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Volumn 150, Issue 4, 2009, Pages 528-536

Glutathione S-transferase as a biomarker in the Antarctic bivalve Laternula elliptica after exposure to the polychlorinated biphenyl mixture Aroclor 1254

Author keywords

Antarctic; Glutathione S transferases; Induction; Laternula elliptica; Polychlorinated biphenyls

Indexed keywords

AROCLOR 1254; BIOLOGICAL MARKER; GLUTATHIONE; GLUTATHIONE TRANSFERASE; POLYCHLORINATED BIPHENYL; RECOMBINANT ENZYME;

EID: 70149104458     PISSN: 15320456     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbpc.2009.07.008     Document Type: Article
Times cited : (37)

References (45)
  • 1
    • 0030576586 scopus 로고    scopus 로고
    • Baseline heavy metal concentrations in the Antarctic clam, Laternula elliptica in Maxwell Bay, King George Island. Antarctica.
    • Ahn I.Y., Lee S.H., Kim K.T., Shim J.H., and Kim D.-Y. Baseline heavy metal concentrations in the Antarctic clam, Laternula elliptica in Maxwell Bay, King George Island. Antarctica. Mar. Pollut. Bull. 32 (1996) 592-598
    • (1996) Mar. Pollut. Bull. , vol.32 , pp. 592-598
    • Ahn, I.Y.1    Lee, S.H.2    Kim, K.T.3    Shim, J.H.4    Kim, D.-Y.5
  • 2
    • 34047182460 scopus 로고    scopus 로고
    • Glutathione S-tranferases and cytochrome P450 activities in Mytilus galloprovincialis from the South coast of Portugal: effect of abiotic factors
    • Bebianno M.J., Lopes B., Guerra L., Hoarau P., and Ferreira A.M. Glutathione S-tranferases and cytochrome P450 activities in Mytilus galloprovincialis from the South coast of Portugal: effect of abiotic factors. Environ. Int. 33 (2007) 550-558
    • (2007) Environ. Int. , vol.33 , pp. 550-558
    • Bebianno, M.J.1    Lopes, B.2    Guerra, L.3    Hoarau, P.4    Ferreira, A.M.5
  • 4
    • 11244303549 scopus 로고    scopus 로고
    • Characterisation and expression of four mRNA sequences encoding glutathione S-transferases pi, mu, omega and sigma classes in the Pacific oyster Crassostrea gigas exposed to hydrocarbons and pesticides
    • Boutet I., Tanguy A., and Moraga D. Characterisation and expression of four mRNA sequences encoding glutathione S-transferases pi, mu, omega and sigma classes in the Pacific oyster Crassostrea gigas exposed to hydrocarbons and pesticides. Mar. Biol. 146 (2004) 53-64
    • (2004) Mar. Biol. , vol.146 , pp. 53-64
    • Boutet, I.1    Tanguy, A.2    Moraga, D.3
  • 5
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M.M., 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 72, 248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 6
    • 0027058697 scopus 로고
    • Glutathione S-transferases: amino acid sequence comparison, classification and phylogenic relationship
    • Buetler T.M., and Eaton D.L. Glutathione S-transferases: amino acid sequence comparison, classification and phylogenic relationship. J. Environ. Sci. Health C. Environ. Carcino. Ecotoxicol. 10 (1992) 181-203
    • (1992) J. Environ. Sci. Health C. Environ. Carcino. Ecotoxicol. , vol.10 , pp. 181-203
    • Buetler, T.M.1    Eaton, D.L.2
  • 7
    • 0025271344 scopus 로고
    • Homologous nuclear genes encode cytoplasmic and mitochondrial glutamine synthetase in Drosophila melanogaster
    • Caizzi R., Bozzetti M.P., Caggese C., and Ritossa F. Homologous nuclear genes encode cytoplasmic and mitochondrial glutamine synthetase in Drosophila melanogaster. J. Mol. Biol. 212 (1990) 17-26
    • (1990) J. Mol. Biol. , vol.212 , pp. 17-26
    • Caizzi, R.1    Bozzetti, M.P.2    Caggese, C.3    Ritossa, F.4
  • 9
    • 0028224013 scopus 로고
    • X-ray crystal structures of cytosolic glutathione S-transferases. Implications for protein architecture, substrate recognition and catalytic function
    • Dirr H., Reinemer P., and Huber R. X-ray crystal structures of cytosolic glutathione S-transferases. Implications for protein architecture, substrate recognition and catalytic function. Eur. J. Biochem. 220 (1994) 645-661
    • (1994) Eur. J. Biochem. , vol.220 , pp. 645-661
    • Dirr, H.1    Reinemer, P.2    Huber, R.3
  • 10
    • 20444390679 scopus 로고    scopus 로고
    • cDNA cloning and expression pattern of pi-class glutathione S-transferase in the freshwater bivalves Unio tumidus and Corbicula fluminea
    • Doyen P., Vasseur P., and Rodius F. cDNA cloning and expression pattern of pi-class glutathione S-transferase in the freshwater bivalves Unio tumidus and Corbicula fluminea. Comp. Biochem. Physiol. C. Toxicol. Pharmacol. 140 (2005) 300-308
    • (2005) Comp. Biochem. Physiol. C. Toxicol. Pharmacol. , vol.140 , pp. 300-308
    • Doyen, P.1    Vasseur, P.2    Rodius, F.3
  • 11
    • 0033038758 scopus 로고    scopus 로고
    • Concise review of the glutathione S-transferases and their significance to toxicology
    • Eaton D.L., and Bammler T.K. Concise review of the glutathione S-transferases and their significance to toxicology. Toxicol. Sci. 49 (1999) 156-164
    • (1999) Toxicol. Sci. , vol.49 , pp. 156-164
    • Eaton, D.L.1    Bammler, T.K.2
  • 12
    • 33845202244 scopus 로고    scopus 로고
    • Identification and expression of a novel class of glutathione-S-transferase from amphioxus Branchiostoma belcheri with implications to the origin of vertebrate liver
    • Fan C., Zhang S., Liu Z., Li L., Luan J., and Saren G. Identification and expression of a novel class of glutathione-S-transferase from amphioxus Branchiostoma belcheri with implications to the origin of vertebrate liver. Int. J. Biochem. Cell Biol. 39 (2007) 450-461
    • (2007) Int. J. Biochem. Cell Biol. , vol.39 , pp. 450-461
    • Fan, C.1    Zhang, S.2    Liu, Z.3    Li, L.4    Luan, J.5    Saren, G.6
  • 13
    • 1242319304 scopus 로고    scopus 로고
    • Increasing levels and biomagnification of persistent organic pollutants (POPs) in Antarctic biota
    • Goerke H., Weber K., Bornemann H., Ramdohr S., and Plotz J. Increasing levels and biomagnification of persistent organic pollutants (POPs) in Antarctic biota. Mar. Pollut. Bull. 48 (2004) 295-302
    • (2004) Mar. Pollut. Bull. , vol.48 , pp. 295-302
    • Goerke, H.1    Weber, K.2    Bornemann, H.3    Ramdohr, S.4    Plotz, J.5
  • 14
    • 0034689586 scopus 로고    scopus 로고
    • Beyond the Mussel Watch-new directions for monitoring marine pollution
    • Goldberg E.D., and Bertine K.K. Beyond the Mussel Watch-new directions for monitoring marine pollution. Sci. Total Environ. 247 (2000) 165-174
    • (2000) Sci. Total Environ. , vol.247 , pp. 165-174
    • Goldberg, E.D.1    Bertine, K.K.2
  • 15
    • 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
  • 17
    • 33747892586 scopus 로고    scopus 로고
    • Cloning and expression of a GST-pi gene in Mytilus galloprovincialis. Attempt to use the GST-pi transcript as a biomarker of pollution
    • Hoarau P., Damiens G., Romeo M., Gnassia-Barelli M., and Bebianno M.J. Cloning and expression of a GST-pi gene in Mytilus galloprovincialis. Attempt to use the GST-pi transcript as a biomarker of pollution. Comp. Biochem. Physiol. C. Toxicol. Pharmacol. 143 (2006) 196-203
    • (2006) Comp. Biochem. Physiol. C. Toxicol. Pharmacol. , vol.143 , pp. 196-203
    • Hoarau, P.1    Damiens, G.2    Romeo, M.3    Gnassia-Barelli, M.4    Bebianno, M.J.5
  • 18
    • 0037424257 scopus 로고    scopus 로고
    • Identification of residues in glutathione transferase capable of driving functional diversification in evolution. A novel approach to protein redesign.
    • Ivarsson Y., Mackey A.J., Edalat M., Pearson W.R., and Mannervik B. Identification of residues in glutathione transferase capable of driving functional diversification in evolution. A novel approach to protein redesign. J. Biol. Chem. 278 (2003) 8733-8738
    • (2003) J. Biol. Chem. , vol.278 , pp. 8733-8738
    • Ivarsson, Y.1    Mackey, A.J.2    Edalat, M.3    Pearson, W.R.4    Mannervik, B.5
  • 19
    • 0030748102 scopus 로고    scopus 로고
    • Structure and function of the xenobiotic substrate-binding site and location of a potential non-substrate-binding site in a class pi glutathione S-transferase
    • Ji X., Tordova M., O'Donnell R., Parsons J.F., Hayden J.B., Gilliland G.L., and Zimniak P. Structure and function of the xenobiotic substrate-binding site and location of a potential non-substrate-binding site in a class pi glutathione S-transferase. Biochemistry 36 (1997) 9690-9702
    • (1997) Biochemistry , vol.36 , pp. 9690-9702
    • Ji, X.1    Tordova, M.2    O'Donnell, R.3    Parsons, J.F.4    Hayden, J.B.5    Gilliland, G.L.6    Zimniak, P.7
  • 21
    • 57649134499 scopus 로고    scopus 로고
    • Molecular cloning and thermal stress-induced expression of a pi-class glutathione S-transferase (GST) in the Antarctic bivalve Laternula elliptica
    • Kim M., Ahn I.Y., Cheon J., and Park H. Molecular cloning and thermal stress-induced expression of a pi-class glutathione S-transferase (GST) in the Antarctic bivalve Laternula elliptica. Comp. Biochem. Physiol. A Mol. Integr. Physiol. 152 (2008) 207-213
    • (2008) Comp. Biochem. Physiol. A Mol. Integr. Physiol. , vol.152 , pp. 207-213
    • Kim, M.1    Ahn, I.Y.2    Cheon, J.3    Park, H.4
  • 22
    • 19544377786 scopus 로고    scopus 로고
    • A new class of glutathione S-transferase from the hepatopancreas of the red sea bream Pagrus major
    • Konishi T., Kato K., Araki T., Shiraki K., Takagi M., and Tamaru Y. A new class of glutathione S-transferase from the hepatopancreas of the red sea bream Pagrus major. Biochem. J. 388 (2005) 299-307
    • (2005) Biochem. J. , vol.388 , pp. 299-307
    • Konishi, T.1    Kato, K.2    Araki, T.3    Shiraki, K.4    Takagi, M.5    Tamaru, Y.6
  • 23
    • 0036009839 scopus 로고    scopus 로고
    • Polychlorinated dibenzo-p-dioxins, dibenzofurans and polychlorinated biphenyls in polar bear, penguin and south polar skua
    • Kumar K.S., Kannan K., Corsolini S., Evans T., Giesy J.P., Nakanishi J., and Masunaga S. Polychlorinated dibenzo-p-dioxins, dibenzofurans and polychlorinated biphenyls in polar bear, penguin and south polar skua. Environ. Pollut. 119 (2002) 151-161
    • (2002) Environ. Pollut. , vol.119 , pp. 151-161
    • Kumar, K.S.1    Kannan, K.2    Corsolini, S.3    Evans, T.4    Giesy, J.P.5    Nakanishi, J.6    Masunaga, S.7
  • 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
    • 0037866875 scopus 로고    scopus 로고
    • Induction of glutathione-S-transferases in primary cultured digestive gland acini from the mollusk bivalve Pecten maximus (L.): application of a new cellular model in biomonitoring studies
    • Le Pennec G., and Le Pennec M. Induction of glutathione-S-transferases in primary cultured digestive gland acini from the mollusk bivalve Pecten maximus (L.): application of a new cellular model in biomonitoring studies. Aquat. Toxicol. 64 (2003) 131-142
    • (2003) Aquat. Toxicol. , vol.64 , pp. 131-142
    • Le Pennec, G.1    Le Pennec, M.2
  • 26
    • 0027232557 scopus 로고
    • Cloning and characterization of the major hepatic glutathione S-transferase from a marine teleost flatfish, the plaice (Pleuronectes platessa), with structural similarities to plant, insect and mammalian Theta class isoenzymes
    • Leaver M.J., Scott K., and George S.G. Cloning and characterization of the major hepatic glutathione S-transferase from a marine teleost flatfish, the plaice (Pleuronectes platessa), with structural similarities to plant, insect and mammalian Theta class isoenzymes. Biochem. J. 292 (1993) 189-195
    • (1993) Biochem. J. , vol.292 , pp. 189-195
    • Leaver, M.J.1    Scott, K.2    George, S.G.3
  • 27
    • 0022555842 scopus 로고
    • Complex transcriptional units: diversity in gene expression by alternative RNA processing
    • Leff S.E., Rosenfeld M.G., and Evans R.M. Complex transcriptional units: diversity in gene expression by alternative RNA processing. Annu. Rev. Biochem. 55 (1986) 1091-1117
    • (1986) Annu. Rev. Biochem. , vol.55 , pp. 1091-1117
    • Leff, S.E.1    Rosenfeld, M.G.2    Evans, R.M.3
  • 29
    • 0345487502 scopus 로고    scopus 로고
    • Biochemical markers for differentiation of exposures to nonplanar polychlorinated biphenyls, organochlorine pesticides, or 2,3,7, 8-tetrachlorodibenzo-p-dioxin in trout liver
    • Machala M., Drabek P., Neca J., Kolarova J., and Svobodova Z. Biochemical markers for differentiation of exposures to nonplanar polychlorinated biphenyls, organochlorine pesticides, or 2,3,7, 8-tetrachlorodibenzo-p-dioxin in trout liver. Ecotoxicol. Environ. Saf. 41 (1998) 107-111
    • (1998) Ecotoxicol. Environ. Saf. , vol.41 , pp. 107-111
    • Machala, M.1    Drabek, P.2    Neca, J.3    Kolarova, J.4    Svobodova, Z.5
  • 30
    • 0024269217 scopus 로고
    • Glutathione transferases-structure and catalytic activity
    • Mannervik B., and Danielson U.H. Glutathione transferases-structure and catalytic activity. CRC Crit. Rev. Biochem. 23 (1988) 283-337
    • (1988) CRC Crit. Rev. Biochem. , vol.23 , pp. 283-337
    • Mannervik, B.1    Danielson, U.H.2
  • 32
    • 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., and Kim M. Analysis of ESTs and expression of two peroxiredoxins in the thermally stressed Antarctic bivalve Laternula elliptica. Fish Shellfish Immunol. 25 (2008) 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
  • 34
    • 30144434095 scopus 로고    scopus 로고
    • Phylogenies of glutathione transferase families
    • Pearson W.R. Phylogenies of glutathione transferase families. Methods Enzymol. 401 (2005) 186-204
    • (2005) Methods Enzymol. , vol.401 , pp. 186-204
    • Pearson, W.R.1
  • 35
    • 0037038087 scopus 로고    scopus 로고
    • Induction of cytosolic glutathione S-transferases from Atlantic eel (Anguilla Anguilla) after intraperitoneal treatment with polychlorinated biphenyls
    • Perez Lopez M., Novoa Valinas M.C., and Melgar Riol M.J. Induction of cytosolic glutathione S-transferases from Atlantic eel (Anguilla Anguilla) after intraperitoneal treatment with polychlorinated biphenyls. Sci. Total Environ. 297 (2002) 141-151
    • (2002) Sci. Total Environ. , vol.297 , pp. 141-151
    • Perez Lopez, M.1    Novoa Valinas, M.C.2    Melgar Riol, M.J.3
  • 36
    • 0028262418 scopus 로고
    • Colorimetric and fluorometric assays of glutathione transferase based on 7-chloro-4-nitrobenzo-2-oxa-1, 3-diazole
    • Ricci G., Caccuri A.M., Lo Bello M., Pastore A., Piemonte F., and Federici G. Colorimetric and fluorometric assays of glutathione transferase based on 7-chloro-4-nitrobenzo-2-oxa-1, 3-diazole. Anal. Biochem. 218 (1994) 463-465
    • (1994) Anal. Biochem. , vol.218 , pp. 463-465
    • Ricci, G.1    Caccuri, A.M.2    Lo Bello, M.3    Pastore, A.4    Piemonte, F.5    Federici, G.6
  • 39
    • 0027279421 scopus 로고
    • Messenger RNA degradation in eukaryotes
    • Sachs A.B. Messenger RNA degradation in eukaryotes. Cell 74 (1993) 413-421
    • (1993) Cell , vol.74 , pp. 413-421
    • Sachs, A.B.1
  • 40
    • 0035890484 scopus 로고    scopus 로고
    • Structure, function and evolution of glutathione transferases: 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 transferases: 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
  • 41
    • 0031847950 scopus 로고    scopus 로고
    • Evaluation of biomarkers in caged fishes and mussels to assess the quality of waters in a bay of the NW Mediterranean Sea
    • Stien X., Percic P., Gnassia-Barelli M., Romeo M., and Lafaurie M. Evaluation of biomarkers in caged fishes and mussels to assess the quality of waters in a bay of the NW Mediterranean Sea. Environ. Pollut. 99 (1998) 339-345
    • (1998) Environ. Pollut. , vol.99 , pp. 339-345
    • Stien, X.1    Percic, P.2    Gnassia-Barelli, M.3    Romeo, M.4    Lafaurie, M.5
  • 42
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications
    • Towbin H., Staehelin T., and Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl Acad. Sci. USA 76 (1979) 4350-4354
    • (1979) Proc. Natl Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 43
    • 0027382661 scopus 로고
    • Global fractionation and cold condensation of low volatility organochlorine compounds in polar regions
    • Wania F., and Mackay D. Global fractionation and cold condensation of low volatility organochlorine compounds in polar regions. Ambio 22 (1993) 10-18
    • (1993) Ambio , vol.22 , pp. 10-18
    • Wania, F.1    Mackay, D.2
  • 44
    • 0033990939 scopus 로고    scopus 로고
    • Evidence for and against the presence of polynuclear aromatic hydrocarbon and 2,3,7, 8-tetrachloro-p-dioxin binding proteins in the marine mussels, Bathymodiolus and Modiolus modiolus
    • Willett K., Wilson C., Thomsen J., and Porter W. Evidence for and against the presence of polynuclear aromatic hydrocarbon and 2,3,7, 8-tetrachloro-p-dioxin binding proteins in the marine mussels, Bathymodiolus and Modiolus modiolus. Aquat. Toxicol. 48 (2000) 51-64
    • (2000) Aquat. Toxicol. , vol.48 , pp. 51-64
    • Willett, K.1    Wilson, C.2    Thomsen, J.3    Porter, W.4
  • 45


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