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Volumn 579, Issue 11, 2005, Pages 2327-2333

Human mitochondrial peroxiredoxin 5 protects from mitochondrial DNA damages induced by hydrogen peroxide

Author keywords

Antioxidant enzyme; Mitochondria; Peroxide; Peroxiredoxin; Thioredoxin peroxidase

Indexed keywords

HYDROGEN PEROXIDE; METAL; MITOCHONDRIAL DNA; PEROXIREDOXIN; PEROXIREDOXIN 5; PLASMID DNA; REACTIVE OXYGEN METABOLITE; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG;

EID: 17644386166     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2005.03.027     Document Type: Article
Times cited : (125)

References (40)
  • 1
    • 0031032817 scopus 로고    scopus 로고
    • Mitochondrial DNA damage is more extensive and persists longer than nuclear DNA damage in human cells following oxidative stress
    • F.M. Yakes, and B. Van Houten Mitochondrial DNA damage is more extensive and persists longer than nuclear DNA damage in human cells following oxidative stress Proc. Natl. Acad. Sci. USA 94 1997 514 519
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 514-519
    • Yakes, F.M.1    Van Houten, B.2
  • 2
    • 0026680209 scopus 로고
    • Efficient protection against oxidative DNA damage in chromatin
    • M. Ljungman, and P.C. Hanawalt Efficient protection against oxidative DNA damage in chromatin Mol. Carcinog. 5 1992 264 269
    • (1992) Mol. Carcinog. , vol.5 , pp. 264-269
    • Ljungman, M.1    Hanawalt, P.C.2
  • 3
    • 0025869755 scopus 로고
    • Damage to the DNA bases in mammalian chromatin by hydrogen peroxide in the presence of ferric and cupric ions
    • M. Dizdaroglu, G. Rao, B. Halliwell, and E. Gajewski Damage to the DNA bases in mammalian chromatin by hydrogen peroxide in the presence of ferric and cupric ions Arch. Biochem. Biophys. 285 1991 317 324
    • (1991) Arch. Biochem. Biophys. , vol.285 , pp. 317-324
    • Dizdaroglu, M.1    Rao, G.2    Halliwell, B.3    Gajewski, E.4
  • 4
    • 0036639779 scopus 로고    scopus 로고
    • The mitochondrial DNA polymerase as a target of oxidative damage
    • M.A. Graziewicz, B.J. Day, and W.C. Copeland The mitochondrial DNA polymerase as a target of oxidative damage Nucleic Acids Res. 30 2002 2817 2824
    • (2002) Nucleic Acids Res. , vol.30 , pp. 2817-2824
    • Graziewicz, M.A.1    Day, B.J.2    Copeland, W.C.3
  • 5
    • 0036570012 scopus 로고    scopus 로고
    • Repair of oxidative DNA damage in nuclear and mitochondrial DNA, and some changes with aging in mammalian cells
    • V.A. Bohr Repair of oxidative DNA damage in nuclear and mitochondrial DNA, and some changes with aging in mammalian cells Free Radic. Biol. Med. 32 2002 804 812
    • (2002) Free Radic. Biol. Med. , vol.32 , pp. 804-812
    • Bohr, V.A.1
  • 6
    • 0033525773 scopus 로고    scopus 로고
    • Mitochondrial diseases in man and mouse
    • D.C. Wallace Mitochondrial diseases in man and mouse Science 283 1999 1482 1488
    • (1999) Science , vol.283 , pp. 1482-1488
    • Wallace, D.C.1
  • 8
    • 0028072911 scopus 로고
    • Thioredoxin-dependent peroxide reductase from yeast
    • H.Z. Chae, S.J. Chung, and S.G. Rhee Thioredoxin-dependent peroxide reductase from yeast J. Biol. Chem. 269 1994 27670 27678
    • (1994) J. Biol. Chem. , vol.269 , pp. 27670-27678
    • Chae, H.Z.1    Chung, S.J.2    Rhee, S.G.3
  • 9
    • 0034648827 scopus 로고    scopus 로고
    • Peroxynitrite reductase activity of bacterial peroxiredoxins
    • R. Bryk, P. Griffin, and C. Nathan Peroxynitrite reductase activity of bacterial peroxiredoxins Nature 407 2000 211 215
    • (2000) Nature , vol.407 , pp. 211-215
    • Bryk, R.1    Griffin, P.2    Nathan, C.3
  • 12
    • 0028260177 scopus 로고
    • Purification and characterization of a substrate protein for mitochondrial ATP-dependent protease in bovine adrenal cortex
    • S. Watabe, H. Kohno, H. Kouyama, T. Hiroi, N. Yago, and T. Nakazawa Purification and characterization of a substrate protein for mitochondrial ATP-dependent protease in bovine adrenal cortex J. Biochem. (Tokyo) 115 1994 648 654
    • (1994) J. Biochem. (Tokyo) , vol.115 , pp. 648-654
    • Watabe, S.1    Kohno, H.2    Kouyama, H.3    Hiroi, T.4    Yago, N.5    Nakazawa, T.6
  • 13
    • 0346056899 scopus 로고    scopus 로고
    • Overexpression of human peroxiredoxin 5 in subcellular compartments of Chinese hamster ovary cells: Effects on cytotoxicity and DNA damage caused by peroxides
    • I. Banmeyer, C. Marchand, C. Verhaeghe, B. Vucic, J.F. Rees, and B. Knoops Overexpression of human peroxiredoxin 5 in subcellular compartments of Chinese hamster ovary cells: effects on cytotoxicity and DNA damage caused by peroxides Free Radic. Biol. Med. 36 2004 65 77
    • (2004) Free Radic. Biol. Med. , vol.36 , pp. 65-77
    • Banmeyer, I.1    Marchand, C.2    Verhaeghe, C.3    Vucic, B.4    Rees, J.F.5    Knoops, B.6
  • 14
    • 2542504409 scopus 로고    scopus 로고
    • Peroxiredoxin-null yeast cells are hypersensitive to oxidative stress and are genomically unstable
    • C.M. Wong, K.L. Siu, and D.Y. Jin Peroxiredoxin-null yeast cells are hypersensitive to oxidative stress and are genomically unstable J. Biol. Chem. 279 2004 23207 23213
    • (2004) J. Biol. Chem. , vol.279 , pp. 23207-23213
    • Wong, C.M.1    Siu, K.L.2    Jin, D.Y.3
  • 15
    • 0141482059 scopus 로고    scopus 로고
    • A genomewide screen in Saccharomyces cerevisiae for genes that suppress the accumulation of mutations
    • M.E. Huang, A.G. Rio, A. Nicolas, and R.D. Kolodner A genomewide screen in Saccharomyces cerevisiae for genes that suppress the accumulation of mutations Proc. Natl. Acad. Sci. USA 100 2003 11529 11534
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 11529-11534
    • Huang, M.E.1    Rio, A.G.2    Nicolas, A.3    Kolodner, R.D.4
  • 16
    • 0001015125 scopus 로고    scopus 로고
    • Identification of a new type of mammalian peroxiredoxin that forms an intramolecular disulfide as a reaction intermediate
    • M.S. Seo, S.W. Kang, K. Kim, I.C. Baines, T.H. Lee, and S.G. Rhee Identification of a new type of mammalian peroxiredoxin that forms an intramolecular disulfide as a reaction intermediate J. Biol. Chem. 275 2000 20346 20354
    • (2000) J. Biol. Chem. , vol.275 , pp. 20346-20354
    • Seo, M.S.1    Kang, S.W.2    Kim, K.3    Baines, I.C.4    Lee, T.H.5    Rhee, S.G.6
  • 18
    • 4744351605 scopus 로고    scopus 로고
    • Expression of peroxiredoxins in bovine oocytes and embryos produced in vitro
    • G. Leyens, B. Knoops, and I. Donnay Expression of peroxiredoxins in bovine oocytes and embryos produced in vitro Mol. Reprod. Dev. 69 2004 243 251
    • (2004) Mol. Reprod. Dev. , vol.69 , pp. 243-251
    • Leyens, G.1    Knoops, B.2    Donnay, I.3
  • 19
    • 0027284395 scopus 로고
    • Strand breaks in DNA induced by a thiol/Fe(III)/O2 mixed-function oxidase system and its protection by a yeast antioxidant protein
    • S.J. Kwon, K. Kim, I.H. Kim, I.K. Yoon, and J.W. Park Strand breaks in DNA induced by a thiol/Fe(III)/O2 mixed-function oxidase system and its protection by a yeast antioxidant protein Biochem. Biophys. Res. Commun. 192 1993 772 777
    • (1993) Biochem. Biophys. Res. Commun. , vol.192 , pp. 772-777
    • Kwon, S.J.1    Kim, K.2    Kim, I.H.3    Yoon, I.K.4    Park, J.W.5
  • 20
    • 0035943382 scopus 로고    scopus 로고
    • Crystal structure of human peroxiredoxin 5, a novel type of mammalian peroxiredoxin at 1.5 Å resolution
    • J.P. Declercq, C. Evrard, A. Clippe, D. Vander Stricht, A. Bernard, and B. Knoops Crystal structure of human peroxiredoxin 5, a novel type of mammalian peroxiredoxin at 1.5 Å resolution J. Mol. Biol. 311 2001 751 759
    • (2001) J. Mol. Biol. , vol.311 , pp. 751-759
    • Declercq, J.P.1    Evrard, C.2    Clippe, A.3    Vander Stricht, D.4    Bernard, A.5    Knoops, B.6
  • 23
    • 0036355070 scopus 로고    scopus 로고
    • Measuring oxidative mtDNA damage and repair using quantitative PCR
    • J.H. Santos, B.S. Mandavilli, and B. Van Houten Measuring oxidative mtDNA damage and repair using quantitative PCR Methods Mol. Biol. 197 2002 159 176
    • (2002) Methods Mol. Biol. , vol.197 , pp. 159-176
    • Santos, J.H.1    Mandavilli, B.S.2    Van Houten, B.3
  • 24
    • 0023929362 scopus 로고
    • The isolation and purification of a specific protector protein which inhibits enzyme inactivation by a thiol/Fe(III)/O2 mixed-function oxidation system
    • K. Kim, I.H. Kim, K.Y. Lee, S.G. Rhee, and E.R. Stadtman The isolation and purification of a specific protector protein which inhibits enzyme inactivation by a thiol/Fe(III)/O2 mixed-function oxidation system J. Biol. Chem. 263 1988 4704 4711
    • (1988) J. Biol. Chem. , vol.263 , pp. 4704-4711
    • Kim, K.1    Kim, I.H.2    Lee, K.Y.3    Rhee, S.G.4    Stadtman, E.R.5
  • 25
    • 0038799736 scopus 로고    scopus 로고
    • Oxidative DNA damage: Mechanisms, mutation, and disease
    • M.S. Cooke, M.D. Evans, M. Dizdaroglu, and J. Lunec Oxidative DNA damage: mechanisms, mutation, and disease FASEB J. 17 2003 1195 1214
    • (2003) FASEB J. , vol.17 , pp. 1195-1214
    • Cooke, M.S.1    Evans, M.D.2    Dizdaroglu, M.3    Lunec, J.4
  • 27
    • 0347926089 scopus 로고    scopus 로고
    • NLS bioconjugates for targeting therapeutic genes to the nucleus
    • V. Escriou, M. Carriere, D. Scherman, and P. Wils NLS bioconjugates for targeting therapeutic genes to the nucleus Adv. Drug Deliv. Rev. 55 2003 295 306
    • (2003) Adv. Drug Deliv. Rev. , vol.55 , pp. 295-306
    • Escriou, V.1    Carriere, M.2    Scherman, D.3    Wils, P.4
  • 28
    • 0022393446 scopus 로고
    • Nonenzymatic cleavage of proteins by reactive oxygen species generated by dithiothreitol and iron
    • K. Kim, S.G. Rhee, and E.R. Stadtman Nonenzymatic cleavage of proteins by reactive oxygen species generated by dithiothreitol and iron J. Biol. Chem. 260 1985 15394 15397
    • (1985) J. Biol. Chem. , vol.260 , pp. 15394-15397
    • Kim, K.1    Rhee, S.G.2    Stadtman, E.R.3
  • 29
    • 0024815224 scopus 로고
    • Urinary 8-hydroxy-2′-deoxyguanosine as a biological marker of in vivo oxidative DNA damage
    • M.K. Shigenaga, C.J. Gimeno, and B.N. Ames Urinary 8-hydroxy-2′- deoxyguanosine as a biological marker of in vivo oxidative DNA damage Proc. Natl. Acad. Sci. USA 86 1989 9697 9701
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 9697-9701
    • Shigenaga, M.K.1    Gimeno, C.J.2    Ames, B.N.3
  • 30
    • 0037449724 scopus 로고    scopus 로고
    • Cell sorting experiments link persistent mitochondrial DNA damage with loss of mitochondrial membrane potential and apoptotic cell death
    • J.H. Santos, L. Hunakova, Y. Chen, C. Bortner, and B. Van Houten Cell sorting experiments link persistent mitochondrial DNA damage with loss of mitochondrial membrane potential and apoptotic cell death J. Biol. Chem. 278 2003 1728 1734
    • (2003) J. Biol. Chem. , vol.278 , pp. 1728-1734
    • Santos, J.H.1    Hunakova, L.2    Chen, Y.3    Bortner, C.4    Van Houten, B.5
  • 31
    • 4544356659 scopus 로고    scopus 로고
    • Effect of DNA damage on PCR amplification efficiency with the relative threshold cycle method
    • J.A. Sikorsky, D.A. Primerano, T.W. Fenger, and J. Denvir Effect of DNA damage on PCR amplification efficiency with the relative threshold cycle method Biochem. Biophys. Res. Commun. 323 2004 823 830
    • (2004) Biochem. Biophys. Res. Commun. , vol.323 , pp. 823-830
    • Sikorsky, J.A.1    Primerano, D.A.2    Fenger, T.W.3    Denvir, J.4
  • 32
    • 0037101879 scopus 로고    scopus 로고
    • Ferritin, iron homeostasis, and oxidative damage
    • P. Arosio, and S. Levi Ferritin, iron homeostasis, and oxidative damage Free Radic. Biol. Med. 33 2002 457 463
    • (2002) Free Radic. Biol. Med. , vol.33 , pp. 457-463
    • Arosio, P.1    Levi, S.2
  • 33
    • 0031441858 scopus 로고    scopus 로고
    • Preferential mitochondrial DNA injury caused by glucose oxidase as a steady generator of hydrogen peroxide in human fibroblasts
    • J.J. Salazar, and B. Van Houten Preferential mitochondrial DNA injury caused by glucose oxidase as a steady generator of hydrogen peroxide in human fibroblasts Mutat. Res. 385 1997 139 149
    • (1997) Mutat. Res. , vol.385 , pp. 139-149
    • Salazar, J.J.1    Van Houten, B.2
  • 34
    • 3242796654 scopus 로고    scopus 로고
    • Overexpression of antioxidant enzyme peroxiredoxin 5 protects human tendon cells against apoptosis and loss of cellular function during oxidative stress
    • J. Yuan, G.A. Murrell, A. Trickett, M. Landtmeters, B. Knoops, and M.X. Wang Overexpression of antioxidant enzyme peroxiredoxin 5 protects human tendon cells against apoptosis and loss of cellular function during oxidative stress Biochim. Biophys. Acta 1693 2004 37 45
    • (2004) Biochim. Biophys. Acta , vol.1693 , pp. 37-45
    • Yuan, J.1    Murrell, G.A.2    Trickett, A.3    Landtmeters, M.4    Knoops, B.5    Wang, M.X.6
  • 35
    • 0030221272 scopus 로고    scopus 로고
    • Inhibition of hydroperoxide-induced DNA single-strand breakage by 1,10-phenanthroline in HL-60 cells: Implications for iron speciation
    • R.W. Byrnes Inhibition of hydroperoxide-induced DNA single-strand breakage by 1,10-phenanthroline in HL-60 cells: implications for iron speciation Arch. Biochem. Biophys. 332 1996 70 78
    • (1996) Arch. Biochem. Biophys. , vol.332 , pp. 70-78
    • Byrnes, R.W.1
  • 36
    • 0038023096 scopus 로고    scopus 로고
    • Oxidative damage of Chinese hamster fibroblasts induced by t-butyl hydroperoxide and by X-rays
    • M. Bryszewska, A. Piasecka, L.B. Zavodnik, L. Distel, and H. Schussler Oxidative damage of Chinese hamster fibroblasts induced by t-butyl hydroperoxide and by X-rays Biochim. Biophys. Acta 1621 2003 285 291
    • (2003) Biochim. Biophys. Acta , vol.1621 , pp. 285-291
    • Bryszewska, M.1    Piasecka, A.2    Zavodnik, L.B.3    Distel, L.4    Schussler, H.5
  • 37
    • 0032695092 scopus 로고    scopus 로고
    • The effect of oxidative stress induced by t-butyl hydroperoxide on the structural dynamics of membrane proteins of Chinese hamster fibroblasts
    • V. Mazhul, D. Shcherbin, I. Zavodnik, K. Rekawiecka, and M. Bryszewska The effect of oxidative stress induced by t-butyl hydroperoxide on the structural dynamics of membrane proteins of Chinese hamster fibroblasts Cell. Biol. Int. 23 1999 345 350
    • (1999) Cell. Biol. Int. , vol.23 , pp. 345-350
    • Mazhul, V.1    Shcherbin, D.2    Zavodnik, I.3    Rekawiecka, K.4    Bryszewska, M.5
  • 38
    • 0037452679 scopus 로고    scopus 로고
    • Electrophile and oxidant damage of mitochondrial DNA leading to rapid evolution of homoplasmic mutations
    • E. Mambo, X. Gao, Y. Cohen, Z. Guo, P. Talalay, and D. Sidransky Electrophile and oxidant damage of mitochondrial DNA leading to rapid evolution of homoplasmic mutations Proc. Natl. Acad. Sci. USA 100 2003 1838 1843
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 1838-1843
    • Mambo, E.1    Gao, X.2    Cohen, Y.3    Guo, Z.4    Talalay, P.5    Sidransky, D.6
  • 40
    • 0345528189 scopus 로고    scopus 로고
    • Cloning of bovine peroxiredoxins-gene expression in bovine tissues and amino acid sequence comparison with rat, mouse and primate peroxiredoxins
    • G. Leyens, I. Donnay, and B. Knoops Cloning of bovine peroxiredoxins-gene expression in bovine tissues and amino acid sequence comparison with rat, mouse and primate peroxiredoxins Comp. Biochem. Physiol. B 136 2003 943 955
    • (2003) Comp. Biochem. Physiol. B , vol.136 , pp. 943-955
    • Leyens, G.1    Donnay, I.2    Knoops, B.3


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