Post-transcriptional control of increased hepatic catalase gene expression in response to oxidative stress

REFERENCES

• Halliwell B, Grootveld M. The measurement of free radical reactions in humans. Some thoughts for future experimentation. FEBS Lett 1987; 213: 9–14.
   PubMed Web of Science ®Google Scholar
• Sies H. Strategies of antioxidant defense. Eur J Biochem 1993; 215: 213–219.
   PubMedGoogle Scholar
• Fridovich I, Freeman B. Antioxidant defenses in the lung. Annu Rev Physiol 1986; 48: 693–702.
   PubMed Web of Science ®Google Scholar
• Aebi H E, Wyss S R. In: Stanbury J B, Wyngaarden J B, Fredrickson D S eds. The Metabolic Basis of Disease. New York: McGraw-Hill Publications, 1978: 1792–1807.
   Google Scholar
• Nemali M R, Usuda N, Reddy M K et al. Comparison of constitutive and inducible levels of expression of peroxisomal β-oxidation and catalase genes in liver and extrahepatic tissues of rat. Cancer Res 1988; 48: 5316–5324.
   PubMed Web of Science ®Google Scholar
• Semsei I, Rao G, Richardson A. Changes in the expression of superoxide dismutase and catalase as a function of age and dietary restriction. Biochem Biophys Res Commun 1989; 164: 620–625.
   PubMed Web of Science ®Google Scholar
• Sato K, Ito K, Kohara H, Yamaguchi Y, Adachi K, Endo H. Negative regulation of catalase gene expression in hepatoma cells. Mol Cell Biol 1992; 12: 2525–2533.
   PubMed Web of Science ®Google Scholar
• Reimer D L, Bailley J, Singh S M. Complete cDNA and 5′ genomic sequences and multilevel regulation of the mouse catalase gene. Genomics 1994; 21: 325–336.
   PubMed Web of Science ®Google Scholar
• Clerch L B, Iqbal J, Massaro D. Perinatal rat lung catalase gene expression: influence of corticosteroid and hyperoxia. Am J Physiol 1991; 260: (Lung Cell Mol Physiol 4): L428–L433.
   PubMed Web of Science ®Google Scholar
• Akman S A, Forrest G, Chu F-F, Doroshow J H. Resistance to hydrogen peroxide associated with altered catalase mRNA stability in MCF7 breast cancer cells. Biochim Biophys Acta 1989; 1009: 70–74.
   PubMed Web of Science ®Google Scholar
• Tacchini L, Pogliaghi G, Radice L, Anzon E, Bernelli-Zazzera A. Differential activation of heat-shock and oxidation-specific stress genes in chemically induced oxidative stress. Biochem J 1995; 309: 453–459.
   PubMed Web of Science ®Google Scholar
• Cairo G, Tacchini L, Pogliaghi G, Anzon E, Tomasi A, Bernelli-Zazzera A. Induction of ferritin synthesis by oxidative stress. Transcriptional and post-transcriptional regulation by expansion of the ‘free’ iron pool. J Biol Chem 1995; 270; 700–703.
   PubMed Web of Science ®Google Scholar
• Balla J, Jacob H S, Balla G, Nath K, Eaton J W, Vercellotti G M. Endothelial-cell heme uptake from heme proteins: induction of sensitization and desensitization to oxidant damage. Proc Natl Acad Sci USA 1993; 90: 9285–9289.
   PubMed Web of Science ®Google Scholar
• Vile G F, Tyrrel R M. Oxidative stress resulting from ultraviolet A irradiation of human skin fibroblasts leads to a heme oxygenase-dependent increase in ferritin. J Biol Chem 1993; 268: 14678–14681.
   PubMed Web of Science ®Google Scholar
• Aust S D, Chignell C F, Bray T M, Kalyanaraman B, Mason R P. Free radicals in toxicology. Toxicol Appl Pharmacol 1993; 120: 168–178.
   PubMed Web of Science ®Google Scholar
• Griffith O W. Determination of glutathione disulfide using glutathione reductase and 2-vinylpyridine. Anal Biochem 1980; 106: 207–212.
   PubMed Web of Science ®Google Scholar
• Wall S R, Fliss H, Korecky B. Role of catalase in myocardial protection against ischemia in heat shocked rats. Mol Cell Biochem 1993; 129: 187–194.
   PubMed Web of Science ®Google Scholar
• Pietrangelo A, Rocchi E, Casalgrandi G et al. Regulation of transferrin, transferrin receptor and ferritin genes in human duodenum. Gastroenterology 1992; 102: 802–809.
   PubMed Web of Science ®Google Scholar
• Cairo G, Pietrangelo A. Nitric-oxide-mediated activation of iron-regulatory protein controls hepatic metabolism during acute inflammation. Eur J Biochem 1995; 232: 358–363.
   PubMedGoogle Scholar
• Cairo G, Pietrangelo A. Transferrin receptor gene expression during rat liver regeneration: evidence for post-transcriptional regulation by IRFB, a second IRE-binding protein. J Biol Chem 1994; 269: 6405–6409.
   PubMed Web of Science ®Google Scholar
• Furuta S, Hayashi H, Hijikata M, Miyazawa S, Osumi T, Hashimoto T. Complete nucleotide sequence of cDNA and deduced amino acid sequence of rat liver catalase. Proc Natl Acad Sci USA 1986; 83: 313–317
   PubMed Web of Science ®Google Scholar
• Clerch L B. A 3′ untranslated region of catalase mRNA composed of a stem-loop and dinucleotide repeat elements binds a 69-κDa redox-sensitive protein. Arch Biochem Biophys 1995; 317: 267–274.
   PubMed Web of Science ®Google Scholar
• Shibahara S, Muller R, Taguchi H, Yoshida T. Cloning and expression of cDNA for rat heme oxygenase. Proc Natl Acad Sci USA 1985; 82: 7865–7869.
   PubMed Web of Science ®Google Scholar
• Clerch L B, Massaro D. Oxidation-reduction-sensitive binding of lung protein to rat catalase mRNA. J Biol Chem 1992; 267: 2853–2855.
   PubMed Web of Science ®Google Scholar
• Jones G M, Sanford K K, Parshad R, Gantt R, Price F M, Tarone R E. Influence of added catalase on chromosome stability and neoplastic transformation of mouse cells in culture. Br J Cancer 1985; 52: 583–590.
   PubMed Web of Science ®Google Scholar
• Lin F, Jackson V E, Girotti A W. Amplification and hyperexpression of the catalase gene in selenoperoxidase-deficient leukemia cells. Arch Biochem Biophys 1995; 317: 7–18.
   PubMed Web of Science ®Google Scholar
• Shaffer J B, Sutton R B, Bewley G C. Isolation of a cDNA clone for murine catalase and analysis of an acatalasemic mutant. J Biol Chem 1987; 262: 12908–12911.
   PubMed Web of Science ®Google Scholar
• Storz G, Tartaglia L A, Ames B N. Transcriptional regulator of oxidative stress-inducible genes: direct activation by oxidation. Science 1990; 248: 189–194.
   PubMed Web of Science ®Google Scholar
• Romaniuk P J, Uhlenbeck O C. Nucleoside and nucleotide inactivation of R17 coat protein: evidence for a transient covalent RNA-protein bond. Biochemistry 1985; 24: 4239–4244.
   PubMed Web of Science ®Google Scholar
• Chu E, Voeller D M, Morrison P F et al. The effect of reducing reagents on binding of thymidilate synthase protein to thymidilate synthase messenger RNA. J Biol Chem 1994; 269: 20289–20293.
   PubMed Web of Science ®Google Scholar
• Klausner R D, Rouault T A, Harford J B. Regulating the fate of mRNA: the control of cellular iron metabolism. Cell 1993; 72: 19–28.
   PubMed Web of Science ®Google Scholar
• Demple B, Amabile-Cuevas C F. Redox redux: the control of oxidative stress responses. Cell 1991; 67: 837–839.
   PubMed Web of Science ®Google Scholar
• Toledano M B, Kullik I, Trinh F, Baird P T, Schneider T D, Store G. Redox-dependent shift of OxyR-DNA contacts along an extended DNA-binding site: a mechanism for differential promoter selection. Cell 1994; 78: 897–909.
   PubMed Web of Science ®Google Scholar
• Fazzone H, Wangner A, Clerch L B. Rat lung contains a developmentally regulated manganese superoxide dismutase mRNA-binding protein. J Clin Invest 1993; 92: 1278–1281.
   PubMed Web of Science ®Google Scholar