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Volumn 176, Issue 1, 2011, Pages 17-24

The activity and hydrogen peroxide sensitivity of the peroxiredoxins from the parasitic nematode Haemonchus contortus

Author keywords

Antioxidant activity; Glutathione system; Haemonchus contortus; Nematode; Peroxiredoxin; Thioredoxin system

Indexed keywords

DNA; FREE RADICAL; GLUTATHIONE; HYDROGEN PEROXIDE; PEROXIREDOXIN 1; PEROXIREDOXIN 2; THIOREDOXIN REDUCTASE 1; THIOREDOXIN REDUCTASE 2;

EID: 78951491178     PISSN: 01666851     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molbiopara.2010.11.006     Document Type: Article
Times cited : (10)

References (44)
  • 1
    • 0034717135 scopus 로고    scopus 로고
    • Mitochondria of Saccharomyces cerevisiae contain one-conserved cysteine type peroxiredoxin with thioredoxin peroxidase activity
    • J.R. Pedrajas, A. Miranda-Vizuete, N. Javanmardy, J.A. Gustafsson, and G. Spyrou Mitochondria of Saccharomyces cerevisiae contain one-conserved cysteine type peroxiredoxin with thioredoxin peroxidase activity J Biol Chem 275 2000 16296 16301
    • (2000) J Biol Chem , vol.275 , pp. 16296-16301
    • Pedrajas, J.R.1    Miranda-Vizuete, A.2    Javanmardy, N.3    Gustafsson, J.A.4    Spyrou, G.5
  • 3
    • 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 Diabetes Res Clin Pract 45 1999 101 112
    • (1999) Diabetes Res Clin Pract , vol.45 , pp. 101-112
    • Chae, H.Z.1    Kim, H.J.2    Kang, S.W.3    Rhee, S.G.4
  • 4
    • 0025996014 scopus 로고
    • Reconstitution of Ca(2+)-dependent K+ transport in erythrocyte membrane vesicles requires a cytoplasmic protein
    • R.B. Moore, M.V. Mankad, S.K. Shriver, V.N. Mankad, and G.A. Plishker Reconstitution of Ca(2+)-dependent K+ transport in erythrocyte membrane vesicles requires a cytoplasmic protein J Biol Chem 266 1991 18964 18968
    • (1991) J Biol Chem , vol.266 , pp. 18964-18968
    • Moore, R.B.1    Mankad, M.V.2    Shriver, S.K.3    Mankad, V.N.4    Plishker, G.A.5
  • 5
    • 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
  • 6
    • 0023263401 scopus 로고
    • Trypanothione dependent peroxide metabolism in Crithidia fasciculata and Trypanosoma brucei
    • G.B. Henderson, A.H. Fairlamb, and A. Cerami Trypanothione dependent peroxide metabolism in Crithidia fasciculata and Trypanosoma brucei Mol Biochem Parasitol 24 1987 39 45
    • (1987) Mol Biochem Parasitol , vol.24 , pp. 39-45
    • Henderson, G.B.1    Fairlamb, A.H.2    Cerami, A.3
  • 7
    • 0030458544 scopus 로고    scopus 로고
    • Antioxidant defense mechanisms in parasitic protozoa
    • R.K. Mehlotra Antioxidant defense mechanisms in parasitic protozoa Crit Rev Microbiol 22 1996 295 314
    • (1996) Crit Rev Microbiol , vol.22 , pp. 295-314
    • Mehlotra, R.K.1
  • 8
    • 0023718663 scopus 로고
    • Antioxidant systems in Schistosoma mansoni: Correlation between susceptibility to oxidant killing and the levels of scavengers of hydrogen peroxide and oxygen free radicals
    • G.M. Mkoji, J.M. Smith, and R.K. Prichard Antioxidant systems in Schistosoma mansoni: correlation between susceptibility to oxidant killing and the levels of scavengers of hydrogen peroxide and oxygen free radicals Int J Parasitol 18 1988 661 666
    • (1988) Int J Parasitol , vol.18 , pp. 661-666
    • Mkoji, G.M.1    Smith, J.M.2    Prichard, R.K.3
  • 9
    • 28244462440 scopus 로고    scopus 로고
    • Plasmodium falciparum 2-Cys peroxiredoxin reacts with plasmoredoxin and peroxynitrite
    • C. Nickel, M. Trujillo, S. Rahlfs, M. Deponte, R. Radi, and K. Becker Plasmodium falciparum 2-Cys peroxiredoxin reacts with plasmoredoxin and peroxynitrite Biol Chem 386 2005 1129 1136
    • (2005) Biol Chem , vol.386 , pp. 1129-1136
    • Nickel, C.1    Trujillo, M.2    Rahlfs, S.3    Deponte, M.4    Radi, R.5    Becker, K.6
  • 11
    • 0023741521 scopus 로고
    • Helminth anti-oxidant enzymes: A protective mechanism against host oxidants?
    • H.L. Callahan, R.K. Crouch, and E.R. James Helminth anti-oxidant enzymes: a protective mechanism against host oxidants? Parasitol Today 4 1988 218 225
    • (1988) Parasitol Today , vol.4 , pp. 218-225
    • Callahan, H.L.1    Crouch, R.K.2    James, E.R.3
  • 13
    • 33749005947 scopus 로고    scopus 로고
    • The thiol-based redox networks of pathogens: Unexploited targets in the search for new drugs
    • T. Jaeger, and L. Flohe The thiol-based redox networks of pathogens: unexploited targets in the search for new drugs Biofactors 27 2006 109 120
    • (2006) Biofactors , vol.27 , pp. 109-120
    • Jaeger, T.1    Flohe, L.2
  • 15
    • 0037634121 scopus 로고    scopus 로고
    • Thioredoxin from Brugia malayi: Defining a 16-kilodalton class of thioredoxins from nematodes
    • K. Kunchithapautham, B. Padmavathi, R.B. Narayanan, P. Kaliraj, and A.L. Scott Thioredoxin from Brugia malayi: defining a 16-kilodalton class of thioredoxins from nematodes Infect Immun 71 2003 4119 4126
    • (2003) Infect Immun , vol.71 , pp. 4119-4126
    • Kunchithapautham, K.1    Padmavathi, B.2    Narayanan, R.B.3    Kaliraj, P.4    Scott, A.L.5
  • 16
    • 43849101278 scopus 로고    scopus 로고
    • Thioredoxins of a parasitic nematode: Comparison of the 16- and 12-kDA thioredoxins from Haemonchus contortus
    • I.M. Sotirchos, A.L. Hudson, J. Ellis, and M.W. Davey Thioredoxins of a parasitic nematode: comparison of the 16- and 12-kDA thioredoxins from Haemonchus contortus Free Radic Biol Med 44 2008 2026 2033
    • (2008) Free Radic Biol Med , vol.44 , pp. 2026-2033
    • Sotirchos, I.M.1    Hudson, A.L.2    Ellis, J.3    Davey, M.W.4
  • 17
    • 59349112324 scopus 로고    scopus 로고
    • A unique thioredoxin of the parasitic nematode Haemonchus contortus with glutaredoxin activity
    • I.M. Sotirchos, A.L. Hudson, J. Ellis, and M.W. Davey A unique thioredoxin of the parasitic nematode Haemonchus contortus with glutaredoxin activity Free Radic Biol Med 46 2009 579 585
    • (2009) Free Radic Biol Med , vol.46 , pp. 579-585
    • Sotirchos, I.M.1    Hudson, A.L.2    Ellis, J.3    Davey, M.W.4
  • 18
    • 8744306872 scopus 로고    scopus 로고
    • CDNA cloning and expression patterns of a peroxiredoxin, a catalase and a glutathione peroxidase from Haemonchus contortus
    • N.H. Bagnall, and A.C. Kotze cDNA cloning and expression patterns of a peroxiredoxin, a catalase and a glutathione peroxidase from Haemonchus contortus Parasitol Res 94 2004 283 289
    • (2004) Parasitol Res , vol.94 , pp. 283-289
    • Bagnall, N.H.1    Kotze, A.C.2
  • 19
    • 77955473248 scopus 로고    scopus 로고
    • Substrate specificity of the mitochondrial thioredoxin reductase of the parasitic nematode Haemonchus contortus
    • A.L. Hudson, I.M. Sotirchos, and M.W. Davey Substrate specificity of the mitochondrial thioredoxin reductase of the parasitic nematode Haemonchus contortus Parasitol Res 107 2010 487 493
    • (2010) Parasitol Res , vol.107 , pp. 487-493
    • Hudson, A.L.1    Sotirchos, I.M.2    Davey, M.W.3
  • 20
    • 33748787130 scopus 로고    scopus 로고
    • Biochemical characterisation of the recombinant peroxiredoxin (FhePrx) of the liver fluke, Fasciola hepatica
    • M. Sekiya, G. Mulcahy, and J.A. Irwin Biochemical characterisation of the recombinant peroxiredoxin (FhePrx) of the liver fluke, Fasciola hepatica FEBS Lett 580 2006 5016 5022
    • (2006) FEBS Lett , vol.580 , pp. 5016-5022
    • Sekiya, M.1    Mulcahy, G.2    Irwin, J.A.3
  • 21
    • 0018723651 scopus 로고
    • Thioredoxin catalyzes the reduction of insulin disulfides by dithiothreitol and dihydrolipoamide
    • A. Holmgren Thioredoxin catalyzes the reduction of insulin disulfides by dithiothreitol and dihydrolipoamide J Biol Chem 254 1979 9627 9632
    • (1979) J Biol Chem , vol.254 , pp. 9627-9632
    • Holmgren, A.1
  • 22
    • 0029187491 scopus 로고
    • Thioredoxin and thioredoxin reductase
    • A. Holmgren, and M. Bjornstedt Thioredoxin and thioredoxin reductase Methods Enzymol 252 1995 199 208
    • (1995) Methods Enzymol , vol.252 , pp. 199-208
    • Holmgren, A.1    Bjornstedt, M.2
  • 23
    • 33845659892 scopus 로고    scopus 로고
    • An evolutionarily conserved 16-kDa thioredoxin-related protein is an antioxidant which regulates the NF-kappaB signaling pathway
    • X.W. Wang, Y.C. Liou, B. Ho, and J.L Ding An evolutionarily conserved 16-kDa thioredoxin-related protein is an antioxidant which regulates the NF-kappaB signaling pathway Free Radic Biol Med 42 2007 247 259
    • (2007) Free Radic Biol Med , vol.42 , pp. 247-259
    • Wang, X.W.1    Liou, Y.C.2    Ho, B.3    Ding, J.L.4
  • 24
    • 34547731488 scopus 로고    scopus 로고
    • A rapid colorimetric assay for the quantitation of the viability of free-living larvae of nematodes in vitro
    • C.E. James, and M.W. Davey A rapid colorimetric assay for the quantitation of the viability of free-living larvae of nematodes in vitro Parasitol Res 101 2007 975 980
    • (2007) Parasitol Res , vol.101 , pp. 975-980
    • James, C.E.1    Davey, M.W.2
  • 25
    • 2942532835 scopus 로고    scopus 로고
    • Biochemical characterization of 2-Cys peroxiredoxins from Schistosoma mansoni
    • A.A. Sayed, and D.L. Williams Biochemical characterization of 2-Cys peroxiredoxins from Schistosoma mansoni J Biol Chem 279 2004 26159 26166
    • (2004) J Biol Chem , vol.279 , pp. 26159-26166
    • Sayed, A.A.1    Williams, D.L.2
  • 26
    • 0035188896 scopus 로고    scopus 로고
    • Overexpression of wild type and SeCys/Cys mutant of human thioredoxin reductase in E. coli: The role of selenocysteine in the catalytic activity
    • S. Bar-Noy, S.N. Gorlatov, and T.C. Stadtman Overexpression of wild type and SeCys/Cys mutant of human thioredoxin reductase in E. coli: the role of selenocysteine in the catalytic activity Free Radic Biol Med 30 2001 51 61
    • (2001) Free Radic Biol Med , vol.30 , pp. 51-61
    • Bar-Noy, S.1    Gorlatov, S.N.2    Stadtman, T.C.3
  • 27
    • 4644224905 scopus 로고    scopus 로고
    • Assessment of production conditions for efficient use of Escherichia coli in high-yield heterologous recombinant selenoprotein synthesis
    • O. Rengby, L. Johansson, and L.A. Carlson Assessment of production conditions for efficient use of Escherichia coli in high-yield heterologous recombinant selenoprotein synthesis Appl Environ Microbiol 70 2004 5159 5167
    • (2004) Appl Environ Microbiol , vol.70 , pp. 5159-5167
    • Rengby, O.1    Johansson, L.2    Carlson, L.A.3
  • 28
    • 0026715159 scopus 로고
    • Thiol-mediated generation of nitric oxide accounts for the vasodilator action of furoxans
    • M. Feelisch, K. Schonafinger, and E. Noack Thiol-mediated generation of nitric oxide accounts for the vasodilator action of furoxans Biochem Pharmacol 44 1992 1149 1157
    • (1992) Biochem Pharmacol , vol.44 , pp. 1149-1157
    • Feelisch, M.1    Schonafinger, K.2    Noack, E.3
  • 29
    • 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
  • 30
    • 0032485270 scopus 로고    scopus 로고
    • A molecular evolutionary framework for the phylum Nematoda
    • M.L. Blaxter, P. De Ley, and J.R. Garey A molecular evolutionary framework for the phylum Nematoda Nature 392 1998 71 75
    • (1998) Nature , vol.392 , pp. 71-75
    • Blaxter, M.L.1    De Ley, P.2    Garey, J.R.3
  • 32
    • 77951893193 scopus 로고    scopus 로고
    • Molecular cloning and characterization of two genes encoding 2-Cys peroxiredoxins from Fasciola gigantica
    • K. Chaithirayanon, and P. Sobhon Molecular cloning and characterization of two genes encoding 2-Cys peroxiredoxins from Fasciola gigantica Exp Parasitol 125 2010 106 113
    • (2010) Exp Parasitol , vol.125 , pp. 106-113
    • Chaithirayanon, K.1    Sobhon, P.2
  • 33
    • 0029846254 scopus 로고    scopus 로고
    • Effect of paraquat intoxication and ambroxol treatment on hydrogen peroxide production and lipid peroxidation in selected organs of rat
    • W.J. Piotrowski, T. Pietras, and Z. Kurmanowska Effect of paraquat intoxication and ambroxol treatment on hydrogen peroxide production and lipid peroxidation in selected organs of rat J Appl Toxicol 16 1996 501 507
    • (1996) J Appl Toxicol , vol.16 , pp. 501-507
    • Piotrowski, W.J.1    Pietras, T.2    Kurmanowska, Z.3
  • 34
    • 58149395029 scopus 로고    scopus 로고
    • A redox-sensitive peroxiredoxin that is important for longevity has tissue- and stress-specific roles in stress resistance
    • M. Olahova, S.R. Taylor, and S. Khazaipoul A redox-sensitive peroxiredoxin that is important for longevity has tissue- and stress-specific roles in stress resistance Proc Natl Acad Sci USA 105 2008 19839 19844
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 19839-19844
    • Olahova, M.1    Taylor, S.R.2    Khazaipoul, S.3
  • 35
    • 73449138216 scopus 로고    scopus 로고
    • Role of the endogenous antioxidant system in the protection of Schistosoma mansoni primary sporocysts against exogenous oxidative stress
    • M. Mourao Mde, N. Dinguirard, G.R. Franco, and T.P. Yoshino Role of the endogenous antioxidant system in the protection of Schistosoma mansoni primary sporocysts against exogenous oxidative stress PLoS Negl Trop Dis 3 2009 e550
    • (2009) PLoS Negl Trop Dis , vol.3 , pp. 550
    • Mourao Mde, M.1    Dinguirard, N.2    Franco, G.R.3    Yoshino, T.P.4
  • 36
    • 38749125910 scopus 로고    scopus 로고
    • History of the peroxiredoxins and topical perspectives
    • L. Flohe, J.R. Harris, and Introduction History of the peroxiredoxins and topical perspectives Subcell Biochem 44 2007 1 25
    • (2007) Subcell Biochem , vol.44 , pp. 1-25
    • Flohe, L.1    Harris, J.R.2    Introduction3
  • 37
    • 0022683672 scopus 로고
    • Isolation of superoxide dismutase mutants in Escherichia coli: Is superoxide dismutase necessary for aerobic life?
    • A. Carlioz, and D. Touati Isolation of superoxide dismutase mutants in Escherichia coli: is superoxide dismutase necessary for aerobic life? EMBO J 5 1986 623 630
    • (1986) EMBO J , vol.5 , pp. 623-630
    • Carlioz, A.1    Touati, D.2
  • 38
    • 0035831464 scopus 로고    scopus 로고
    • The putative glutathione peroxidase gene of Plasmodium falciparum codes for a thioredoxin peroxidase
    • H. Sztajer, B. Gamain, and K.D. Aumann The putative glutathione peroxidase gene of Plasmodium falciparum codes for a thioredoxin peroxidase J Biol Chem 276 2001 7397 7403
    • (2001) J Biol Chem , vol.276 , pp. 7397-7403
    • Sztajer, H.1    Gamain, B.2    Aumann, K.D.3
  • 39
    • 40849136587 scopus 로고    scopus 로고
    • Substrate specificity and redox potential of AhpC, a bacterial peroxiredoxin
    • D. Parsonage, P.A. Karplus, and L.B. Poole Substrate specificity and redox potential of AhpC, a bacterial peroxiredoxin Proc Natl Acad Sci USA 105 2008 8209 8214
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 8209-8214
    • Parsonage, D.1    Karplus, P.A.2    Poole, L.B.3
  • 40
    • 31444451689 scopus 로고    scopus 로고
    • 2 at physiological concentrations modulates Leydig cell function inducing oxidative stress and apoptosis
    • 2 at physiological concentrations modulates Leydig cell function inducing oxidative stress and apoptosis Apoptosis 11 2006 39 46
    • (2006) Apoptosis , vol.11 , pp. 39-46
    • Gautam, D.K.1    Misro, M.M.2    Chaki, S.P.3    Sehgal, N.4
  • 41
    • 19444375216 scopus 로고    scopus 로고
    • Peroxiredoxins: A historical overview and speculative preview of novel mechanisms and emerging concepts in cell signaling
    • S.G. Rhee, H.Z. Chae, and K. Kim Peroxiredoxins: a historical overview and speculative preview of novel mechanisms and emerging concepts in cell signaling Free Radic Biol Med 38 2005 1543 1552
    • (2005) Free Radic Biol Med , vol.38 , pp. 1543-1552
    • Rhee, S.G.1    Chae, H.Z.2    Kim, K.3
  • 42
    • 15044362438 scopus 로고    scopus 로고
    • Intracellular messenger function of hydrogen peroxide and its regulation by peroxiredoxins
    • S.G. Rhee, S.W. Kang, W. Jeong, T.S. Chang, K.S. Yang, and H.A. Woo Intracellular messenger function of hydrogen peroxide and its regulation by peroxiredoxins Curr Opin Cell Biol 17 2005 183 189
    • (2005) Curr Opin Cell Biol , vol.17 , pp. 183-189
    • Rhee, S.G.1    Kang, S.W.2    Jeong, W.3    Chang, T.S.4    Yang, K.S.5    Woo, H.A.6
  • 43
    • 41849098521 scopus 로고    scopus 로고
    • Identification of oxadiazoles as new drug leads for the control of schistosomiasis
    • A.A. Sayed, A. Simeonov, C.J. Thomas, J. Inglese, C.P. Austin, and D.L. Williams Identification of oxadiazoles as new drug leads for the control of schistosomiasis Nat Med 14 2008 407 412
    • (2008) Nat Med , vol.14 , pp. 407-412
    • Sayed, A.A.1    Simeonov, A.2    Thomas, C.J.3    Inglese, J.4    Austin, C.P.5    Williams, D.L.6
  • 44
    • 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


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