Polyamine-Mediated Regulation of Mouse Ornithine Decarboxylase Is Posttranslational

LITERATURE CITED

• Brabant, M., L. McConlogue, T. van Daalen Wetters, and P. Coffino. 1988. Mouse ornithine decarboxylase gene: cloning, structure, and expression. Proc. Natl. Acad. Sci. USA 85:2200–2204.
   PubMedGoogle Scholar
• Casadaban, M. J., A. Martinez-Arias, S. K. Shapira, and J. Chou. 1983. Beta galactosidase gene fusions for analyzing gene expression in Escherichia coli and yeast. Methods Enzymol. 100:293–308.
   PubMed Web of Science ®Google Scholar
• Clark, J. L.. 1974. Specific induction of ornithine decarboxylase in 3T3 mouse fibroblasts by pituitary growth factors: cell density-dependent biphasic response and alteration of half-life. Biochemistry 13:4668–4674.
   PubMed Web of Science ®Google Scholar
• Coffino, P., and E. L. Chen. 1988. Nucleotide sequence of the mouse ornithine decarboxylase gene. Nucleic Acids Res. 16:2731–2732.
   PubMedGoogle Scholar
• Dircks, L., A. Grens, T. C. Slezynger, and I. E. Scheffler. 1986. Posttranscriptional regulation of ornithine decarboxylase activity. J. Cell. Physiol. 126:371–378.
   PubMedGoogle Scholar
• Feinberg, A. P., and B. Vogelstein. 1983. A technique for radiolabeling DNA restriction endonuclease fragments to high specific activity. Anal. Biochem. 132:6–13.
   PubMed Web of Science ®Google Scholar
• Ghoda, L., T. van Daalen Wetters, M. Macrae, D. Ascherman, and P. Coffino. 1989. Prevention of rapid intracellular degradation of ODC by a carboxyl-terminal truncation. Science 243:1493–1495.
   PubMedGoogle Scholar
• Gupta, M., and P. Coffino. 1985. Mouse ornithine decarboxylase: complete amino acid sequence deduced from cDNA. J. Biol. Chem. 260:2941–2944.
   PubMedGoogle Scholar
• Hall, C. V., P. E. Jacob, G. M. Ringold, and F. Lee. 1983. Expression and regulation of Escherichia coli lacZ gene fusions in mammalian cells. J. Mol. Appl. Genet. 2:101–109.
   PubMedGoogle Scholar
• Herbomel, P., B. Bourachot, and M. Yaniv. 1984. Two distinct enhancers with different cell specificities coexist in the regulatory region of polyoma. Cell 39:653–662.
   PubMed Web of Science ®Google Scholar
• Holm, I., L. Persson, L. Stjemborg, L. Thorsson, and O. Heby. 1989. Feedback control of ornithine decarboxylase expression by polyamines. Biochem. J. 258:343–350.
   PubMedGoogle Scholar
• Holtta, E., and P. Pofijanpelto. 1986. Control of ornithine decarboxylase in Chinese hamster ovary cells by polyamines. J. Biol. Chem. 261:9502–9508.
   PubMedGoogle Scholar
• Isomaa, V. V., A. E. I. Pajunen, C. W. Bardin, and O. A. Janne. 1983. Ornithine decarboxylase in mouse kidney: purification, characterization and radioimmunological determination of the enzyme protein. J. Biol. Chem. 258:6735–6740.
   PubMedGoogle Scholar
• Jacobson, A. Β., H. Kumar, and M. Zuker. 1985. Effect of spermidine on the conformation of bacteriophage MS2 RNA electron microscopy and computer modeling. J. Mol. Biol. 181:517–531.
   PubMedGoogle Scholar
• Jones, C. L., and E. Ehrenfeld. 1983. The effect of poliovirus infection on the translation in vitro of VSV messenger ribonucleoprotein particles. Virology 129:415–430.
   PubMedGoogle Scholar
• Kahana, C., and D. Nathans. 1985. Translational regulation of mammalian ornithine decarboxylase by polyamines. J. Biol. Chem. 260:15390–15393.
   PubMedGoogle Scholar
• Katz, A., and C. Kahana. 1988. Isolation and characterization of the mouse ornithine decarboxylase gene. J. Biol. Chem. 263:7604–7609.
   PubMedGoogle Scholar
• Madhubala, R., J. A. Secrist III, and A. E. Pegg. 1988. Effect of inhibitors of S-adenosylmethionine decarboxylase on the contents of ornithine decarboxylase and S-adenosylmethionine decarboxylase in L1210 cells. Biochem. J. 254:45–50.
   PubMedGoogle Scholar
• Mathews, M. B. (ed.). 1986. Translational control. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
   Google Scholar
• McConlogue, L., and P. Coffino. 1983. Ornithine decarboxylase in difluoromethylomithine-resistant mouse lymphoma cells. J. Biol. Chem. 258:8384–8388.
   PubMedGoogle Scholar
• McConlogue, L., S. L. Dana, and P. Coffino. 1986. Multiple mechanisms are responsible for altered expression of ornithine decarboxylase in overproducing variant cells. Mol. Cell. Biol. 6:2865–2871.
   PubMedGoogle Scholar
• McConlogue, L. C., L. J. Marton, and P. Coffino. 1983. Growth regulatory effects of cyclic AMP and polyamine depletion are dissociable in cultured mouse lymphoma cells. J. Cell. Biol. 96:762–767.
   PubMedGoogle Scholar
• Pachter, J. S., T. J. Yen, and D. W. Cleveland. 1987. Autoregulation of tubulin expression is achieved through specific degradation of polysomal tubulin mRNAs. Cell 51:283–292.
   PubMedGoogle Scholar
• Pegg, A. E.. 1986. Recent advances in the biochemistry of polyamines in eukaryotes. Biochem. J. 234:249–262.
   PubMed Web of Science ®Google Scholar
• Pegg, A. E., R. Madhubala, T. Kameji, and R. J. Bergereon. 1988. Control of ornithine decarboxylase activity in alpha- difluoromethylomithine-resistant L1210 cells by polyamines and synthetic analogues. J. Biol. Chem. 263:11008–11014.
   PubMed Web of Science ®Google Scholar
• Penman, S., C. Vesco, and M. Penman. 1968. Localization and kinetics of formation of nuclear heterodisperse RNA, cytoplasmic heterodisperse RNA and polyribosome-associated messenger RNA in HeLa cells. J. Mol. Biol. 34:49–69.
   PubMed Web of Science ®Google Scholar
• Persson, L., I. Holm, and O. Heby. 1986. Translational regulation of ornithine decarboxylase by polyamines. FEBS Lett. 205:175–178.
   PubMed Web of Science ®Google Scholar
• Persson, L., I. Holm, and O. Heby. 1988. Regulation of ornithine decarboxylase mRNA translation by polyamines. J. Biol. Chem. 263:3528–3533.
   PubMed Web of Science ®Google Scholar
• Persson, L., S. M. Oredsson, S. Anehus, and O. Heby. 1985. Ornithine decarboxylase inhibitors increase the cellular content of the enzyme: implications for translational regulation. Biochem. Biophys. Res. Commun. 131:239–245.
   PubMed Web of Science ®Google Scholar
• Quigley, G. J., M. M. Teeter, and A. Rich. 1978. Structural analysis of spermine and magnesium ion binding to yeast phenylalanine transfer RNA. Proc. Natl. Acad. Sci. USA 75:64–68.
   PubMed Web of Science ®Google Scholar
• Russell, D. H., and S. H. Snyder. 1969. Amine synthesis in regenerating rat liver: extremely rapid turnover of ornithine decarboxylase. Mol. Pharmacol. 5:253–262.
   PubMed Web of Science ®Google Scholar
• Schimke, R. T.. 1973. Control of enzyme levels in mammalian tissues. Adv. Enzymol. 37:135–187.
   PubMedGoogle Scholar
• Seely, J. E., and A. E. Pegg. 1983. 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. 258:2496–2500.
   PubMed Web of Science ®Google Scholar
• Seely, S. E., H. Poso, and A. E. Pegg. 1982. Effect of androgens on turnover of ornithine decarboxylase in mouse kidney. J. Biol. Chem. 257:7549–7553.
   PubMedGoogle Scholar
• Sertich, G. J., and A. E. Pegg. 1987. Polyamine administration reduces ornithine decarboxylase activity without affecting its mRNA content. Biochem. Biophys. Res. Commun. 143:424–430.
   PubMedGoogle Scholar
• Simonsen, C. C., and A. D. Levinson. 1983. Isolation and expression of an altered mouse dihydrofolate reductase cDNA. Proc. Natl. Acad. Sci. USA 80:2495–2499.
   PubMed Web of Science ®Google Scholar
• Spiegelman, Β. M., M. Frank, and H. Green. 1983. Molecular cloning of mRNA from 3T3 adipocytes. J. Biol. Chem. 258:10083–10089.
   PubMed Web of Science ®Google Scholar
• Steglich, C., A. Grens, and I. E. Scheffler. 1985. Chinese hamster cells deficient in ornithine decarboxylase activity: reversion by gene amplification and by azacytidine treatment. Somatic Cell Mol. Genet. 11:11–23.
   PubMedGoogle Scholar
• Steglich, C., and I. E. Scheffler. 1982. An ornithine decarboxylase-deficient mutant of Chinese hamster ovary cells. J. Biol. Chem. 257:4603–4609.
   PubMedGoogle Scholar
• Tabor, C. W., and H. Tabor. 1984. Polyamines. Annu. Rev. Biochem. 53:749–790.
   PubMed Web of Science ®Google Scholar
• White, M. W., T. Kameji, A. E. Pegg, and D. R. Morris. 1987. Increased efficiency of translation of ornithine decarboxylase mRNA in mitogen-activated lymphocytes. FEBS Lett. 170:87–92.
   Google Scholar