메뉴 건너뛰기




Volumn 38, Issue 11, 2005, Pages 1518-1525

A Caenorhabditis elegans mutant lacking functional nicotinamide nucleotide transhydrogenase displays increased sensitivity to oxidative stress

Author keywords

Caenorhabditis elegans; Free radical; NADPH; Oxidative stress; Paraquat; Transhydrogenase

Indexed keywords

GLUTATHIONE; NICOTINAMIDE ADENINE DINUCLEOTIDE (PHOSPHATE) TRANSHYDROGENASE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; PARAQUAT; PROTON; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; SUPEROXIDE;

EID: 18844415919     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2005.02.012     Document Type: Article
Times cited : (90)

References (33)
  • 1
    • 0027171266 scopus 로고
    • Oxidants, antioxidants, and the degenerative diseases of aging
    • B. Ames, M. Shigenaga, and T. Hagen Oxidants, antioxidants, and the degenerative diseases of aging Proc. Natl. Acad. Sci. USA 90 1993 7915 7922
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 7915-7922
    • Ames, B.1    Shigenaga, M.2    Hagen, T.3
  • 2
    • 0031128356 scopus 로고    scopus 로고
    • The Gpx1 gene encodes mitochondrial glutathione peroxidase in the mouse liver
    • R. Esworthy, Y. Ho, and F. Chu The Gpx1 gene encodes mitochondrial glutathione peroxidase in the mouse liver Arch. Biochem. Biophys. 340 1997 59 63
    • (1997) Arch. Biochem. Biophys. , vol.340 , pp. 59-63
    • Esworthy, R.1    Ho, Y.2    Chu, F.3
  • 3
    • 0033582533 scopus 로고    scopus 로고
    • Mitochondrial phospholipid hydroperoxide glutathione peroxidase plays a major role in preventing oxidative injury to cells
    • M. Arai, H. Imai, T. Koumura, M. Yoshida, K. Emoto, M. Umeda, N. Chiba, and Y. Nakagawa Mitochondrial phospholipid hydroperoxide glutathione peroxidase plays a major role in preventing oxidative injury to cells J. Biol. Chem. 274 1999 4924 4933
    • (1999) J. Biol. Chem. , vol.274 , pp. 4924-4933
    • Arai, M.1    Imai, H.2    Koumura, T.3    Yoshida, M.4    Emoto, K.5    Umeda, M.6    Chiba, N.7    Nakagawa, Y.8
  • 4
    • 0034639911 scopus 로고    scopus 로고
    • Proton translocating nicotinamide nucleotide transhydrogenase from E. coli. Mechanism of action deduced from its structural and catalytic properties
    • T. Bizouarn, O. Fjellström, J. Meuller, M. Axelsson, A. Bergkvist, C. Johansson, G. Karlsson, and J. Rydström Proton translocating nicotinamide nucleotide transhydrogenase from E. coli. Mechanism of action deduced from its structural and catalytic properties Biochim. Biophys. Acta 1457 2000 211 228
    • (2000) Biochim. Biophys. Acta , vol.1457 , pp. 211-228
    • Bizouarn, T.1    Fjellström, O.2    Meuller, J.3    Axelsson, M.4    Bergkvist, A.5    Johansson, C.6    Karlsson, G.7    Rydström, J.8
  • 5
    • 0037006970 scopus 로고    scopus 로고
    • The alternating site, binding change mechanism for proton translocation by transhydrogenase
    • J.B. Jackson, S.A. White, P.G. Quirk, and J.D. Venning The alternating site, binding change mechanism for proton translocation by transhydrogenase Biochemistry 41 2002 4173-4185
    • (2002) Biochemistry , vol.41 , pp. 4173-4185
    • Jackson, J.B.1    White, S.A.2    Quirk, P.G.3    Venning, J.D.4
  • 6
    • 0023681148 scopus 로고
    • Physiological roles of nicotinamide nucleotide transhydrogenase
    • J.B. Hoek, and J. Rydström Physiological roles of nicotinamide nucleotide transhydrogenase Biochem. J. 254 1988 1 10
    • (1988) Biochem. J. , vol.254 , pp. 1-10
    • Hoek, J.B.1    Rydström, J.2
  • 7
    • 0032716145 scopus 로고    scopus 로고
    • The regeneration of reduced glutathione in rat forebrain mitochondria identifies metabolic pathways providing the NADPH required
    • R. Vogel, H. Wiesinger, B. Hamprecht, and R. Dringen The regeneration of reduced glutathione in rat forebrain mitochondria identifies metabolic pathways providing the NADPH required Neurosci. Lett. 275 1999 97 100
    • (1999) Neurosci. Lett. , vol.275 , pp. 97-100
    • Vogel, R.1    Wiesinger, H.2    Hamprecht, B.3    Dringen, R.4
  • 8
    • 0036135679 scopus 로고    scopus 로고
    • Link between the membrane-bound pyridine nucleotide transhydrogenase and glutathione-dependent processes in Rhodobacter sphaeroides
    • J.W. Hickman, R.D. Barber, E.P. Skaar, and T.J. Donohue Link between the membrane-bound pyridine nucleotide transhydrogenase and glutathione-dependent processes in Rhodobacter sphaeroides J. Bacteriol. 184 2002 400 409
    • (2002) J. Bacteriol. , vol.184 , pp. 400-409
    • Hickman, J.W.1    Barber, R.D.2    Skaar, E.P.3    Donohue, T.J.4
  • 9
    • 0028339522 scopus 로고
    • Proton-translocating transhydrogenase and NAD- and NADP-linked isocitrate dehydrogenases operate in a substrate cycle which contributes to fine regulation of the tricarboxylic acid cycle activity in mitochondria
    • L.A. Sazanov, and J.B. Jackson Proton-translocating transhydrogenase and NAD- and NADP-linked isocitrate dehydrogenases operate in a substrate cycle which contributes to fine regulation of the tricarboxylic acid cycle activity in mitochondria FEBS Lett. 344 1994 109 116
    • (1994) FEBS Lett. , vol.344 , pp. 109-116
    • Sazanov, L.A.1    Jackson, J.B.2
  • 10
    • 0035451525 scopus 로고    scopus 로고
    • Does the redox status of cytochrome C act as a fail-safe mechanism in the regulation of programmed cell death?
    • J.T. Hancock, R. Desikan, and S.J. Neill Does the redox status of cytochrome C act as a fail-safe mechanism in the regulation of programmed cell death? Free Radic. Biol. Med. 31 2001 697 703
    • (2001) Free Radic. Biol. Med. , vol.31 , pp. 697-703
    • Hancock, J.T.1    Desikan, R.2    Neill, S.J.3
  • 11
    • 3442886811 scopus 로고    scopus 로고
    • The pathophysiology of mitochondrial cell death
    • D.R. Green, and G. Kroemer The pathophysiology of mitochondrial cell death Science 305 2004 626 629
    • (2004) Science , vol.305 , pp. 626-629
    • Green, D.R.1    Kroemer, G.2
  • 12
    • 1342325419 scopus 로고    scopus 로고
    • The soluble and membrane-bound transhydrogenases UdhA and PntAB have divergent functions in NADPH metabolism of Escherichia coli
    • U. Sauer, F. Canonaco, S. Heri, A. Perrenoud, and E. Fisher The soluble and membrane-bound transhydrogenases UdhA and PntAB have divergent functions in NADPH metabolism of Escherichia coli J. Biol. Chem. 279 2004 6613 6619
    • (2004) J. Biol. Chem. , vol.279 , pp. 6613-6619
    • Sauer, U.1    Canonaco, F.2    Heri, S.3    Perrenoud, A.4    Fisher, E.5
  • 13
    • 0024393963 scopus 로고
    • Thioredoxin and glutaredoxin systems
    • A. Holmgren Thioredoxin and glutaredoxin systems J. Biol. Chem. 264 1989 13963 13966
    • (1989) J. Biol. Chem. , vol.264 , pp. 13963-13966
    • Holmgren, A.1
  • 14
    • 9144249116 scopus 로고    scopus 로고
    • Glutatredoxin 2 catalyzes the reversible oxidation and glutathionylation of mitochondrial membrane thiol proteins
    • S.M. Beer, E.R. Taylor, S.E. Brown, C.C. Dahm, N.J. Costa, M.J. Runswick, and M.P. Murphy Glutatredoxin 2 catalyzes the reversible oxidation and glutathionylation of mitochondrial membrane thiol proteins J. Biol. Chem. 279 2004 47939 47951
    • (2004) J. Biol. Chem. , vol.279 , pp. 47939-47951
    • Beer, S.M.1    Taylor, E.R.2    Brown, S.E.3    Dahm, C.C.4    Costa, N.J.5    Runswick, M.J.6    Murphy, M.P.7
  • 15
    • 0035978884 scopus 로고    scopus 로고
    • Insulin-like signaling, metabolism, stress resistance and aging in Caenorhabditis elegans
    • B. Braeckman, K. Houthoofd, and J. Vanfleteren Insulin-like signaling, metabolism, stress resistance and aging in Caenorhabditis elegans Mech. Ageing Dev. 122 2001 673 693
    • (2001) Mech. Ageing Dev. , vol.122 , pp. 673-693
    • Braeckman, B.1    Houthoofd, K.2    Vanfleteren, J.3
  • 16
    • 0027197284 scopus 로고
    • Oxidative stress and ageing in Caenorhabditis elegans
    • J.R. Vanfleteren Oxidative stress and ageing in Caenorhabditis elegans Biochem. J. 292 1993 605 608
    • (1993) Biochem. J. , vol.292 , pp. 605-608
    • Vanfleteren, J.R.1
  • 18
    • 0034613164 scopus 로고    scopus 로고
    • Regulation of C. elegans life-span by insulinlike signaling in the nervous system
    • C.A. Wolkow, K.D. Kimura, M.L. Lee, and G. Ruvkun Regulation of C. elegans life-span by insulinlike signaling in the nervous system Science 290 2002 147 150
    • (2002) Science , vol.290 , pp. 147-150
    • Wolkow, C.A.1    Kimura, K.D.2    Lee, M.L.3    Ruvkun, G.4
  • 19
    • 0031877935 scopus 로고    scopus 로고
    • A new marker for mosaic analysis in Caenorhabditis elegans indicates a fusion between hyp6 and hyp7, two major components of the hypodermis
    • J. Yochem, T. Gu, and M. Han A new marker for mosaic analysis in Caenorhabditis elegans indicates a fusion between hyp6 and hyp7, two major components of the hypodermis Genetics 149 1998 1323 1334
    • (1998) Genetics , vol.149 , pp. 1323-1334
    • Yochem, J.1    Gu, T.2    Han, M.3
  • 20
    • 0027771804 scopus 로고
    • A C. elegans mutant that lives twice as long as wild type
    • C. Kenyon, J. Chang, E. Gensch, A. Rudner, and R.A. Tabtiang A C. elegans mutant that lives twice as long as wild type Nature 366 1993 461 464
    • (1993) Nature , vol.366 , pp. 461-464
    • Kenyon, C.1    Chang, J.2    Gensch, E.3    Rudner, A.4    Tabtiang, R.A.5
  • 21
    • 0028950419 scopus 로고
    • Mutations in the clk-1 gene of Caenorhabditis elegans affect developmental and behavioral timing
    • A. Wong, P. Boutis, and S. Hekimi Mutations in the clk-1 gene of Caenorhabditis elegans affect developmental and behavioral timing Genetics 139 1995 1247 1249
    • (1995) Genetics , vol.139 , pp. 1247-1249
    • Wong, A.1    Boutis, P.2    Hekimi, S.3
  • 24
    • 0030561203 scopus 로고    scopus 로고
    • Preparation of biotinylated, affinity-purified antibodies for enzyme-linked immunoassays using blotting membrane as an antigen support
    • G.J. Rucklidge, G. Milne, S.M. Chaudhry, and S.P. Robins Preparation of biotinylated, affinity-purified antibodies for enzyme-linked immunoassays using blotting membrane as an antigen support Anal. Biochem. 243 1996 158 164
    • (1996) Anal. Biochem. , vol.243 , pp. 158-164
    • Rucklidge, G.J.1    Milne, G.2    Chaudhry, S.M.3    Robins, S.P.4
  • 25
    • 0019293885 scopus 로고
    • An absolute method for protein determination based on difference in absorbance at 235 and 280 nm
    • R. Whitaker, and P.E. Granum An absolute method for protein determination based on difference in absorbance at 235 and 280 nm Anal. Biochem. 109 1980 156 159
    • (1980) Anal. Biochem. , vol.109 , pp. 156-159
    • Whitaker, R.1    Granum, P.E.2
  • 26
    • 0032030445 scopus 로고    scopus 로고
    • Mitochondrial NADH-quinone oxidoreductase of the outer membrane is responsible for paraquat cytotoxicity in rat livers
    • H. Shimada, K.-H. Hirai, E. Simamura, and J. Pan Mitochondrial NADH-quinone oxidoreductase of the outer membrane is responsible for paraquat cytotoxicity in rat livers Arch. Biochem. Biophys. 351 1998 75 81
    • (1998) Arch. Biochem. Biophys. , vol.351 , pp. 75-81
    • Shimada, H.1    Hirai, K.-H.2    Simamura, E.3    Pan, J.4
  • 27
    • 0035202072 scopus 로고    scopus 로고
    • Differential sensitivities of plant and animal mitochondria to the herbicide paraquat
    • J.A.F. Vicente, F. Peixoto, M.L. Lopes, and V.M.C. Madeira Differential sensitivities of plant and animal mitochondria to the herbicide paraquat J. Biochem. Mol. Toxicol. 15 2001 322 330
    • (2001) J. Biochem. Mol. Toxicol. , vol.15 , pp. 322-330
    • Vicente, J.A.F.1    Peixoto, F.2    Lopes, M.L.3    Madeira, V.M.C.4
  • 28
    • 0035515923 scopus 로고    scopus 로고
    • Mitochondrial electron transport is a key determinant of life span in Caenorhabditis elegans
    • J. Feng, F. Bussiere, and S. Hekimi Mitochondrial electron transport is a key determinant of life span in Caenorhabditis elegans Dev. Cell 1 2001 633 644
    • (2001) Dev. Cell , vol.1 , pp. 633-644
    • Feng, J.1    Bussiere, F.2    Hekimi, S.3
  • 29
    • 0035834789 scopus 로고    scopus 로고
    • A defect in the cytochrome b large subunit in complex II causes both superoxide anion overproduction and abnormal energy metabolism in Caenorhabditis elegans
    • N. Senoo-Matsuda, K. Yasuda, M. Tsuda, T. Ohkubo, S. Yoshimura, H. Nakazawa, P.S. Hartman, and N. Ishii A defect in the cytochrome b large subunit in complex II causes both superoxide anion overproduction and abnormal energy metabolism in Caenorhabditis elegans J. Biol. Chem. 276 2001 41553 41558
    • (2001) J. Biol. Chem. , vol.276 , pp. 41553-41558
    • Senoo-Matsuda, N.1    Yasuda, K.2    Tsuda, M.3    Ohkubo, T.4    Yoshimura, S.5    Nakazawa, H.6    Hartman, P.S.7    Ishii, N.8
  • 30
    • 0020478933 scopus 로고
    • Status of the mitochondrial pool of glutathione in the isolated hepatocyte
    • M.J. Meredith, and D.J. Reed Status of the mitochondrial pool of glutathione in the isolated hepatocyte J. Biol. Chem. 257 1982 3747 3753
    • (1982) J. Biol. Chem. , vol.257 , pp. 3747-3753
    • Meredith, M.J.1    Reed, D.J.2
  • 31
    • 0033198944 scopus 로고    scopus 로고
    • RNA-triggered gene silencing
    • A. Fire RNA-triggered gene silencing Trends Genet. 15 1999 358 363
    • (1999) Trends Genet. , vol.15 , pp. 358-363
    • Fire, A.1
  • 32
    • 0027515616 scopus 로고
    • Aging and resistance to oxidative damage in Caenorhabditis elegans
    • P.L. Larsen Aging and resistance to oxidative damage in Caenorhabditis elegans Proc. Natl. Acad. Sci. USA 90 1993 8905 8909
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 8905-8909
    • Larsen, P.L.1
  • 33
    • 0036233808 scopus 로고    scopus 로고
    • Oxidative stress and life span determination in the nematode Caenorhabditis elegans
    • Y. Honda, and S. Honda Oxidative stress and life span determination in the nematode Caenorhabditis elegans Ann. N. Y. Acad. Sci. 959 2002 466 474
    • (2002) Ann. N. Y. Acad. Sci. , vol.959 , pp. 466-474
    • Honda, Y.1    Honda, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.