Extracellular H₂O₂ and not superoxide determines the compartment-specific activation of transferrin receptor by iron regulatory protein 1

References

• Frausto da Silva JJR, Williams RJP. The biological chemistry of the elements: The inorganic chemistry of life. Vol. 21. Oxford: Clarendon; 1991. p 319–368.
   Google Scholar
• Halliwell B, Gutteridge JM. Role of free radicals and catalytic metal ions in human disease: An overview. Methods Enzymol 1990;186:1–85.
   PubMed Web of Science ®Google Scholar
• Beinert H, Holm RH, Munck E. Iron—sulfur clusters: nature's modular, multipurpose structures. Science 1997;277: 653–659.
   Google Scholar
• Haile DJ, Rouault TA, Harford JB, Kennedy MC, Blondin GA, Beinert H, Klausner RD. Cellular regulation of the iron-responsive element binding protein: Disassembly of the cubane iron—sulfur cluster results in high- affinity RNA binding. Proc Natl Acad Sci USA 1992;89:11735–11739.
   Google Scholar
• Rouault T, Klausner R. Regulation of iron metabolism in eukaryotes. Curr Top Cell Regul 1997;35:1–19.
   PubMedGoogle Scholar
• Hentze MW, Kuhn LC. Molecular control of vertebrate iron metabolism: mRNA-based regulatory circuits operated by iron, nitric oxide, and oxidative stress. Proc Natl Acad Sci USA 1996;93:8175–8182.
   PubMed Web of Science ®Google Scholar
• Pantopoulos K. Iron metabolism and the IRE/IRP regulatory system: An update. Ann NY Acad Sci 2004;1012:1–1315.
   PubMed Web of Science ®Google Scholar
• Pantopoulos K, Hentze MW. Rapid responses to oxidative stress mediated by iron regulatory protein. EMBO J 1995;14:2917–2924.
   PubMed Web of Science ®Google Scholar
• Pantopoulos K, Mueller S, Atzberger A, Ansorge W, Stremmel W, Hentze MW. Differences in the regulation of IRP-1 (iron regulatory protein-1) by extra- and intracelullar oxidative stress. J Biol Chem 1997;272:9802–9808.
   PubMed Web of Science ®Google Scholar
• Rost D, Hegediisch D, Mangin J, Riedel HD, Hebling U, Wang J, Pantopoulos K, Mueller S. Sustained non-toxic hydrogen peroxide induces iron uptake by transferrin receptor-1. Implications for the anemia of chronic disease. 2005 (submitted for publication).
   Google Scholar
• Miitze S, Hebling U, Stremmel W, Wang J, Arnhold J, Pantopoulos K, Mueller S. Myeloperoxidase-derived hypo-chlorous acid antagonizes the oxidative stress-mediated activation of iron regulatory protein 1. J Biol Chem 2003;278: 40542–40549.
   Google Scholar
• Martins EA, Robalinho RL, Meneghini R. Oxidative stress induces activation of a cytosolic protein responsible for control of iron uptake. Arch Biochem Biophys 1995;316: 128–134.
   Google Scholar
• Cairo G, Pietrangelo A. Nitric-oxide-mediated activation of iron-regulatory protein controls hepatic iron metabolism during acute inflammation. Eur J Biochem 1995;232: 358–363.
   PubMedGoogle Scholar
• Pantopoulos K, Weiss G, Hentze MW. Nitric oxide and oxidative stress (H202) control mammalian iron metabolism by different pathways. Mol Cell Biol 1996;16: 3781–3788.
   Google Scholar
• Mueller S, Pantopoulos K, Hübner CA, Stremmel W, Hentze MW. IRP1 activation by extracellular oxidative stress in the perfused rat liver. J Biol Chem 2001;276: 23192–23196.
   Google Scholar
• Cairo G, Castrusini E, Minotti G, Bernelli-Zazzera A. Superoxide and hydrogen peroxide-dependent inhibition of iron regulatory protein activity: A protective stratagem against oxidative injury. FASEB J 1996;10:1326–1335.
   Google Scholar
• Kennedy MC, Antholine WE, Beinert H. An EPR investi-gation of the products of the reaction of cytosolic and mitochondrial aconitases with nitric oxide. J Biol Chem 1997;272:20340–20347.
   Google Scholar
• Castro LA, Robalinho RL, Cayota A, Meneghini R, Radi R. Nitric oxide and peroxynitrite-dependent aconitase inacti-vation and iron-regulatory protein-1 activation in mammalian fibroblasts. Arch Biochem Biophys 1998;359: 215–224.
   Google Scholar
• Bouton C, Raveau M, Drapier JC. Modulation of iron regulatory protein functions, Further insights into the role of nitrogen- and oxygen-derived reactive species. J Biol Chem 1996;271:2300–2306.
   Google Scholar
• Hausladen A, Fridovich I. Superoxide and peroxynitrite inactivate aconitases, but nitric oxide does not. J Biol Chem 1994;269:29405–29408.
   PubMed Web of Science ®Google Scholar
• Baggiolini M, Theian M. In: Sies H, editor. Oxidative stress: Oxidants and antioxidants. London: Harcourt Braze Jovano-vich; 1991.
   Google Scholar
• Klebanoff SJ. In: Snyderman R, editor. In Inflammation: Basic principles and clinical correlates. New York: Raven Press; 1988. p 391–444.
   Google Scholar
• Klebanoff SJ. In: Grisham MB, editor. Peroxidases in chemistry and biology. Boca Raton of Florida: CRC Press; 1991. p 1–35.
   Google Scholar
• Caltagirone A, Weiss G, Pantopoulos K. Modulation of cellular iron metabolism by hydrogen peroxide, effects of H202 on the expression and function of iron-responsive element-containing mRNAs in B6 fibroblasts. J Biol Chem 2001;22: 22.
   Google Scholar
• De Freitas JM, Liba A, Meneghini R, Valentine JS, Gralla EB. Yeast lacking Cu-Zn superoxide dismutase show altered iron homeostasis. Role of oxidative stress in iron metabolism. J Biol Chem 2000;275:11645–11649.
   Google Scholar
• Srinivasan C, Liba A, Imlay JA, Valentine JS, Gralla EB. Yeast lacking superoxide dismutase(s) show elevated levels of free iron as measured by whole cell electron paramagnetic resonance. J Biol Chem 2000;275:29187–29192.
   Google Scholar
• Park JI, Grant CM, Davies MJ, Dawes IW. The cytoplasmic Cu,Zn superoxide dismutase of saccharomyces cerevisiae is required for resistance to freeze-thaw stress. Generation of free radicals during freezing and thawing. J Biol Chem 1998;273:22921–22928.
   Google Scholar
• Sturtz LA, Diekert K, Jensen LT, Lill R, Culotta VC. A fraction of yeast Cu,Zn-superoxide dismutase and its metallochaperone, CCS, localize to the intermembrane space of mitochondria. A physiological role for SOD1 in guarding against mitochondrial oxidative damage. J Biol Chem 2001;276: 38084–38089.
   Google Scholar
• Corson LB, Folmer J, Strain jj, Culotta VC, Cleveland DW. Oxidative stress and iron are implicated in fragmenting vacuoles of Saccharomyces cerevisiae lacking Cu,Zn-super-oxide dismutase. J Biol Chem 1999;274:27590–27596.
   Google Scholar
• Balzan R, Bannister WH, Hunter GJ, Bannister JV. Escherichia coli iron superoxide dismutase targeted to the mitochondria of yeast cells protects the cells against oxidative stress. Proc Natl Acad Sci USA 1995;92:4219–4223.
   Google Scholar
• Balzan R, Agius DR, Bannister WH. Cloned prokaryotic iron superoxide dismutase protects yeast cells against oxidative stress depending on mitochondrial location. Biochem Biophys Res Commun 1999;256:63–67.
   Google Scholar
• Missirlis F, Hu J, Kirby K, Hilliker AJ, Rouault TA, Phillips JP. Compartment-specific protection of iron-sulfur proteins by superoxide dismutase. J Biol Chem 2003;278:47365–47369.
   PubMed Web of Science ®Google Scholar
• Mueller S, Arnhold J. Fast and sensitive chemiluminescence determination of H202 concentration in stimulated human neutrophils. J Biolumin Chemilumin 1995;10:229–237.
   PubMedGoogle Scholar
• Mueller S. Sensitive and nonenzymatic measurement of hydrogen peroxide in biological systems. Free Radic Biol Med 2000;29:410–415.
   PubMed Web of Science ®Google Scholar
• Mueller S, Riedel HD, Stremmel W. Determination of catalase activity at physiological hydrogen peroxide concentrations. Anal Biochem 1997;245:55–60.
   Google Scholar
• Aebi H. Catalase in vitro. Method Enzymol 1984;105:121–126.
   PubMed Web of Science ®Google Scholar
• Dringen R, Kussmaul L, Hamprecht B. Detoxification of exogenous hydrogen peroxide and organic hydroperoxides by cultured astroglial cells assessed by microtiter plate assay. Brain Res Brain Res Protoc 1998;2:223–228.
   Google Scholar
• McCord JM, Fridovich I. Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein). J Biol Chem 1969;244:6049–6055.
   PubMed Web of Science ®Google Scholar
• Mueller S, Pantopoulos K. Activation of iron regulatory protein-1 (IRP1) by oxidative stress. Methods Enzymol 2002;348:324–337.
   PubMedGoogle Scholar
• Mueller S, Pantopoulos K, Hentze MW, Stremmel W. In: Stanley PE, editor. Bioluminescence and chemiluminescence: Molecular reporting with photons. Baffins Lane, Chichester, Sussex: John Wiley & Sons Ltd; 1997. p 338–341.
   Google Scholar
• Pantopoulos K, Hentze MW. Activation of iron regulatory protein-1 by oxidative stress in vitro. Proc Natl Acad Sci USA 1998;95:10559–10563.
   PubMed Web of Science ®Google Scholar
• Rossi F. The 02-forming NADPH oxidase of the phagocytes: nature, mechanism of activation and function. Biochim Biophys Acta 1986;853:65–89.
   PubMed Web of Science ®Google Scholar
• Guskova RA, Ivanov II, Kol'tover VK, Akhobadze VV, Rubin AB. Permeability of bilayer lipid membranes for superoxide (OD radicals. Biochim Biophys Acta 1984;778:579–585.
   Google Scholar
• Brazzolotto X, Gaillard J, Pantopoulos K, Hentze MW, Moulis JM. Human cytoplasmic aconitase (Iron regulatory protein 1) is converted into its [3Fe-45] form by hydrogen peroxide in vitro but is not activated for iron-responsive element binding. J Biol Chem 1999;274: 21625–21630.
   Google Scholar
• Flint DH, Tuminello JF, Emptage MH. The inactivation of Fe- S cluster containing hydro-lyases by superoxide. J Biol Chem 1993;268:22369–22376.
   Google Scholar
• Gardner PR, Fridovich I. Superoxide sensitivity of the Escherichia coli 6-phosphogluconate dehydratase. J Biol Chem 1991;266:1478–1483.
   PubMed Web of Science ®Google Scholar
• Gardner PR, Raineri I, Epstein LB, White CW. Superoxide radical and iron modulate aconitase activity in mammalian cells. J Biol Chem 1995;270:13399–13405.
   PubMed Web of Science ®Google Scholar
• Halliwell B, Gutteridge JMC. Free radicals in biology and medicine. Oxford: Clarendon Press; 1999.
   Google Scholar
• Gehring NH, Hentze MW, Pantopoulos K. Inactivation of both RNA binding and aconitase activities of iron regulatory protein-1 by quinone-induced oxidative stress. J Biol Chem 1999;274: 6219–6225.
   Google Scholar
• Wisnicka R, Krzepilko A, Wawryn J, Krawiec Z, Bilinski T. Protective role of superoxide dismutase in iron toxicity in yeast. Biochem Mol Biol Int 1998;44:635–641.
   Google Scholar
• Bilinski T. Oxygen toxicity and microbial evolution. Bio-Systems 1991;24:305–312.
   Google Scholar