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Volumn 149, Issue 4, 2009, Pages 500-506

Increased level of superoxide dismutase (SOD) activity in larvae of Chironomus ramosus (Diptera: Chironomidae) subjected to ionizing radiation

Author keywords

Antioxidant enzymes; Chironomus ramosus; Ionizing radiation; Oxidative stress

Indexed keywords

CATALASE; COPPER ZINC SUPEROXIDE DISMUTASE; GLUTATHIONE PEROXIDASE; GLUTATHIONE REDUCTASE; ISOENZYME; MANGANESE SUPEROXIDE DISMUTASE; SUPEROXIDE DISMUTASE;

EID: 63449125586     PISSN: 15320456     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbpc.2008.11.003     Document Type: Article
Times cited : (46)

References (48)
  • 1
    • 39749091799 scopus 로고    scopus 로고
    • The kinetic mechanism of manganese-containing superoxide dismutase from Dienococcus radiodurans: a specialized enzyme for elimination of high superoxide concentrations
    • Abreu I.A., Hearn A., An H., Nick H.S., Silverman D.N., and Cabelli D.E. The kinetic mechanism of manganese-containing superoxide dismutase from Dienococcus radiodurans: a specialized enzyme for elimination of high superoxide concentrations. Biochemistry 47 (2008) 2350-2356
    • (2008) Biochemistry , vol.47 , pp. 2350-2356
    • Abreu, I.A.1    Hearn, A.2    An, H.3    Nick, H.S.4    Silverman, D.N.5    Cabelli, D.E.6
  • 2
    • 0000024076 scopus 로고
    • Catalase
    • Bergmeyer H.U. (Ed), Verlag, Weinheim
    • Aebi H.E. Catalase. In: Bergmeyer H.U. (Ed). Methods of Enzymatic Analysis (1983), Verlag, Weinheim 273-286
    • (1983) Methods of Enzymatic Analysis , pp. 273-286
    • Aebi, H.E.1
  • 3
    • 0001750578 scopus 로고
    • Biochemical defense of pro-oxidant plant allelochemicals by herbivorous insects
    • Ahmad S. Biochemical defense of pro-oxidant plant allelochemicals by herbivorous insects. Biochem. Ecol. System. 20 (1992) 269-296
    • (1992) Biochem. Ecol. System. , vol.20 , pp. 269-296
    • Ahmad, S.1
  • 4
    • 0001414007 scopus 로고
    • Antioxidant mechanisms of the enzymes and proteins
    • Ahmad S. (Ed), Chapman and Hall, New York
    • Ahmad S. Antioxidant mechanisms of the enzymes and proteins. In: Ahmad S. (Ed). Oxidative stress and Antioxidant Defense in Biology (1995), Chapman and Hall, New York 238-272
    • (1995) Oxidative stress and Antioxidant Defense in Biology , pp. 238-272
    • Ahmad, S.1
  • 5
    • 0003529594 scopus 로고
    • Armitage P., Cranston P.S., and Pinder L.C.V. (Eds), Chapman and Hall, London
    • In: Armitage P., Cranston P.S., and Pinder L.C.V. (Eds). Chironomidae: Biology and Ecology of Non-biting Midges (1995), Chapman and Hall, London
    • (1995) Chironomidae: Biology and Ecology of Non-biting Midges
  • 6
    • 0035990056 scopus 로고    scopus 로고
    • Gut-based antioxidant enzymes in a polyphagous and a graminivorous grasshopper
    • Barbehenn R.V. Gut-based antioxidant enzymes in a polyphagous and a graminivorous grasshopper. J. Chem. Ecol. 28 (2002) 1329-1347
    • (2002) J. Chem. Ecol. , vol.28 , pp. 1329-1347
    • Barbehenn, R.V.1
  • 7
    • 0015153416 scopus 로고
    • Super oxide dismutase: improved assays and assay applicable to acrylamide gels
    • Beauchamp C., and Fridovich I. Super oxide dismutase: improved assays and assay applicable to acrylamide gels. Anal. Biochem. 44 (1971) 276-287
    • (1971) Anal. Biochem. , vol.44 , pp. 276-287
    • Beauchamp, C.1    Fridovich, I.2
  • 8
    • 0036281117 scopus 로고    scopus 로고
    • Effect of temperature and pirimiphos methyl on biochemical biomarkers in Chironomus riparius Meigen
    • Callaghan A., Thomas C., Albania F., Grosso G., Holloway J., and Crane M. Effect of temperature and pirimiphos methyl on biochemical biomarkers in Chironomus riparius Meigen. Ecotoxicol. Environ. Saf. 52 (2002) 128-133
    • (2002) Ecotoxicol. Environ. Saf. , vol.52 , pp. 128-133
    • Callaghan, A.1    Thomas, C.2    Albania, F.3    Grosso, G.4    Holloway, J.5    Crane, M.6
  • 9
    • 0035952333 scopus 로고    scopus 로고
    • A simple technique for simultaneous determination of molecular weight and activity of superoxide dismutase using SDS-PAGE
    • Chen J.R., Liao C.W., Simon J.T., Chen T.H., and Weng C.N. A simple technique for simultaneous determination of molecular weight and activity of superoxide dismutase using SDS-PAGE. J. Biochem. Biophys. Methods. 47 (2001) 233-237
    • (2001) J. Biochem. Biophys. Methods. , vol.47 , pp. 233-237
    • Chen, J.R.1    Liao, C.W.2    Simon, J.T.3    Chen, T.H.4    Weng, C.N.5
  • 10
    • 0032832795 scopus 로고    scopus 로고
    • Characterization of superoxide dismutase activity in Chironomus riparius Mg. (Diptera, Chironomidae) larvae - a potential biomarker
    • Choi J., Roche H., and Caquet T. Characterization of superoxide dismutase activity in Chironomus riparius Mg. (Diptera, Chironomidae) larvae - a potential biomarker. Comp. Biochem. Physiol. C: Pharmacol. Toxicol. Endochrinol. 124 (1999) 73-81
    • (1999) Comp. Biochem. Physiol. C: Pharmacol. Toxicol. Endochrinol. , vol.124 , pp. 73-81
    • Choi, J.1    Roche, H.2    Caquet, T.3
  • 11
    • 0034107817 scopus 로고    scopus 로고
    • Effects of physical (hypoxia,hyperoxia) and chemical (potassium dichromate, fentrothion) stress on antioxidant enzyme activities in Chironomus riparus Mg. (Diptera, Chironomidae) larvae: potential biomarkers
    • Choi J., Roche H., and Caquet T. Effects of physical (hypoxia,hyperoxia) and chemical (potassium dichromate, fentrothion) stress on antioxidant enzyme activities in Chironomus riparus Mg. (Diptera, Chironomidae) larvae: potential biomarkers. Environ. Toxicol. Chem. 19 (2000) 495-500
    • (2000) Environ. Toxicol. Chem. , vol.19 , pp. 495-500
    • Choi, J.1    Roche, H.2    Caquet, T.3
  • 12
    • 43049162537 scopus 로고    scopus 로고
    • Exposure of Chironomus riparus larvae to uranium: effects on survival, development time, growth, and mouthpart deformities
    • Dias V., Vasseur C., and Bonzom J.M. Exposure of Chironomus riparus larvae to uranium: effects on survival, development time, growth, and mouthpart deformities. Chemosphere 71 (2008) 574-581
    • (2008) Chemosphere , vol.71 , pp. 574-581
    • Dias, V.1    Vasseur, C.2    Bonzom, J.M.3
  • 16
    • 0001528839 scopus 로고
    • Glutathione reductase
    • Bergemeyer H.U. (Ed), Verlag, Basel Chemie
    • Goldberg D.M., and Spooner R.J. Glutathione reductase. In: Bergemeyer H.U. (Ed). Methods in Enzymology vol. 3. (1983), Verlag, Basel 258-265 Chemie
    • (1983) Methods in Enzymology , vol.3 , pp. 258-265
    • Goldberg, D.M.1    Spooner, R.J.2
  • 18
    • 33751084912 scopus 로고    scopus 로고
    • Sub-lethal and chronic salinity tolerances of three freshwater insects: Cloeon sp. and Centroptilum sp. (Ephemeroptera: Baetidae) and Chironomus sp. (Diptera: Chironomidae)
    • Hassell K.L., Kefford B.J., and Nugegoda D. Sub-lethal and chronic salinity tolerances of three freshwater insects: Cloeon sp. and Centroptilum sp. (Ephemeroptera: Baetidae) and Chironomus sp. (Diptera: Chironomidae). J. Exp. Biol. 209 (2006) 4024-4032
    • (2006) J. Exp. Biol. , vol.209 , pp. 4024-4032
    • Hassell, K.L.1    Kefford, B.J.2    Nugegoda, D.3
  • 19
    • 0036892444 scopus 로고    scopus 로고
    • Animal response to drastic changes in oxygen availability and physiological oxidative stress
    • Hermes-Lima M., and Zenteno-Savi{dotless}n T. Animal response to drastic changes in oxygen availability and physiological oxidative stress. Comp. Biochem. Physiol. C: Toxicol. Pharmacol. 133 (2002) 537-556
    • (2002) Comp. Biochem. Physiol. C: Toxicol. Pharmacol. , vol.133 , pp. 537-556
    • Hermes-Lima, M.1    Zenteno-Savin, T.2
  • 21
    • 0037284273 scopus 로고    scopus 로고
    • Activities of superoxide dismutase and glutathione peroxidase in leaves of different cultivars of Liriope spicata L. on 10% SDS-PAGE gels
    • Hou W.C., Lu Y.L., Liu S.Y., and Lin Y.H. Activities of superoxide dismutase and glutathione peroxidase in leaves of different cultivars of Liriope spicata L. on 10% SDS-PAGE gels. Bot. Bull. Acad. Sin. 44 (2003) 37-41
    • (2003) Bot. Bull. Acad. Sin. , vol.44 , pp. 37-41
    • Hou, W.C.1    Lu, Y.L.2    Liu, S.Y.3    Lin, Y.H.4
  • 23
    • 0017067418 scopus 로고
    • Glutathione peroxidase activity in selenium deficient rat liver
    • Lawrence R.A., and Burk R.F. Glutathione peroxidase activity in selenium deficient rat liver. Biochem. Biophys. Res. Commun. 71 (1976) 952-958
    • (1976) Biochem. Biophys. Res. Commun. , vol.71 , pp. 952-958
    • Lawrence, R.A.1    Burk, R.F.2
  • 24
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227 (1970) 680-685
    • (1970) Nature. , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 25
    • 34447573968 scopus 로고    scopus 로고
    • Effects of bisphenol A and ethynyl estradiol exposure on enzyme activities, growth and development in the fourth instar larvae of Chironomus riparus (Diptera: Chironomidae)
    • Lee S.B., and Choi J. Effects of bisphenol A and ethynyl estradiol exposure on enzyme activities, growth and development in the fourth instar larvae of Chironomus riparus (Diptera: Chironomidae). Ecotoxicol. Environ. Saf. 68 (2007) 84-90
    • (2007) Ecotoxicol. Environ. Saf. , vol.68 , pp. 84-90
    • Lee, S.B.1    Choi, J.2
  • 26
    • 0000160668 scopus 로고
    • Antioxidant enzymes in the digestive gland of the common mussel Mytilus edulis
    • Livingstone D.R., Lips F., Martinez P.G., and Pipe R.K. Antioxidant enzymes in the digestive gland of the common mussel Mytilus edulis. Mar. Biol. 112 (1992) 265-276
    • (1992) Mar. Biol. , vol.112 , pp. 265-276
    • Livingstone, D.R.1    Lips, F.2    Martinez, P.G.3    Pipe, R.K.4
  • 29
    • 0016252209 scopus 로고
    • Effects of superoxide radicals on myoblast growth and differentiation
    • Michelson A.M., and Buckingham M.E. Effects of superoxide radicals on myoblast growth and differentiation. Biochem. Biophys. Res. Commun. 58 (1974) 1079-1086
    • (1974) Biochem. Biophys. Res. Commun. , vol.58 , pp. 1079-1086
    • Michelson, A.M.1    Buckingham, M.E.2
  • 30
    • 0342790993 scopus 로고    scopus 로고
    • Technique for mass rearing of Indian Chironomus species
    • Nath B.B., and Godbole N.N. Technique for mass rearing of Indian Chironomus species. Studia Dipterol. 5 (1998) 187-193
    • (1998) Studia Dipterol. , vol.5 , pp. 187-193
    • Nath, B.B.1    Godbole, N.N.2
  • 31
    • 36049026782 scopus 로고    scopus 로고
    • Consequences of inbreeding and reduced genetic variation on tolerance to cadmium stress in the midge Chironomus riparius
    • Nowak C., Jost D., Vogt C., Oetken M., Schwenk K., and Oehlmann J. Consequences of inbreeding and reduced genetic variation on tolerance to cadmium stress in the midge Chironomus riparius. Aquat. Toxicol. 85 (2007) 278-284
    • (2007) Aquat. Toxicol. , vol.85 , pp. 278-284
    • Nowak, C.1    Jost, D.2    Vogt, C.3    Oetken, M.4    Schwenk, K.5    Oehlmann, J.6
  • 33
    • 63449092022 scopus 로고    scopus 로고
    • Peculiarities of radio nuclide accumulation by the representatives of "soft" benthos after the Chernobyl accident
    • Pankov I.V., and Andreev A.D. Peculiarities of radio nuclide accumulation by the representatives of "soft" benthos after the Chernobyl accident. Gidrobiol. Zhu 35 (1999) 81-89
    • (1999) Gidrobiol. Zhu , vol.35 , pp. 81-89
    • Pankov, I.V.1    Andreev, A.D.2
  • 34
    • 0022666536 scopus 로고
    • Irradiation-resistance conferred by superoxide dismutase: possible adaptive role of a natural polymorphism in Drosophila melanogaster
    • Peng T., Xu M.A., and Ayala F.J. Irradiation-resistance conferred by superoxide dismutase: possible adaptive role of a natural polymorphism in Drosophila melanogaster. Proc. Natl. Acad. Sci. U. S. A. 83 (1986) 684-687
    • (1986) Proc. Natl. Acad. Sci. U. S. A. , vol.83 , pp. 684-687
    • Peng, T.1    Xu, M.A.2    Ayala, F.J.3
  • 37
    • 33847096515 scopus 로고    scopus 로고
    • Many faces of superoxide dismutase, originally known as erythrocuprein
    • Ramasarma T. Many faces of superoxide dismutase, originally known as erythrocuprein. Curr. Sci. 92 (2007) 184-191
    • (2007) Curr. Sci. , vol.92 , pp. 184-191
    • Ramasarma, T.1
  • 39
    • 0002696602 scopus 로고
    • Oxygen stress and superoxide dismutases
    • Scandalios J.G. Oxygen stress and superoxide dismutases. Plant Physiol. 101 (1993) 7-12
    • (1993) Plant Physiol. , vol.101 , pp. 7-12
    • Scandalios, J.G.1
  • 40
    • 0023891014 scopus 로고
    • The role of redox in the regulation of manganese containing superoxide dismutase biosynthesis in Escherichia coli
    • Schiavone J.R., and Hassan H.M. The role of redox in the regulation of manganese containing superoxide dismutase biosynthesis in Escherichia coli. J. Biol. Chem. 263 (1988) 4269-4273
    • (1988) J. Biol. Chem. , vol.263 , pp. 4269-4273
    • Schiavone, J.R.1    Hassan, H.M.2
  • 41
    • 0035989388 scopus 로고    scopus 로고
    • Induced overexpression of mitochondrial Mn-superoxide dismutase extends the life span of adult Drosophila melanogaster
    • Sun J., Folk D., Bradley T.J., and Tower J. Induced overexpression of mitochondrial Mn-superoxide dismutase extends the life span of adult Drosophila melanogaster. Genetics. 161 (2002) 661-672
    • (2002) Genetics. , vol.161 , pp. 661-672
    • Sun, J.1    Folk, D.2    Bradley, T.J.3    Tower, J.4
  • 42
    • 0001072593 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose: procedure and some applications
    • Towbin H., Staehelin T., and Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose: procedure and some applications. Proc. Natl. Acad. Sci. U. S. A. 83 (1979) 4849-4853
    • (1979) Proc. Natl. Acad. Sci. U. S. A. , vol.83 , pp. 4849-4853
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 43
    • 0016794741 scopus 로고
    • Inactivation of biologically active DNA by gamma-ray-induced superoxide radicals and their dismutation products singlet molecular oxygen and hydrogen peroxide
    • Van Hemmen J.J., and Meuling W.J.A. Inactivation of biologically active DNA by gamma-ray-induced superoxide radicals and their dismutation products singlet molecular oxygen and hydrogen peroxide. Biochim. Biophys. Acta 402 (1975) 133-141
    • (1975) Biochim. Biophys. Acta , vol.402 , pp. 133-141
    • Van Hemmen, J.J.1    Meuling, W.J.A.2
  • 44
    • 33947324211 scopus 로고    scopus 로고
    • Multi-generation studies with Chironomus riparius - effects of low tributyltin concentrations on life history parameters and genetic diversity
    • Vogt C., Nowak C., Diogo J.B., Oetken M., Schwenk K., and Oehlmann J. Multi-generation studies with Chironomus riparius - effects of low tributyltin concentrations on life history parameters and genetic diversity. Chemosphere 67 (2007) 2192-2200
    • (2007) Chemosphere , vol.67 , pp. 2192-2200
    • Vogt, C.1    Nowak, C.2    Diogo, J.B.3    Oetken, M.4    Schwenk, K.5    Oehlmann, J.6
  • 45
    • 0015848173 scopus 로고
    • Superoxide dismutase organelle specificity
    • Weisiger R.A., and Fridovich I. Superoxide dismutase organelle specificity. J. Biol.Chem. 248 (1973) 3582-3592
    • (1973) J. Biol.Chem. , vol.248 , pp. 3582-3592
    • Weisiger, R.A.1    Fridovich, I.2
  • 46
    • 0035030505 scopus 로고    scopus 로고
    • Morphological deformities occurring in Belarusian Chironomids (Diptera; Chironomidae) subsequent to the Chernobyl nuclear disaster
    • Williams D.D., Nesterovitch A.I., Travares A.F., and Muzzetti E.G. Morphological deformities occurring in Belarusian Chironomids (Diptera; Chironomidae) subsequent to the Chernobyl nuclear disaster. Freshw. Biol. 46 (2001) 503-512
    • (2001) Freshw. Biol. , vol.46 , pp. 503-512
    • Williams, D.D.1    Nesterovitch, A.I.2    Travares, A.F.3    Muzzetti, E.G.4
  • 47
    • 42249088093 scopus 로고    scopus 로고
    • Reconciling the chemistry and biology of the reactive oxygen species
    • Winterbourn C.C. Reconciling the chemistry and biology of the reactive oxygen species. Nat. Chem. Biol. 4 (2008) 278-286
    • (2008) Nat. Chem. Biol. , vol.4 , pp. 278-286
    • Winterbourn, C.C.1


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