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Volumn 29, Issue 2, 2010, Pages 305-311

Analysis of the expression and antioxidative property of a peroxiredoxin 6 from Scophthalmus maximus

Author keywords

Antioxidant; Oxidative stress; Peroxiredoxin; Reactive oxygen species; Scophthalmus maximus

Indexed keywords

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; SCOPHTHALMIDAE; SCOPHTHALMUS MAXIMUS;

EID: 77954958461     PISSN: 10504648     EISSN: 10959947     Source Type: Journal    
DOI: 10.1016/j.fsi.2010.04.008     Document Type: Article
Times cited : (44)

References (37)
  • 1
    • 14644437730 scopus 로고    scopus 로고
    • Reactive oxygen species and development in microbial eukaryotes
    • Aguirre J., Momberg M.R., Hewitt D., Hansberg W. Reactive oxygen species and development in microbial eukaryotes. Trends Microbiol 2005, 13:111-118.
    • (2005) Trends Microbiol , vol.13 , pp. 111-118
    • Aguirre, J.1    Momberg, M.R.2    Hewitt, D.3    Hansberg, W.4
  • 2
    • 0033301995 scopus 로고    scopus 로고
    • From cytoprotection to tumor suppression: the multifactorial role of peroxiredoxins
    • Butterfield L.H., Merino A., Golub S.H., Shau H. From cytoprotection to tumor suppression: the multifactorial role of peroxiredoxins. Antioxid Redox Signal 1999, 1:385-402.
    • (1999) Antioxid Redox Signal , vol.1 , pp. 385-402
    • Butterfield, L.H.1    Merino, A.2    Golub, S.H.3    Shau, H.4
  • 3
    • 0036287739 scopus 로고    scopus 로고
    • Advances in our understanding of peroxiredoxin. A multifunctional mammalian redox protein
    • Fujii J., Ikeda Y. Advances in our understanding of peroxiredoxin. A multifunctional mammalian redox protein. Redox Rep 2002, 7:123-130.
    • (2002) Redox Rep , vol.7 , pp. 123-130
    • Fujii, J.1    Ikeda, Y.2
  • 4
    • 64149085448 scopus 로고    scopus 로고
    • Typical 2-Cys peroxiredoxins-structures, mechanisms and functions
    • Hall A., Karplus P.A., Poole L.B. Typical 2-Cys peroxiredoxins-structures, mechanisms and functions. FEBS J 2009, 276:2469-2477.
    • (2009) FEBS J , vol.276 , pp. 2469-2477
    • Hall, A.1    Karplus, P.A.2    Poole, L.B.3
  • 5
    • 64149090868 scopus 로고    scopus 로고
    • Typical 2-Cys peroxiredoxins-modulation by covalent transformations and noncovalent interactions
    • Aran M., Ferrero D.S., Pagano E., Wolosiuk R.A. Typical 2-Cys peroxiredoxins-modulation by covalent transformations and noncovalent interactions. FEBS J 2009, 276:2478-2493.
    • (2009) FEBS J , vol.276 , pp. 2478-2493
    • Aran, M.1    Ferrero, D.S.2    Pagano, E.3    Wolosiuk, R.A.4
  • 6
    • 0028226006 scopus 로고
    • Cloning and sequencing of thiol-specific antioxidant from mammalian brain: alkyl hydroperoxide reductase and thiol-specific antioxidant define a large family of antioxidant enzymes
    • Chae H.Z., Robison K., Pooleo L.B., Church G., Storz G., Rhee S.G. Cloning and sequencing of thiol-specific antioxidant from mammalian brain: alkyl hydroperoxide reductase and thiol-specific antioxidant define a large family of antioxidant enzymes. Proc Natl Acad Sci USA 1994, 91:7017-7021.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 7017-7021
    • Chae, H.Z.1    Robison, K.2    Pooleo, L.B.3    Church, G.4    Storz, G.5    Rhee, S.G.6
  • 8
    • 18844400905 scopus 로고    scopus 로고
    • Peroxiredoxin 6, a 1-Cys peroxiredoxin, functions in antioxidant defense and lung phospholipid metabolism
    • Manevich Y., Fisher A.B. Peroxiredoxin 6, a 1-Cys peroxiredoxin, functions in antioxidant defense and lung phospholipid metabolism. Free Radic Biol Med 2005, 38:1422-1432.
    • (2005) Free Radic Biol Med , vol.38 , pp. 1422-1432
    • Manevich, Y.1    Fisher, A.B.2
  • 9
    • 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
    • Leyens G., Donnay I., Knoops B. Cloning of bovine peroxiredoxins-gene expression in bovine tissues and amino acid sequence comparison with rat, mouse and primate peroxiredoxins. Com Biochem Physiol B, Biochem Mol Biol 2003, 136:943-955.
    • (2003) Com Biochem Physiol B, Biochem Mol Biol , vol.136 , pp. 943-955
    • Leyens, G.1    Donnay, I.2    Knoops, B.3
  • 10
    • 0033597885 scopus 로고    scopus 로고
    • Phospholipid hydroperoxides are substrates for non selenium glutathione peroxidase
    • Fisher A.B., Dodia C., Manevich Y., Chen J.W., Feinstein S.I. Phospholipid hydroperoxides are substrates for non selenium glutathione peroxidase. J Biol Chem 1999, 274:21326-21334.
    • (1999) J Biol Chem , vol.274 , pp. 21326-21334
    • Fisher, A.B.1    Dodia, C.2    Manevich, Y.3    Chen, J.W.4    Feinstein, S.I.5
  • 11
    • 0035425780 scopus 로고    scopus 로고
    • Oxidation of active center cysteine of bovine 1-Cys peroxiredoxin to the cysteine sulfenic acid form by peroxide and peroxynitrite
    • Peshenko I.V., Shichi H. Oxidation of active center cysteine of bovine 1-Cys peroxiredoxin to the cysteine sulfenic acid form by peroxide and peroxynitrite. Free Radic Biol Med 2001, 31:292-303.
    • (2001) Free Radic Biol Med , vol.31 , pp. 292-303
    • Peshenko, I.V.1    Shichi, H.2
  • 12
    • 0034666290 scopus 로고    scopus 로고
    • 1-Cys peroxiredoxin, a bifunctional enzyme with glutathione peroxidase peroxidase and phospholipase A2 activities
    • Chen J.W., Dodia C., Feinstein S.I., Jain M.K., Fisher A.B. 1-Cys peroxiredoxin, a bifunctional enzyme with glutathione peroxidase peroxidase and phospholipase A2 activities. J Biol Chem 2000, 275:28421-28427.
    • (2000) J Biol Chem , vol.275 , pp. 28421-28427
    • Chen, J.W.1    Dodia, C.2    Feinstein, S.I.3    Jain, M.K.4    Fisher, A.B.5
  • 13
    • 0031945918 scopus 로고    scopus 로고
    • Crystal structure of a novel human peroxidase enzyme at 2.0 A resolution
    • Choi H.J., Kang S.W., Yang C.H., Rhee S.G., Ryu S.E. Crystal structure of a novel human peroxidase enzyme at 2.0 A resolution. Nat Struct Biol 1998, 5:400-406.
    • (1998) Nat Struct Biol , vol.5 , pp. 400-406
    • Choi, H.J.1    Kang, S.W.2    Yang, C.H.3    Rhee, S.G.4    Ryu, S.E.5
  • 14
    • 8344281472 scopus 로고    scopus 로고
    • Divergence of function in the thioredoxin fold suprafamily: evidence for evolution of peroxiredoxins from a thioredoxin-like ancestor
    • Copley S.D., Novak W.R., Babbitt P.C. Divergence of function in the thioredoxin fold suprafamily: evidence for evolution of peroxiredoxins from a thioredoxin-like ancestor. Biochemistry 2004, 43:13981-13995.
    • (2004) Biochemistry , vol.43 , pp. 13981-13995
    • Copley, S.D.1    Novak, W.R.2    Babbitt, P.C.3
  • 16
    • 54949159505 scopus 로고    scopus 로고
    • Analysis of ESTs and expression of two peroxiredoxins in the thermally stressed Antarctic bivalve Laternula elliptica
    • Park H., Ahn I.Y., Kim H., Cheon J., Kim M. Analysis of ESTs and expression of two peroxiredoxins in the thermally stressed Antarctic bivalve Laternula elliptica. Fish Shellfish Immunol 2008, 25:550-559.
    • (2008) Fish Shellfish Immunol , vol.25 , pp. 550-559
    • Park, H.1    Ahn, I.Y.2    Kim, H.3    Cheon, J.4    Kim, M.5
  • 17
    • 34248587901 scopus 로고    scopus 로고
    • Molecular cloning, expression of a peroxiredoxin gene in Chinese shrimp Fenneropenaeus chinensis and the antioxidant activity of its recombinant protein
    • Zhang Q., Li F., Zhang J., Wang B., Gao H., Huang B., et al. Molecular cloning, expression of a peroxiredoxin gene in Chinese shrimp Fenneropenaeus chinensis and the antioxidant activity of its recombinant protein. Mol Immunol 2007, 44:3501-3509.
    • (2007) Mol Immunol , vol.44 , pp. 3501-3509
    • Zhang, Q.1    Li, F.2    Zhang, J.3    Wang, B.4    Gao, H.5    Huang, B.6
  • 18
    • 67650621580 scopus 로고    scopus 로고
    • Molecular cloning, characterization and expression analysis of peroxiredoxin 6 from disk abalone Haliotis discus discus and the antioxidant activity of its recombinant protein
    • Nikapitiya C., De Zoysa M., Whang I., Kim C.G., Lee Y.H., Kim S.J., et al. Molecular cloning, characterization and expression analysis of peroxiredoxin 6 from disk abalone Haliotis discus discus and the antioxidant activity of its recombinant protein. Fish Shellfish Immunol 2009, 27:239-249.
    • (2009) Fish Shellfish Immunol , vol.27 , pp. 239-249
    • Nikapitiya, C.1    De Zoysa, M.2    Whang, I.3    Kim, C.G.4    Lee, Y.H.5    Kim, S.J.6
  • 19
    • 34547925595 scopus 로고    scopus 로고
    • Peroxiredoxin 6 gene: a new physiological and genetic indicator of multiple environmental stress response in Pacific oyster Crassostrea gigas
    • David E., Tanguy A., Moraga D. Peroxiredoxin 6 gene: a new physiological and genetic indicator of multiple environmental stress response in Pacific oyster Crassostrea gigas. Aquat Toxicol 2007, 84:389-398.
    • (2007) Aquat Toxicol , vol.84 , pp. 389-398
    • David, E.1    Tanguy, A.2    Moraga, D.3
  • 20
    • 46649091500 scopus 로고    scopus 로고
    • Cloning and characterization of Arenicola marina peroxiredoxin 6, an annelid two-cysteine peroxiredoxin highly homologous to mammalian one-cysteine peroxiredoxins
    • Loumaye E., Andersen A.C., Clippe A., Degand H., Dubuisson M., Zal F., et al. Cloning and characterization of Arenicola marina peroxiredoxin 6, an annelid two-cysteine peroxiredoxin highly homologous to mammalian one-cysteine peroxiredoxins. Free Radic Biol Med 2008, 45:482-493.
    • (2008) Free Radic Biol Med , vol.45 , pp. 482-493
    • Loumaye, E.1    Andersen, A.C.2    Clippe, A.3    Degand, H.4    Dubuisson, M.5    Zal, F.6
  • 21
    • 1542315378 scopus 로고    scopus 로고
    • Construction of a subtractive library from hexavalent chromium treated winter flounder (Pseudopleuronectes americanus) reveals alterations in non-selenium glutathione peroxidases
    • Chapman L.M., Roling J.A., Bingham L.K., Herald M.R., Baldwin W.S. Construction of a subtractive library from hexavalent chromium treated winter flounder (Pseudopleuronectes americanus) reveals alterations in non-selenium glutathione peroxidases. Aquat Toxicol 2004, 67:181-194.
    • (2004) Aquat Toxicol , vol.67 , pp. 181-194
    • Chapman, L.M.1    Roling, J.A.2    Bingham, L.K.3    Herald, M.R.4    Baldwin, W.S.5
  • 22
    • 33751340314 scopus 로고    scopus 로고
    • Molecular identification and expression analysis of the natural killer cell enhancing factor (NKEF) gene from turbot (Scophthalmus maximus)
    • Chen Y., Zhang Y., Fan T., Meng L., Ren G., Chen S. Molecular identification and expression analysis of the natural killer cell enhancing factor (NKEF) gene from turbot (Scophthalmus maximus). Aquaculture 2006, 261:1186-1193.
    • (2006) Aquaculture , vol.261 , pp. 1186-1193
    • Chen, Y.1    Zhang, Y.2    Fan, T.3    Meng, L.4    Ren, G.5    Chen, S.6
  • 23
    • 34248162825 scopus 로고    scopus 로고
    • Cloning, characterization, and molecular application of a beta-agarase gene from Vibrio sp. strain V134
    • Zhang W.W., Sun L. Cloning, characterization, and molecular application of a beta-agarase gene from Vibrio sp. strain V134. Appl Environ Microbiol 2007, 73:2825-2831.
    • (2007) Appl Environ Microbiol , vol.73 , pp. 2825-2831
    • Zhang, W.W.1    Sun, L.2
  • 24
    • 51149119260 scopus 로고    scopus 로고
    • Regulation of autoinducer 2 production and luxS expression in a pathogenic Edwardsiella tarda strain
    • Zhang M., Sun K., Sun L. Regulation of autoinducer 2 production and luxS expression in a pathogenic Edwardsiella tarda strain. Microbiology 2008, 154:2060-2069.
    • (2008) Microbiology , vol.154 , pp. 2060-2069
    • Zhang, M.1    Sun, K.2    Sun, L.3
  • 26
    • 54949145378 scopus 로고    scopus 로고
    • Characterization of DegQVh, a serine protease and a protective immunogen from a pathogenic Vibrio harveyi strain
    • Zhang W.W., Sun K., Cheng S., Sun L. Characterization of DegQVh, a serine protease and a protective immunogen from a pathogenic Vibrio harveyi strain. Appl Environ Microbiol 2008, 74:6254-6262.
    • (2008) Appl Environ Microbiol , vol.74 , pp. 6254-6262
    • Zhang, W.W.1    Sun, K.2    Cheng, S.3    Sun, L.4
  • 27
    • 77949912897 scopus 로고    scopus 로고
    • Establishment of a primary liver cell culture from a teleost, Oreochromis mossambicus, the tilapia: a valid tool for physiological studies
    • A. Bernard (Ed.)
    • Schmid A., Kloas W., Reinecke M. Establishment of a primary liver cell culture from a teleost, Oreochromis mossambicus, the tilapia: a valid tool for physiological studies. Animal cell Technology: products from cells. Cells as products 1999, 143-145. A. Bernard (Ed.).
    • (1999) Animal cell Technology: products from cells. Cells as products , pp. 143-145
    • Schmid, A.1    Kloas, W.2    Reinecke, M.3
  • 28
    • 67651092389 scopus 로고    scopus 로고
    • Construction and evaluation of DNA vaccines encoding Edwardsiella tarda antigens
    • Jiao X., Zhang M., Hu Y., Sun L. Construction and evaluation of DNA vaccines encoding Edwardsiella tarda antigens. Vaccine 2009, 27:5195-5202.
    • (2009) Vaccine , vol.27 , pp. 5195-5202
    • Jiao, X.1    Zhang, M.2    Hu, Y.3    Sun, L.4
  • 29
    • 0032513056 scopus 로고    scopus 로고
    • Characterization of amammalian peroxiredoxin that contains one conserved cysteine
    • Kang S.W., Baines I.C., Rhee S.G. Characterization of amammalian peroxiredoxin that contains one conserved cysteine. J Biol Chem 1998, 273:6303-6311.
    • (1998) J Biol Chem , vol.273 , pp. 6303-6311
    • Kang, S.W.1    Baines, I.C.2    Rhee, S.G.3
  • 31
    • 0031807420 scopus 로고    scopus 로고
    • Cloning and expression of rat lung acidic Ca(2+)-independent PLA2 and its organ distribution
    • Kim T.S., Dodia C., Chen X., Hennigan B.B., Jain M., Feinstein S.I., et al. Cloning and expression of rat lung acidic Ca(2+)-independent PLA2 and its organ distribution. Am J Physiol 1998, 274:750-761.
    • (1998) Am J Physiol , vol.274 , pp. 750-761
    • Kim, T.S.1    Dodia, C.2    Chen, X.3    Hennigan, B.B.4    Jain, M.5    Feinstein, S.I.6
  • 32
    • 0344009504 scopus 로고    scopus 로고
    • 1-Cys peroxiredoxin knock-out mice express mRNA but not protein for a highly related intronless gene
    • Mo Y., Feinstein S.I., Manevich Y., Zhang Q., Lu L., Ho Y.S., et al. 1-Cys peroxiredoxin knock-out mice express mRNA but not protein for a highly related intronless gene. FEBS Lett 2003, 555:192-198.
    • (2003) FEBS Lett , vol.555 , pp. 192-198
    • Mo, Y.1    Feinstein, S.I.2    Manevich, Y.3    Zhang, Q.4    Lu, L.5    Ho, Y.S.6
  • 33
    • 38149076427 scopus 로고    scopus 로고
    • CDNA cloning, characterization, and expression analysis of channel catfish (Ictalurus punctatus Rafinesque, 1818) peroxiredoxin 6 gene
    • Yeh H.Y., Klesius P.H. cDNA cloning, characterization, and expression analysis of channel catfish (Ictalurus punctatus Rafinesque, 1818) peroxiredoxin 6 gene. Fish Physiol Biochem 2007, 33:233-239.
    • (2007) Fish Physiol Biochem , vol.33 , pp. 233-239
    • Yeh, H.Y.1    Klesius, P.H.2
  • 34
    • 33744939176 scopus 로고    scopus 로고
    • Oxidative stress response of European flounder (Platichthys flesus) to cadmium determined by a custom cDNA microarray
    • Sheader D.L., Williams T.D., Lyons B.P., Chipman J.K. Oxidative stress response of European flounder (Platichthys flesus) to cadmium determined by a custom cDNA microarray. Mar Environ Res 2006, 62:33-44.
    • (2006) Mar Environ Res , vol.62 , pp. 33-44
    • Sheader, D.L.1    Williams, T.D.2    Lyons, B.P.3    Chipman, J.K.4
  • 35
    • 50949128129 scopus 로고    scopus 로고
    • Gender-specific proteomic responses in zebrafish liver following exposure to a selected mixture of brominated flame retardants
    • Kling P., Norman A., Andersson P.L., Norrgren L., Förlin L. Gender-specific proteomic responses in zebrafish liver following exposure to a selected mixture of brominated flame retardants. Ecotoxicol Environ Saf 2008, 71:319-327.
    • (2008) Ecotoxicol Environ Saf , vol.71 , pp. 319-327
    • Kling, P.1    Norman, A.2    Andersson, P.L.3    Norrgren, L.4    Förlin, L.5
  • 36
    • 36549021015 scopus 로고    scopus 로고
    • A peroxiredoxin from kuruma shrimp, Marsupenaeus japonicus, inhibited by peptidoglycan
    • Bacano Maningas M.B., Koyama T., Kondo H., Hirono I., Aoki T. A peroxiredoxin from kuruma shrimp, Marsupenaeus japonicus, inhibited by peptidoglycan. Dev Comp Immunol 2008, 32:198-203.
    • (2008) Dev Comp Immunol , vol.32 , pp. 198-203
    • Bacano Maningas, M.B.1    Koyama, T.2    Kondo, H.3    Hirono, I.4    Aoki, T.5
  • 37
    • 33947380590 scopus 로고    scopus 로고
    • Roles of peroxiredoxin II in the regulation of proinflammatory responses to LPS and protection against endotoxin-induced lethal shock
    • Yang C.S., Lee D.S., Song C.H., An S.J., Li S., Kim J.M., et al. Roles of peroxiredoxin II in the regulation of proinflammatory responses to LPS and protection against endotoxin-induced lethal shock. J Exp Med 2007, 204:583-594.
    • (2007) J Exp Med , vol.204 , pp. 583-594
    • Yang, C.S.1    Lee, D.S.2    Song, C.H.3    An, S.J.4    Li, S.5    Kim, J.M.6


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