Oxidative modification of ferritin induced by hydrogen peroxide
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Excess free iron generates oxidative stress that may contribute to the pathogenesis of various causes of neurodegenerative diseases. In this study, we assessed the modification of ferritin induced by H₂O₂. When ferritin was incubated with H₂O₂, the degradation of ferritin L-chain increased with the H₂O₂concentration whereas ferritin H-chain was remained. Free radical scavengers, azide, thiourea, and N-acetyl-L-cysteine suppressed the H₂O₂-mediated ferritin modification. The iron specific chelator,deferoxamine, effectively prevented H₂O₂-mediated ferritin degradation in modified ferritin. The release of iron ions from ferritin was increased in H₂O₂concentration-dependent manner. The present results suggest that free radicals may play a role in the modification and iron releasing of ferritin by H₂O₂. It is assumed that oxidative damage of ferritin by H₂O₂may induce the increase of iron content in cells and subsequently lead to the deleterious condition. [BMB reports 2011; 44(3): 165-169]
Abstract
Excess free iron generates oxidative stress that may contribute to the pathogenesis of various causes of neurodegenerative diseases. In this study, we assessed the modification of ferritin induced by H₂O₂. When ferritin was incubated with H₂O₂, the degradation of ferritin L-chain increased with the H₂O₂concentration whereas ferritin H-chain was remained. Free radical scavengers, azide, thiourea, and N-acetyl-L-cysteine suppressed the H₂O₂-mediated ferritin modification. The iron specific chelator,deferoxamine, effectively prevented H₂O₂-mediated ferritin degradation in modified ferritin. The release of iron ions from ferritin was increased in H₂O₂concentration-dependent manner. The present results suggest that free radicals may play a role in the modification and iron releasing of ferritin by H₂O₂. It is assumed that oxidative damage of ferritin by H₂O₂may induce the increase of iron content in cells and subsequently lead to the deleterious condition. [BMB reports 2011; 44(3): 165-169]
참고문헌 (26)
- Knovich, M. A, "Ferritin for the clinician", Blood Rev, 23, pp.95~104 (2009)
- Halliwell, B, "Free Radicals in Biology and Medicine (Fourth Edition)" (2007), Oxford University Press
- Galkina, E, "Immune and inflammatory mechanisms of atherosclerosis", Annu. Rev. Immunol, 27, pp.165~197 (2009)
- Maynarol, S, "Base excision repair of oxidative DNA damage and association with cancer and aging", Carcinogenesis, 30, pp.2~10 (2009)
- Pflueger, A, "Role of oxidative stress in contrast-induced acute kidney injury in diabetes mellitus", Med. Sci. Monit, 15, pp.125~136 (2009)
- Galaris, D, "Oxidative stress and iron homeostasis: mechanistic and health aspects", Crit. Rev. Clin. Lab. Sci, 45, pp.1~23 (2008)
- Torti, F. M, "Regulation of ferritin genes and protein", Blood, 99, pp.3505~3516 (2002)
- Thomas, M, "Neurodegenerative disease and iron storage in the brain", Curr. Opin. Neurol, 17, pp.437~442 (2004)
- Zecca, L, "Iron, brain ageing and neurodegenerative disorders", Nat. Rev. Neurosci, 5, pp.863~873 (2004)
- Wallis, L. I, "MRI assessment of basal ganglia iron deposition in Parkinson’s disease", J. Magn. Reson Imaging, 28, pp.1061~1067 (2008)
- Double, K. L, "In vitro studies of ferritin iron release and neurotoxicity", J. Neurochem, 70, pp.2492~2499 (1998)
- Schuessler, H, "Oxygen effect in the radiolysis of proteins. Part 2. Bovine serum albumin", Int. J. Radiat. Biol, 45, pp.267~281 (1984)
- Hunt, J. V, "Free radical-mediated degradation of proteins: the protective and deleterious effects of membranes", Biochem. Biophys. Res. Commun, 162, pp.1076~1084 (1989)
- Stadtman, E. R, "Reactive oxygen- mediated protein oxidation in aging and disease", Chem. Res. Toxicol, 10, pp.485~494 (1997)
- Robello, E, "Labile iron pool and ferritin content in developing rat brain gamma- irradiated in utero", Neurotoxicology, 30, pp.430~435 (2009)
- Kim, K. S, "Aggregation of α-synuclein induced by the Cu,Zn-superoxide dismutase and hydrogen peroxide system", Free Radic. Biol. Med, 32, pp.544~550 (2002)
- Kang,J.H, "Ferritin enhances salsolinol-mediated DNA strand braekage: protection by carnosine and related compounds", Toxicol. Lett, 188, pp.20~25 (2009)
- Davies, K. J, "Protein damage and degradation by oxygen radicals. II. Modification of amino acids", J. Biol. Chem, 262, pp.9902~9907 (1987)
- Kang, J. H, "Oxidative modification of human ceruloplasmin by peroxyl radicals", Biochem. Biophys. Acta, 1568, pp.30~36 (2001)
- Granier, T, "Structural description of the active sites of mouse L-chain ferritin at 1.2 A resolution", J. Biol. Inorg. Chem, 8, pp.105~111 (2003)
- Flaherty, J. T, "Reperfusion injury", Free Radic. Biol. Med, 5, pp.409~419 (1988)
- Zweier, J. L, "Measurement and characterization of postischemic free radical generation in the isolated perfused heart", J. Biol. Chem, 264, pp.18890~18895 (1989)
- Smith, P. K, "Measurement of protein using bicinchoninic acid", Anal. Biochem, 150, pp.76~85 (1985)
- Laemmli, U. K, "Cleavage of structural proteins during the assembly of the head of bacteriophage T4", Nature, 227, pp.680~685 (1970)
- Pieroni, L, "Comparison of bathophenanthroline sulfonate and ferene as chromogens in colorimetric measurement of low hepatic iron concentration", Clin. Chem, 47, pp.2059~2061 (2001)
- Hugli, T, E, "Determination of the tryptophan content of proteins by ion exchange chromatography of alkaline hydrolysates", J. Biol. Chem, 247, pp.2828~2834 (1972)