메뉴 건너뛰기




Volumn 49, Issue 12, 2010, Pages 1892-1902

Mitochondrial peroxiredoxins are critical for the maintenance of redox state and the survival of adult Drosophila

Author keywords

Aging; Apoptosis; Drosophila; Free radicals; Glutathione; Mitochondria; Oxidative stress; Peroxiredoxin; Redox state; Thiol; Thioredoxin

Indexed keywords

CATALASE; GLUTATHIONE; PEROXIREDOXIN; PEROXIREDOXIN 3; PEROXIREDOXIN 5; THIOL; THIOREDOXIN; THIOREDOXIN REDUCTASE;

EID: 78650171689     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2010.09.014     Document Type: Article
Times cited : (36)

References (36)
  • 1
    • 39649091198 scopus 로고    scopus 로고
    • Drosophila peroxiredoxin 5 is the second gene in a dicistronic operon
    • K. Michalak, W.C. Orr, and S.N. Radyuk Drosophila peroxiredoxin 5 is the second gene in a dicistronic operon Biochem. Biophys. Res. Commun. 368 2008 273 278
    • (2008) Biochem. Biophys. Res. Commun. , vol.368 , pp. 273-278
    • Michalak, K.1    Orr, W.C.2    Radyuk, S.N.3
  • 3
    • 2142857696 scopus 로고    scopus 로고
    • Polypeptides differentially expressed in imaginal discs define the peroxiredoxin family of genes in Drosophila
    • J. Rodriguez, M. Agudo, J. Van Damme, J. Vandekerckhove, and J.F. Santaren Polypeptides differentially expressed in imaginal discs define the peroxiredoxin family of genes in Drosophila Eur. J. Biochem./FEBS 267 2000 487 497
    • (2000) Eur. J. Biochem./FEBS , vol.267 , pp. 487-497
    • Rodriguez, J.1    Agudo, M.2    Van Damme, J.3    Vandekerckhove, J.4    Santaren, J.F.5
  • 4
    • 64249103993 scopus 로고    scopus 로고
    • Peroxiredoxin 5 confers protection against oxidative stress and apoptosis and also promotes longevity in Drosophila
    • S.N. Radyuk, K. Michalak, V.I. Klichko, J. Benes, I. Rebrin, R.S. Sohal, and W.C. Orr Peroxiredoxin 5 confers protection against oxidative stress and apoptosis and also promotes longevity in Drosophila Biochem. J. 419 2009 437 445
    • (2009) Biochem. J. , vol.419 , pp. 437-445
    • Radyuk, S.N.1    Michalak, K.2    Klichko, V.I.3    Benes, J.4    Rebrin, I.5    Sohal, R.S.6    Orr, W.C.7
  • 5
    • 0001445231 scopus 로고    scopus 로고
    • Characterization of three isoforms of mammalian peroxiredoxin that reduce peroxides in the presence of thioredoxin
    • H.Z. Chae, H.J. Kim, S.W. Kang, and S.G. Rhee Characterization of three isoforms of mammalian peroxiredoxin that reduce peroxides in the presence of thioredoxin Diab. Res. Clin. Pract. 45 1999 101 112
    • (1999) Diab. Res. Clin. Pract. , vol.45 , pp. 101-112
    • Chae, H.Z.1    Kim, H.J.2    Kang, S.W.3    Rhee, S.G.4
  • 6
    • 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
  • 7
    • 0033106406 scopus 로고    scopus 로고
    • A novel human DNA-binding protein with sequence similarity to a subfamily of redox proteins which is able to repress RNA-polymerase-III-driven transcription of the Alu-family retroposons in vitro
    • A. Kropotov, V. Sedova, V. Ivanov, N. Sazeeva, A. Tomilin, R. Krutilina, S.L. Oei, J. Griesenbeck, G. Buchlow, and N. Tomilin A novel human DNA-binding protein with sequence similarity to a subfamily of redox proteins which is able to repress RNA-polymerase-III-driven transcription of the Alu-family retroposons in vitro Eur. J. Biochem./FEBS 260 1999 336 346
    • (1999) Eur. J. Biochem./FEBS , vol.260 , pp. 336-346
    • Kropotov, A.1    Sedova, V.2    Ivanov, V.3    Sazeeva, N.4    Tomilin, A.5    Krutilina, R.6    Oei, S.L.7    Griesenbeck, J.8    Buchlow, G.9    Tomilin, N.10
  • 9
    • 4744373181 scopus 로고    scopus 로고
    • Peroxiredoxin III, a mitochondrion-specific peroxidase, regulates apoptotic signaling by mitochondria
    • T.S. Chang, C.S. Cho, S. Park, S. Yu, S.W. Kang, and S.G. Rhee Peroxiredoxin III, a mitochondrion-specific peroxidase, regulates apoptotic signaling by mitochondria J. Biol. Chem. 279 2004 41975 41984
    • (2004) J. Biol. Chem. , vol.279 , pp. 41975-41984
    • Chang, T.S.1    Cho, C.S.2    Park, S.3    Yu, S.4    Kang, S.W.5    Rhee, S.G.6
  • 10
    • 17644386166 scopus 로고    scopus 로고
    • Human mitochondrial peroxiredoxin 5 protects from mitochondrial DNA damages induced by hydrogen peroxide
    • I. Banmeyer, C. Marchand, A. Clippe, and B. Knoops Human mitochondrial peroxiredoxin 5 protects from mitochondrial DNA damages induced by hydrogen peroxide FEBS Lett. 579 2005 2327 2333
    • (2005) FEBS Lett. , vol.579 , pp. 2327-2333
    • Banmeyer, I.1    Marchand, C.2    Clippe, A.3    Knoops, B.4
  • 12
    • 0025665173 scopus 로고
    • Effect of age on superoxide dismutase, catalase, glutathione reductase, inorganic peroxides, TBA-reactive material, GSH/GSSG, NADPH/NADP + and NADH/NAD + in Drosophila melanogaster
    • R.S. Sohal, L. Arnold, and W.C. Orr Effect of age on superoxide dismutase, catalase, glutathione reductase, inorganic peroxides, TBA-reactive material, GSH/GSSG, NADPH/NADP + and NADH/NAD + in Drosophila melanogaster Mech. Ageing Dev. 56 1990 223 235
    • (1990) Mech. Ageing Dev. , vol.56 , pp. 223-235
    • Sohal, R.S.1    Arnold, L.2    Orr, W.C.3
  • 13
    • 0034669473 scopus 로고    scopus 로고
    • Decreased mitochondrial hydrogen peroxide release in transgenic Drosophila melanogaster expressing intramitochondrial catalase
    • L.K. Kwong, R.J. Mockett, A.C. Bayne, W.C. Orr, and R.S. Sohal Decreased mitochondrial hydrogen peroxide release in transgenic Drosophila melanogaster expressing intramitochondrial catalase Arch. Biochem. Biophys. 383 2000 303 308
    • (2000) Arch. Biochem. Biophys. , vol.383 , pp. 303-308
    • Kwong, L.K.1    Mockett, R.J.2    Bayne, A.C.3    Orr, W.C.4    Sohal, R.S.5
  • 14
    • 33751081281 scopus 로고    scopus 로고
    • Fast cloning inverted repeats for RNA interference
    • S. Bao, and R. Cagan Fast cloning inverted repeats for RNA interference RNA 12 2006 2020 2024
    • (2006) RNA , vol.12 , pp. 2020-2024
    • Bao, S.1    Cagan, R.2
  • 15
    • 0031569419 scopus 로고    scopus 로고
    • Molecular organization of the glutathione reductase gene in Drosophila melanogaster
    • M. Candas, R.S. Sohal, S.N. Radyuk, V.I. Klichko, and W.C. Orr Molecular organization of the glutathione reductase gene in Drosophila melanogaster Arch. Biochem. Biophys. 339 1997 323 334
    • (1997) Arch. Biochem. Biophys. , vol.339 , pp. 323-334
    • Candas, M.1    Sohal, R.S.2    Radyuk, S.N.3    Klichko, V.I.4    Orr, W.C.5
  • 16
    • 0032844257 scopus 로고    scopus 로고
    • Overexpression of glutathione reductase extends survival in transgenic Drosophila melanogaster under hyperoxia but not normoxia
    • R.J. Mockett, R.S. Sohal, and W.C. Orr Overexpression of glutathione reductase extends survival in transgenic Drosophila melanogaster under hyperoxia but not normoxia FASEB J. 13 1999 1733 1742
    • (1999) FASEB J. , vol.13 , pp. 1733-1742
    • Mockett, R.J.1    Sohal, R.S.2    Orr, W.C.3
  • 17
  • 18
    • 34748907199 scopus 로고    scopus 로고
    • Carbonylation of mitochondrial proteins in Drosophila melanogaster during aging
    • D. Toroser, W.C. Orr, and R.S. Sohal Carbonylation of mitochondrial proteins in Drosophila melanogaster during aging Biochem. Biophys. Res. Commun. 363 2007 418 424
    • (2007) Biochem. Biophys. Res. Commun. , vol.363 , pp. 418-424
    • Toroser, D.1    Orr, W.C.2    Sohal, R.S.3
  • 19
    • 0037908649 scopus 로고    scopus 로고
    • Thioredoxin peroxidases can foster cytoprotection or cell death in response to different stressors: Over- and under-expression of thioredoxin peroxidase in Drosophila cells
    • S.N. Radyuk, R.S. Sohal, and W.C. Orr Thioredoxin peroxidases can foster cytoprotection or cell death in response to different stressors: over- and under-expression of thioredoxin peroxidase in Drosophila cells Biochem. J. 371 2003 743 752
    • (2003) Biochem. J. , vol.371 , pp. 743-752
    • Radyuk, S.N.1    Sohal, R.S.2    Orr, W.C.3
  • 20
    • 59049093741 scopus 로고    scopus 로고
    • The catalytic subunit of Drosophila glutamate-cysteine ligase is a nucleocytoplasmic shuttling protein
    • S.N. Radyuk, I. Rebrin, J.M. Luchak, K. Michalak, V.I. Klichko, R.S. Sohal, and W.C. Orr The catalytic subunit of Drosophila glutamate-cysteine ligase is a nucleocytoplasmic shuttling protein J. Biol. Chem. 284 2009 2266 2274
    • (2009) J. Biol. Chem. , vol.284 , pp. 2266-2274
    • Radyuk, S.N.1    Rebrin, I.2    Luchak, J.M.3    Michalak, K.4    Klichko, V.I.5    Sohal, R.S.6    Orr, W.C.7
  • 21
    • 4344587626 scopus 로고    scopus 로고
    • Free aminothiols, glutathione redox state and protein mixed disulphides in aging Drosophila melanogaster
    • I. Rebrin, A.C. Bayne, R.J. Mockett, W.C. Orr, and R.S. Sohal Free aminothiols, glutathione redox state and protein mixed disulphides in aging Drosophila melanogaster Biochem. J. 382 2004 131 136
    • (2004) Biochem. J. , vol.382 , pp. 131-136
    • Rebrin, I.1    Bayne, A.C.2    Mockett, R.J.3    Orr, W.C.4    Sohal, R.S.5
  • 22
    • 0041326831 scopus 로고    scopus 로고
    • Effects of age and caloric restriction on glutathione redox state in mice
    • I. Rebrin, S. Kamzalov, and R.S. Sohal Effects of age and caloric restriction on glutathione redox state in mice Free Radic. Biol. Med. 35 2003 626 635
    • (2003) Free Radic. Biol. Med. , vol.35 , pp. 626-635
    • Rebrin, I.1    Kamzalov, S.2    Sohal, R.S.3
  • 23
    • 0028926834 scopus 로고
    • Mammalian antioxidant protein complements alkylhydroperoxide reductase (ahpC) mutation in Escherichia coli
    • K. Tsuji, N.G. Copeland, N.A. Jenkins, and M. Obinata Mammalian antioxidant protein complements alkylhydroperoxide reductase (ahpC) mutation in Escherichia coli Biochem. J. 307 Pt 2 1995 377 381
    • (1995) Biochem. J. , vol.307 , Issue.PART 2 , pp. 377-381
    • Tsuji, K.1    Copeland, N.G.2    Jenkins, N.A.3    Obinata, M.4
  • 24
    • 0024443323 scopus 로고
    • Cloning of a housekeeping-type gene (MER5) preferentially expressed in murine erythroleukemia cells
    • T. Yamamoto, Y. Matsui, S. Natori, and M. Obinata Cloning of a housekeeping-type gene (MER5) preferentially expressed in murine erythroleukemia cells Gene 80 1989 337 343
    • (1989) Gene , vol.80 , pp. 337-343
    • Yamamoto, T.1    Matsui, Y.2    Natori, S.3    Obinata, M.4
  • 28
    • 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
  • 30
    • 45849119036 scopus 로고    scopus 로고
    • Crucial role of peroxiredoxin III in placental antioxidant defense of mice
    • L. Li, W. Shoji, H. Oshima, M. Obinata, M. Fukumoto, and N. Kanno Crucial role of peroxiredoxin III in placental antioxidant defense of mice FEBS Lett. 582 2008 2431 2434
    • (2008) FEBS Lett. , vol.582 , pp. 2431-2434
    • Li, L.1    Shoji, W.2    Oshima, H.3    Obinata, M.4    Fukumoto, M.5    Kanno, N.6
  • 32
    • 40849133786 scopus 로고    scopus 로고
    • Silencing of peroxiredoxin 3 and peroxiredoxin 5 reveals the role of mitochondrial peroxiredoxins in the protection of human neuroblastoma SH-SY5Y cells toward MPP+
    • S. De Simoni, J. Goemaere, and B. Knoops Silencing of peroxiredoxin 3 and peroxiredoxin 5 reveals the role of mitochondrial peroxiredoxins in the protection of human neuroblastoma SH-SY5Y cells toward MPP+ Neurosci. Lett. 433 2008 219 224
    • (2008) Neurosci. Lett. , vol.433 , pp. 219-224
    • De Simoni, S.1    Goemaere, J.2    Knoops, B.3
  • 33
    • 0242668686 scopus 로고    scopus 로고
    • Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling
    • Z.A. Wood, L.B. Poole, and P.A. Karplus Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling Science 300 2003 650 653
    • (2003) Science , vol.300 , pp. 650-653
    • Wood, Z.A.1    Poole, L.B.2    Karplus, P.A.3
  • 35
    • 0010478667 scopus 로고
    • Mitochondrial damage in muscle occurs after marked depletion of glutathione and is prevented by giving glutathione monoester
    • J. Martensson, and A. Meister Mitochondrial damage in muscle occurs after marked depletion of glutathione and is prevented by giving glutathione monoester Proc. Natl Acad. Sci. USA 86 1989 471 475
    • (1989) Proc. Natl Acad. Sci. USA , vol.86 , pp. 471-475
    • Martensson, J.1    Meister, A.2
  • 36
    • 0033540268 scopus 로고    scopus 로고
    • Depletion of glutathione by buthionine sulfoxine is cytotoxic for human neuroblastoma cell lines via apoptosis
    • C.P. Anderson, J.M. Tsai, W.E. Meek, R.M. Liu, Y. Tang, H.J. Forman, and C.P. Reynolds Depletion of glutathione by buthionine sulfoxine is cytotoxic for human neuroblastoma cell lines via apoptosis Exp. Cell Res. 246 1999 183 192
    • (1999) Exp. Cell Res. , vol.246 , pp. 183-192
    • Anderson, C.P.1    Tsai, J.M.2    Meek, W.E.3    Liu, R.M.4    Tang, Y.5    Forman, H.J.6    Reynolds, C.P.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.