메뉴 건너뛰기




Volumn 146, Issue 4, 2007, Pages 688-694

Relationship between glutathione S-transferase, catalase, oxygen consumption, lipid peroxidation and oxidative stress in eggs and larvae of Boophilus microplus (Acarina: Ixodidae)

Author keywords

Boophilus microplus; Catalase; Embryonic development; Glutathione S transferases; Larval aging; Lipid peroxidation; Oxidative stress; Total glutathione

Indexed keywords

CATALASE; GLUTATHIONE TRANSFERASE; THIOBARBITURIC ACID REACTIVE SUBSTANCE;

EID: 33847632596     PISSN: 10956433     EISSN: 15314332     Source Type: Journal    
DOI: 10.1016/j.cbpa.2006.04.032     Document Type: Article
Times cited : (56)

References (48)
  • 1
    • 0021318441 scopus 로고
    • Catalase in vitro
    • Aebi H. Catalase in vitro. Methods Enzymol. 105 (1984) 121-126
    • (1984) Methods Enzymol. , vol.105 , pp. 121-126
    • Aebi, H.1
  • 2
    • 0037423744 scopus 로고    scopus 로고
    • Structure of a Drosophila sigma class glutathione S-transferase reveals a novel active site topography suited for lipid peroxidation products
    • Agianian B., Tucker P.A., Schouten A., Leonard K., Bullard B., and Gros P. Structure of a Drosophila sigma class glutathione S-transferase reveals a novel active site topography suited for lipid peroxidation products. J. Mol. Biol. 326 (2003) 151-165
    • (2003) J. Mol. Biol. , vol.326 , pp. 151-165
    • Agianian, B.1    Tucker, P.A.2    Schouten, A.3    Leonard, K.4    Bullard, B.5    Gros, P.6
  • 3
    • 0019740345 scopus 로고
    • Assay of glutathione, glutathione disulfide, and glutathione mixed disulfides in biological samples
    • Akerboom T.P., and Sies H. Assay of glutathione, glutathione disulfide, and glutathione mixed disulfides in biological samples. Methods Enzymol. 77 (1981) 373-382
    • (1981) Methods Enzymol. , vol.77 , pp. 373-382
    • Akerboom, T.P.1    Sies, H.2
  • 4
    • 0031021397 scopus 로고    scopus 로고
    • Structure, catalytic mechanism, and evolution of the glutathione S-transferase
    • Armstrong R.N. Structure, catalytic mechanism, and evolution of the glutathione S-transferase. Chem. Res. Toxicol. 10 (1997) 2-18
    • (1997) Chem. Res. Toxicol. , vol.10 , pp. 2-18
    • Armstrong, R.N.1
  • 6
    • 22044431761 scopus 로고    scopus 로고
    • Trace metal concentration, antioxidant enzyme activities and susceptibility to oxidative stress in the tricoptera larvae Hydropsyche exocellata from the Llobregat River Basin (NE Spain)
    • Barata C., Lekumberri I., Vila-Escale M., Prat N., and Porte C. Trace metal concentration, antioxidant enzyme activities and susceptibility to oxidative stress in the tricoptera larvae Hydropsyche exocellata from the Llobregat River Basin (NE Spain). Aquat. Toxicol. 74 (2005) 3-19
    • (2005) Aquat. Toxicol. , vol.74 , pp. 3-19
    • Barata, C.1    Lekumberri, I.2    Vila-Escale, M.3    Prat, N.4    Porte, C.5
  • 7
    • 0026485274 scopus 로고
    • Isolation of a Drosophila gene encoding glutathione S-transferase
    • Beall C., Fyrberg C., Song S., and Fyrberg E. Isolation of a Drosophila gene encoding glutathione S-transferase. Biochem. Genet. 30 (1992) 515-527
    • (1992) Biochem. Genet. , vol.30 , pp. 515-527
    • Beall, C.1    Fyrberg, C.2    Song, S.3    Fyrberg, E.4
  • 8
    • 0031439569 scopus 로고    scopus 로고
    • Zeta, a novel class of glutathione transferases in a range of species from plants to humans
    • Board P.G., Baker R.T., Chelvanayagam G., and Jermiin L.S. Zeta, a novel class of glutathione transferases in a range of species from plants to humans. Biochem. J. 328 (1997) 929-935
    • (1997) Biochem. J. , vol.328 , pp. 929-935
    • Board, P.G.1    Baker, R.T.2    Chelvanayagam, G.3    Jermiin, L.S.4
  • 9
    • 0030271356 scopus 로고    scopus 로고
    • Tick salivary prostaglandins: presence, origin and significance
    • Bowman A.S., Dillwith J.W., and Sauer J.R. Tick salivary prostaglandins: presence, origin and significance. Parasitol. Today 12 (1996) 388-396
    • (1996) Parasitol. Today , vol.12 , pp. 388-396
    • Bowman, A.S.1    Dillwith, J.W.2    Sauer, J.R.3
  • 10
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 11
    • 0042591480 scopus 로고    scopus 로고
    • Lipid peroxidation and antioxidant defence status during larval development and metamorphosis of giant prawn, Macrobrachium rosenbergii
    • Dandapat J., Chainy G.B., and Rao K.J. Lipid peroxidation and antioxidant defence status during larval development and metamorphosis of giant prawn, Macrobrachium rosenbergii. Comp. Biochem. Physiol. C 135 (2003) 221-233
    • (2003) Comp. Biochem. Physiol. C , vol.135 , pp. 221-233
    • Dandapat, J.1    Chainy, G.B.2    Rao, K.J.3
  • 13
    • 0024724977 scopus 로고
    • Effects of prolonged exposure at low temperature on Boophilus microplus (Acari: Ixodidae)
    • Davey R.B., and Cooksey L.M. Effects of prolonged exposure at low temperature on Boophilus microplus (Acari: Ixodidae). J. Med. Entomol. 26 (1989) 407-410
    • (1989) J. Med. Entomol. , vol.26 , pp. 407-410
    • Davey, R.B.1    Cooksey, L.M.2
  • 14
    • 0032198640 scopus 로고    scopus 로고
    • In vitro and in vivo evaluations of a strain of Boophilus microplus (Acari: Ixodidae) selected for resistance to permethrin
    • Davey R.B., and George J.E. In vitro and in vivo evaluations of a strain of Boophilus microplus (Acari: Ixodidae) selected for resistance to permethrin. J. Med. Entomol. 35 (1998) 1013-1019
    • (1998) J. Med. Entomol. , vol.35 , pp. 1013-1019
    • Davey, R.B.1    George, J.E.2
  • 15
    • 9144243812 scopus 로고    scopus 로고
    • The Anopheles gambiae glutathione transferase supergene family: annotation, phylogeny and expression profiles
    • Ding Y., Ortelli F., Rossiter L.C., Hemingway J., and Ranson H. The Anopheles gambiae glutathione transferase supergene family: annotation, phylogeny and expression profiles. BMC Genomics 4 (2003) 35
    • (2003) BMC Genomics , vol.4 , pp. 35
    • Ding, Y.1    Ortelli, F.2    Rossiter, L.C.3    Hemingway, J.4    Ranson, H.5
  • 17
    • 0025142672 scopus 로고
    • Malondialdehyde determination as index of lipid peroxidation
    • Draper H.H., and Hadley M. Malondialdehyde determination as index of lipid peroxidation. Methods Enzymol. 186 (1990) 421-431
    • (1990) Methods Enzymol. , vol.186 , pp. 421-431
    • Draper, H.H.1    Hadley, M.2
  • 19
    • 0016275313 scopus 로고
    • Glutathione S-transferases. The first enzymatic step in mercapturic acid formation
    • Habig W.H., Pabst M.J., and Jakoby W.B. Glutathione S-transferases. The first enzymatic step in mercapturic acid formation. J. Biol. Chem. 249 (1974) 7130-7139
    • (1974) J. Biol. Chem. , vol.249 , pp. 7130-7139
    • Habig, W.H.1    Pabst, M.J.2    Jakoby, W.B.3
  • 21
    • 0033179317 scopus 로고    scopus 로고
    • Characterization and molecular cloning of a glutathione S-transferase gene from the tick, Boophilus microplus (Acari: Ixodidae)
    • He H., Chen A.C., Davey R.B., Ivie G.W., and George J.E. Characterization and molecular cloning of a glutathione S-transferase gene from the tick, Boophilus microplus (Acari: Ixodidae). Insect Biochem. Mol. Biol. 29 (1999) 737-743
    • (1999) Insect Biochem. Mol. Biol. , vol.29 , pp. 737-743
    • He, H.1    Chen, A.C.2    Davey, R.B.3    Ivie, G.W.4    George, J.E.5
  • 22
    • 0033818365 scopus 로고    scopus 로고
    • The molecular basis of two contrasting metabolic mechanisms of insecticide resistance
    • Hemingway J. The molecular basis of two contrasting metabolic mechanisms of insecticide resistance. Insect Biochem. Mol. Biol. 30 (2000) 1009-1015
    • (2000) Insect Biochem. Mol. Biol. , vol.30 , pp. 1009-1015
    • Hemingway, J.1
  • 23
    • 0034751813 scopus 로고    scopus 로고
    • Mechanism, origin, and evolution of anoxia tolerance in animals
    • Hochachka P.W., and Lutz P.L. Mechanism, origin, and evolution of anoxia tolerance in animals. Comp. Biochem. Physiol. B 130 (2001) 435-459
    • (2001) Comp. Biochem. Physiol. B , vol.130 , pp. 435-459
    • Hochachka, P.W.1    Lutz, P.L.2
  • 24
    • 0034127336 scopus 로고    scopus 로고
    • Molecular and biochemical survey of acaricide resistance mechanisms in larvae from Mexican strains of the southern cattle tick, Boophilus microplus
    • Jamroz R.C., Guerrero F.D., Pruett J.H., Oehler D.D., and Miller R.J. Molecular and biochemical survey of acaricide resistance mechanisms in larvae from Mexican strains of the southern cattle tick, Boophilus microplus. J. Insect Physiol. 46 (2000) 685-695
    • (2000) J. Insect Physiol. , vol.46 , pp. 685-695
    • Jamroz, R.C.1    Guerrero, F.D.2    Pruett, J.H.3    Oehler, D.D.4    Miller, R.J.5
  • 28
    • 0038361352 scopus 로고    scopus 로고
    • Larval behavioral diapause regulates life cycle of Amblyomma cajennense (Acari: Ixodidae) in Southeast Brazil
    • Labruna M.B., Amaku M., Metzner J.Á., Pinter A., and Ferreira F. Larval behavioral diapause regulates life cycle of Amblyomma cajennense (Acari: Ixodidae) in Southeast Brazil. J. Med. Entomol. 40 (2003) 170-178
    • (2003) J. Med. Entomol. , vol.40 , pp. 170-178
    • Labruna, M.B.1    Amaku, M.2    Metzner, J.Á.3    Pinter, A.4    Ferreira, F.5
  • 30
  • 31
    • 0024392669 scopus 로고
    • The genetics of catalase in Drosophila melanogaster: isolation and characterization of acatalasemic mutants
    • Mackay W.J., and Bewley G.C. The genetics of catalase in Drosophila melanogaster: isolation and characterization of acatalasemic mutants. Genetics 122 (1989) 643-652
    • (1989) Genetics , vol.122 , pp. 643-652
    • Mackay, W.J.1    Bewley, G.C.2
  • 32
    • 1942533492 scopus 로고    scopus 로고
    • Gene and protein characterization of the human glutathione S-transferase Kappa and evidence for a peroxisomal localization
    • Morel F., Rauch C., Petit E., Piton A., Theret N., Coles B., and Guillouzo A. Gene and protein characterization of the human glutathione S-transferase Kappa and evidence for a peroxisomal localization. J. Biol. Chem. 279 (2004) 16246-16253
    • (2004) J. Biol. Chem. , vol.279 , pp. 16246-16253
    • Morel, F.1    Rauch, C.2    Petit, E.3    Piton, A.4    Theret, N.5    Coles, B.6    Guillouzo, A.7
  • 33
    • 0017395103 scopus 로고
    • On the use of the scrotum for feeding larval ixodid ticks on hosts
    • Ogunji F.O., and Dipeolu O.O. On the use of the scrotum for feeding larval ixodid ticks on hosts. Z. Parasitenkd. 51 (1977) 285-288
    • (1977) Z. Parasitenkd. , vol.51 , pp. 285-288
    • Ogunji, F.O.1    Dipeolu, O.O.2
  • 34
    • 11144279910 scopus 로고    scopus 로고
    • Effects of environmental anoxia and different periods of reoxygenation on oxidative balance in gills of the estuarine crab Chasmagnathus granulata
    • Oliveira U.O., Da Rosa Araujo A.S., Bello-Klein A., Da Silva R.S., and Kucharski L.C. Effects of environmental anoxia and different periods of reoxygenation on oxidative balance in gills of the estuarine crab Chasmagnathus granulata. Comp. Biochem. Physiol. B 140 (2005) 51-57
    • (2005) Comp. Biochem. Physiol. B , vol.140 , pp. 51-57
    • Oliveira, U.O.1    Da Rosa Araujo, A.S.2    Bello-Klein, A.3    Da Silva, R.S.4    Kucharski, L.C.5
  • 35
    • 8844240688 scopus 로고    scopus 로고
    • Glutathione S-transferase in the insect Apis mellifera macedonica kinetic characteristics and effect of stress on the expression of GST isoenzymes in the adult worker bee
    • Papadopoulos A.I., Polemitou I., Laifi P., Yiangou A., and Tananaki C. Glutathione S-transferase in the insect Apis mellifera macedonica kinetic characteristics and effect of stress on the expression of GST isoenzymes in the adult worker bee. Comp. Biochem. Physiol. C 139 (2004) 93-97
    • (2004) Comp. Biochem. Physiol. C , vol.139 , pp. 93-97
    • Papadopoulos, A.I.1    Polemitou, I.2    Laifi, P.3    Yiangou, A.4    Tananaki, C.5
  • 36
    • 0029239538 scopus 로고
    • Respiratory metabolism of the soft tick, Ornithodoros turicata (Duges)
    • Phillips J.S., Adeyeye O., and Bruni D. Respiratory metabolism of the soft tick, Ornithodoros turicata (Duges). Exp. Appl. Acarol. 19 (1995) 103-115
    • (1995) Exp. Appl. Acarol. , vol.19 , pp. 103-115
    • Phillips, J.S.1    Adeyeye, O.2    Bruni, D.3
  • 37
    • 0031593219 scopus 로고    scopus 로고
    • Lipid peroxidation, antioxidant protection and aging
    • Rikans L.E., and Hornbrook K.R. Lipid peroxidation, antioxidant protection and aging. Biochim. Biophys. Acta 1362 (1997) 116-127
    • (1997) Biochim. Biophys. Acta , vol.1362 , pp. 116-127
    • Rikans, L.E.1    Hornbrook, K.R.2
  • 38
    • 1942521481 scopus 로고    scopus 로고
    • Modelling and bioinformatics studies of the human Kappa-class glutathione transferase predict a novel third glutathione transferase family with similarity to prokaryotic 2-hydroxychromene-2-carboxylate isomerases
    • Robinson A., Huttley G.A., Booth H.S., and Board P.G. Modelling and bioinformatics studies of the human Kappa-class glutathione transferase predict a novel third glutathione transferase family with similarity to prokaryotic 2-hydroxychromene-2-carboxylate isomerases. Biochem. J. 379 (2004) 541-552
    • (2004) Biochem. J. , vol.379 , pp. 541-552
    • Robinson, A.1    Huttley, G.A.2    Booth, H.S.3    Board, P.G.4
  • 40
    • 0032955185 scopus 로고    scopus 로고
    • Glutathione S-transferases - a review
    • Salinas A.E., and Wong M.G. Glutathione S-transferases - a review. Curr. Med. Chem. 6 (1999) 279-309
    • (1999) Curr. Med. Chem. , vol.6 , pp. 279-309
    • Salinas, A.E.1    Wong, M.G.2
  • 42
    • 0035890484 scopus 로고    scopus 로고
    • Structure, function and evolution of glutathione transferase: implications for classification of non-mammalian members of an ancient enzyme superfamily
    • Sheehan D., Meade G., Foley V.M., and Dowd C.A. Structure, function and evolution of glutathione transferase: implications for classification of non-mammalian members of an ancient enzyme superfamily. Biochem. J. 360 (2001) 1-16
    • (2001) Biochem. J. , vol.360 , pp. 1-16
    • Sheehan, D.1    Meade, G.2    Foley, V.M.3    Dowd, C.A.4
  • 43
    • 0033230043 scopus 로고    scopus 로고
    • Glutathione and its role in cellular functions
    • Sies H. Glutathione and its role in cellular functions. Free Radic. Biol. Med. 27 (1999) 916-921
    • (1999) Free Radic. Biol. Med. , vol.27 , pp. 916-921
    • Sies, H.1
  • 47
    • 0035499462 scopus 로고    scopus 로고
    • Identification and cloning of a key insecticide-metabolizing glutathione S-transferase (MdGST-6A) from a hyperinsecticide-resistant strain of the housefly Musca domestica
    • Wei S.H., Clark A.G., and Syvanen M. Identification and cloning of a key insecticide-metabolizing glutathione S-transferase (MdGST-6A) from a hyperinsecticide-resistant strain of the housefly Musca domestica. Insect Biochem. Mol. Biol. 31 (2001) 1145-1153
    • (2001) Insect Biochem. Mol. Biol. , vol.31 , pp. 1145-1153
    • Wei, S.H.1    Clark, A.G.2    Syvanen, M.3
  • 48
    • 0029008514 scopus 로고
    • Glutathione transferases with novel active sites isolated by phage display from a library of random mutants
    • Widersten M., and Mannervik B. Glutathione transferases with novel active sites isolated by phage display from a library of random mutants. J. Mol. Biol. 250 (1995) 115-122
    • (1995) J. Mol. Biol. , vol.250 , pp. 115-122
    • Widersten, M.1    Mannervik, B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.