, J. S. Heller, and E. S. Canellakis, The appearance of an ornithine decarboxylase inhibitory protein upon addition of putrescine to cell cultures, Biochim. Biophys. Acta, 428: 456 (1876)
J. S. Heller, W. F. Fong, and E. S. Canellakis, Induction of a protein inhibitor to ornithine decarboxylase by the end products of its reaction, Proc. Natl. Acad. Sci. USA, 73: 1858 (1876)
S. Hayashi and E. S. Canellakis, Ornithine decarboxylase antizymes, in “Ornithine Decarboxylase: Biology, Enzymology, and Molecular Genetics,” S. Hayashi, ed., Pergamon Press, Elmsford, N.Y., (In the press)
Y. Murakami, K. Fujita, T. Kameji, and S. Hayashi, Accumulation of ornithine decarboxylase-antizyme complex in HMOA cells, Biochem. J., 225: 689 (1985)
Y. Murakami and S. Hayashi, Role of antizyme in degradation of ornithine decarboxylase in HTC cells, Biochem. J., 226: 893 (1985)
J. E. Seely and A. E. Pegg, Effect of 1,3-diaminopropane on ornithine decarboxylase enzyme protein in thioacetamide-treated rat liver, Biochem. J., 216: 701 (1983)
L. Persson and E. Rosengren, Inhibition of ornithine decarboxylase activity in mouse kidney by administration of diamines, Acta Chem. Scand., 33: 537 (1979)
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)
P. H. Laitinen, R.-L. Huhtinen, O. A. Hietala, and A. E. I. Pajunen, Ornithine decarboxylase activity in brain regulated by a specific macromolecule, the antizyme, J. Neurochem., 44: 1885 (1985)
Y. Murakami, M. Marumo, and S. Hayashi, Ornithine decarboxylase antizyme in kidneys of male and female mice, Biochem. J., (In the press)
K. Fujita, Y. Murakami, and S. Hayashi, A macromolecular inhibitor of the antizyme to ornithine decarboxylase, Biochem. J., 204: 647 (1982)
L. Persson, Putrescine turnover in kidneys of testosterone-treated mice, Biochim. Biophys. Acta,, 674: 204 (1981)
J. E. Seely, H. Pösö, and A. E. Pegg, Effect of androgens on turnover of ornithine decarboxylase in mouse kidney. Studies using labeling of the enzyme by reaction with (14C)alpha-difluoromethylornithine, J. Biol. Chem., 257: 7549 (1982)
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)
S. Henningsson and E. Rosengren, Biosynthesis of histamine and putrescine in mice during post-natal development and its hormone dependence, J. Physiol., 245: 467 (1975)
S. I. Harik, M. D. Hollenberg, and S. H. Snyder, Ornithine decarboxylase turnover slowed by alpha-hydrazinoornithine, Mol. Pharmacol., 10: 41 (1974)
H. Inoue, Y. Kato, M. Takigawa, K. Adachi, and Y. Takeda, Effect of DL-alpha-hydrazino-delta-aminovaleric acid, an inhibitor of ornithine decarboxylase, on polyamine metabolism in isoproterenolstimulated mouse parotid glands, J. Biochem., 77: 879 (1975)
P. P. McCann, C. Tardif, M. C. Duchesne, and P. S. Mamont, Effect of alpha-methylornithine on ornithine decarboxylase activity of rat hepatoma cells in culture, Biochem. Biophys. Res. Commun., 76: 893 (1977)
P. P. McCann, Regulation of ornithine decarboxylase in eukaryotes, in “Polyamines in Biomedical Research,” G. M. Gaugas, ed., John Wiley and Sons, New York (1980)
J. L. A. Mitchell, D. W. Maha, P. P. McCann, and P. Qasba, Dicyclohexylamine effects on HTC cell polyamine content and ornithine decarboxylase activity, Biochim. Biophys. Acta, 840: 309 (1985)
E. Karvonen and H. Pösö, Stabilization of ornithine decarboxylase and N1-spermidine acetyltransferase in rat liver by methylglyoxalbis(guanylhydrazone), Biochim. Biophys. Acta, 791: 239 (1984)
P. Nikula, L. Alhonen-Hongisto, and J. Jänne, Effects of bis(guanylhydrazone)s on the activity and expression of ornithine decarboxylase, Biochem. J., 231: 213 (1985)
L. Persson, S. M. Oredsson, S. Anehus, and O. Heby, Ornithine decarboxylase inhibitors increase the cellular content of the enzyme: Implications for translational regulation, Biochem. Biophys. Res. Commun., 131: 239 (1985)
Y. Murakami, M. Nishiyama, and S. Hayashi, Involvement of antizyme in stabilization of ornithine decarboxylase caused by inhibitors of polyamine synthesis, (Submitted to Eur. J. Biochem.)
A. E. Pegg, Recent advances in the biochemistry of polyamines in eukaryotes, Biochem. J., 234: 249 (1986)
H. Onoue, S. Matsufuji, M. Nishiyama, Y. Murakami, and S. Hayashi, Changes in ornithine decarboxylase and antizyme activities in developing mouse brain, Biochem. J., 250: 797 (1988)
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1988 Plenum Press, New York
About this chapter
Cite this chapter
Hayashi, S., Murakami, Y., Matsufuji, S., Nishiyama, M., Kanamoto, R., Kameji, T. (1988). Studies on Ornithine Decarboxylase Antizyme. 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_3
Download citation
DOI: https://doi.org/10.1007/978-1-4684-5637-0_3
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4684-5639-4
Online ISBN: 978-1-4684-5637-0
eBook Packages: Springer Book Archive