메뉴 건너뛰기




Volumn 147, Issue 1, 2008, Pages 69-77

Molecular cloning and expression study of pi-class glutathione S-transferase (pi-GST) and selenium-dependent glutathione peroxidase (Se-GPx) transcripts in the freshwater bivalve Dreissena polymorpha

Author keywords

Bivalvia mollusc; Coding sequences; Dreissena polymorpha; Expression pattern; Pi class GST; Selenium dependent GPx

Indexed keywords

AMINO ACID; GLUTATHIONE PEROXIDASE; GLUTATHIONE TRANSFERASE P1; PRIMER DNA; SELENIUM DEPENDENT GLUTATHIONE PEROXIDASE; UNCLASSIFIED DRUG;

EID: 36749002700     PISSN: 15320456     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbpc.2007.08.002     Document Type: Article
Times cited : (60)

References (42)
  • 1
    • 0031733938 scopus 로고    scopus 로고
    • Liver glutathione content and glutathione-dependent enzymes of two species of freshwater fish as bioindicators of chemical pollution
    • Almar M., Otero L., Santos C., and Gallego J.G. Liver glutathione content and glutathione-dependent enzymes of two species of freshwater fish as bioindicators of chemical pollution. J. Environ. Sci. Health 33 (1998) 769-783
    • (1998) J. Environ. Sci. Health , vol.33 , pp. 769-783
    • Almar, M.1    Otero, L.2    Santos, C.3    Gallego, J.G.4
  • 5
    • 0031021397 scopus 로고    scopus 로고
    • Structure, catalytic mechanism, and evolution of the glutathione transferases
    • Armstrong R.N. Structure, catalytic mechanism, and evolution of the glutathione transferases. Chem. Res. Toxicol. 10 (1997) 2-18
    • (1997) Chem. Res. Toxicol. , vol.10 , pp. 2-18
    • Armstrong, R.N.1
  • 6
    • 0031227819 scopus 로고    scopus 로고
    • Glutathione peroxidase revisited-simulation of the catalytic cycle by computer-assisted molecular modelling
    • Aumann K.D., Bedorf N., Brigelius-Flohé R., Schomburg D., and Flohé L. Glutathione peroxidase revisited-simulation of the catalytic cycle by computer-assisted molecular modelling. Biomed. Environ. Sci. 10 (1997) 136-155
    • (1997) Biomed. Environ. Sci. , vol.10 , pp. 136-155
    • Aumann, K.D.1    Bedorf, N.2    Brigelius-Flohé, R.3    Schomburg, D.4    Flohé, L.5
  • 7
    • 0023891262 scopus 로고
    • Elevation of glutathione S-transferase activity as a stress response to organochlorine compounds, in the freshwater mussel, Sphaerium corneum
    • Boryslawsky M., Garrood A.C., and Pearson J.T. Elevation of glutathione S-transferase activity as a stress response to organochlorine compounds, in the freshwater mussel, Sphaerium corneum. Mar. Environ. Res. 24 (1988) 101-104
    • (1988) Mar. Environ. Res. , vol.24 , pp. 101-104
    • Boryslawsky, M.1    Garrood, A.C.2    Pearson, J.T.3
  • 8
    • 0022730806 scopus 로고
    • The structure of the mouse glutathione peroxidase gene: the selenocysteine in the active site is encoded by the 'termination' codon TGA
    • Chambers I., Frampton J., Goldfarb P., Affara N., McBain W., and Harrison P. The structure of the mouse glutathione peroxidase gene: the selenocysteine in the active site is encoded by the 'termination' codon TGA. EMBO J. 5 (1986) 1221-1227
    • (1986) EMBO J. , vol.5 , pp. 1221-1227
    • Chambers, I.1    Frampton, J.2    Goldfarb, P.3    Affara, N.4    McBain, W.5    Harrison, P.6
  • 9
    • 2942744630 scopus 로고    scopus 로고
    • A comparative study of the expression of CYP1A and CYP4 genes in aquatic invertebrate (freshwater mussel, Unio tumidus) and vertebrate (rainbow trout, Oncorhynchus mykiss)
    • Chaty S., Rodius F., and Vasseur P. A comparative study of the expression of CYP1A and CYP4 genes in aquatic invertebrate (freshwater mussel, Unio tumidus) and vertebrate (rainbow trout, Oncorhynchus mykiss). Aquat. Toxicol. 69 (2004) 81-93
    • (2004) Aquat. Toxicol. , vol.69 , pp. 81-93
    • Chaty, S.1    Rodius, F.2    Vasseur, P.3
  • 10
    • 0024297354 scopus 로고
    • Multiple sequence alignment with hierarchical clustering
    • Corpet F. Multiple sequence alignment with hierarchical clustering. Nucleic Acids Res. 16 (1988) 10881-10890
    • (1988) Nucleic Acids Res. , vol.16 , pp. 10881-10890
    • Corpet, F.1
  • 11
    • 0031280403 scopus 로고    scopus 로고
    • Glutathione reductase, selenium-dependent glutathione peroxidase, glutathione levels, and lipid peroxidation in freshwater bivalves, Unio tumidus, as biomarkers of aquatic contamination in field studies
    • Cossu C., Doyotte A., Jacquin M.C., Babut M., Exinger A., and Vasseur P. Glutathione reductase, selenium-dependent glutathione peroxidase, glutathione levels, and lipid peroxidation in freshwater bivalves, Unio tumidus, as biomarkers of aquatic contamination in field studies. Ecotoxicol. Environ. Saf. 38 (1997) 122-131
    • (1997) Ecotoxicol. Environ. Saf. , vol.38 , pp. 122-131
    • Cossu, C.1    Doyotte, A.2    Jacquin, M.C.3    Babut, M.4    Exinger, A.5    Vasseur, P.6
  • 12
    • 27744584950 scopus 로고    scopus 로고
    • Field validation of antioxidant enzyme biomarkers in mussels (Perna viridis) and clams (Ruditapes philippinarum) transplanted in Hong Kong coastal waters
    • De Luca-Abbott S.B., Richardson B.J., McClellan K.E., Zheng G.J., Martin M., and Lam P.K. Field validation of antioxidant enzyme biomarkers in mussels (Perna viridis) and clams (Ruditapes philippinarum) transplanted in Hong Kong coastal waters. Mar. Pollut. Bull. 51 (2005) 694-707
    • (2005) Mar. Pollut. Bull. , vol.51 , pp. 694-707
    • De Luca-Abbott, S.B.1    Richardson, B.J.2    McClellan, K.E.3    Zheng, G.J.4    Martin, M.5    Lam, P.K.6
  • 13
    • 8644245285 scopus 로고    scopus 로고
    • Cytochemical and histochemical aspects of the digestive gland of the mussel Mytilus galloprovincialis (L.) in relation to function
    • Dimitriadis V.K., Domouhstidou G.P., and Cajaraville M.P. Cytochemical and histochemical aspects of the digestive gland of the mussel Mytilus galloprovincialis (L.) in relation to function. J. Mol. Histol. 35 (2004) 501-509
    • (2004) J. Mol. Histol. , vol.35 , pp. 501-509
    • Dimitriadis, V.K.1    Domouhstidou, G.P.2    Cajaraville, M.P.3
  • 14
    • 0028224013 scopus 로고
    • X-ray structures of cytosolic glutathione S-transferases, implications for protein architecture, substrate recognition and catalytic function
    • Dirr H., Reinemer P., and Huber R. X-ray 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
  • 15
    • 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
  • 16
    • 33750159082 scopus 로고    scopus 로고
    • Identification, sequencing and expression of the selenium-dependent glutathione peroxidase transcript in the freshwater bivalve Unio tumidus exposed to Aroclor 1254
    • Doyen P., Vasseur P., and Rodius F. Identification, sequencing and expression of the selenium-dependent glutathione peroxidase transcript in the freshwater bivalve Unio tumidus exposed to Aroclor 1254. Comp. Biochem. Physiol. C Toxicol. Pharmacol. 144 (2006) 122-129
    • (2006) Comp. Biochem. Physiol. C Toxicol. Pharmacol. , vol.144 , pp. 122-129
    • Doyen, P.1    Vasseur, P.2    Rodius, F.3
  • 17
    • 0015880169 scopus 로고
    • Glutathione peroxidase: a selenoenzyme
    • Flohé L., Gunzler W.A., and Schock H.H. Glutathione peroxidase: a selenoenzyme. FEBS lett. 32 (1973) 132-134
    • (1973) FEBS lett. , vol.32 , pp. 132-134
    • Flohé, L.1    Gunzler, W.A.2    Schock, H.H.3
  • 18
    • 0017889205 scopus 로고
    • Identification of the catalytic site of rat liver glutathione peroxidase as selenocysteine
    • Forstrom J.W., Zakowski J.J., and Tappel A.L. Identification of the catalytic site of rat liver glutathione peroxidase as selenocysteine. Biochemistry 17 (1978) 2639-2644
    • (1978) Biochemistry , vol.17 , pp. 2639-2644
    • Forstrom, J.W.1    Zakowski, J.J.2    Tappel, A.L.3
  • 20
    • 33847625456 scopus 로고    scopus 로고
    • Towards a validation of a cellular biomarker suite in native and transplanted zebra mussels: a 2-year integrative field study of seasonal and pollution-induced variations
    • Guerlet E., Ledy K., Meyer A., and Giamberini L. Towards a validation of a cellular biomarker suite in native and transplanted zebra mussels: a 2-year integrative field study of seasonal and pollution-induced variations. Aquat. Toxicol. 8 (2007) 377-388
    • (2007) Aquat. Toxicol. , vol.8 , pp. 377-388
    • Guerlet, E.1    Ledy, K.2    Meyer, A.3    Giamberini, L.4
  • 21
    • 0016275313 scopus 로고
    • Glutathione S-transferases the first enzymatic step in mercapturic acid formation
    • Habig W., 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.1    Pabst, M.J.2    Jakoby, W.B.3
  • 22
    • 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., Roméo 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 143 (2006) 196-203
    • (2006) Comp. Biochem. Physiol. C , vol.143 , pp. 196-203
    • Hoarau, P.1    Damiens, G.2    Roméo, M.3    Gnassia-Barelli, M.4    Bebianno, M.J.5
  • 23
    • 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 π 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 π 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
  • 25
    • 0022885217 scopus 로고
    • Glutathione peroxidase on approval
    • Bannister J., and Michelson A. (Eds)
    • Ladenstein R., Epp O., Gunzler W.A., and Flohé L. Glutathione peroxidase on approval. In: Bannister J., and Michelson A. (Eds). Life Chemistry Reports vol. 14 (1986) 37-55
    • (1986) Life Chemistry Reports , vol.14 , pp. 37-55
    • Ladenstein, R.1    Epp, O.2    Gunzler, W.A.3    Flohé, L.4
  • 26
    • 0026705291 scopus 로고
    • Contribution of tyrosine 6 to the catalytic mechanism of isoenzymes 3-3 of glutathione S-transferase
    • Liu S., Zhang P., Ji X., Johnson W.W., Gilliland G.L., and Armstrong R. Contribution of tyrosine 6 to the catalytic mechanism of isoenzymes 3-3 of glutathione S-transferase. J. Biol. Chem. 267 (1992) 4296-4299
    • (1992) J. Biol. Chem. , vol.267 , pp. 4296-4299
    • Liu, S.1    Zhang, P.2    Ji, X.3    Johnson, W.W.4    Gilliland, G.L.5    Armstrong, R.6
  • 27
    • 0027325607 scopus 로고
    • Peculiar spectroscopic and kinetic properties of Cys-47 in human placenta glutathione transferase, evidence for an atypical thiolate ion pair near the active site
    • Lo Bello M., Parker M.W., Desideri A., Polticelli F., Falconi M., Del Boccio G., Pennelli A., Federici G., and Ricci G. Peculiar spectroscopic and kinetic properties of Cys-47 in human placenta glutathione transferase, evidence for an atypical thiolate ion pair near the active site. J. Biol. Chem. 268 (1993) 19033-19038
    • (1993) J. Biol. Chem. , vol.268 , pp. 19033-19038
    • Lo Bello, M.1    Parker, M.W.2    Desideri, A.3    Polticelli, F.4    Falconi, M.5    Del Boccio, G.6    Pennelli, A.7    Federici, G.8    Ricci, G.9
  • 28
    • 0030923311 scopus 로고    scopus 로고
    • Multifunctional role of Tyr 108 in the catalytic mechanism of human glutathione transferase P1-1, crystallographic and kinetic studies on the Y108F mutant enzyme
    • Lo Bello M., Oakley A.J., Battistoni A., Mazzetti A.P., Nuccetelli M., Mazzarese G., Rossjohn J., Parker M.W., and Ricci G. Multifunctional role of Tyr 108 in the catalytic mechanism of human glutathione transferase P1-1, crystallographic and kinetic studies on the Y108F mutant enzyme. Biochemistry 36 (1997) 6207-6217
    • (1997) Biochemistry , vol.36 , pp. 6207-6217
    • Lo Bello, M.1    Oakley, A.J.2    Battistoni, A.3    Mazzetti, A.P.4    Nuccetelli, M.5    Mazzarese, G.6    Rossjohn, J.7    Parker, M.W.8    Ricci, G.9
  • 29
    • 70449174079 scopus 로고
    • Hemoglobin catabolism. I. Glutathione peroxidase, an erythrocyte enzyme which protects hemoglobin from oxidative breakdown
    • Mills G.C. Hemoglobin catabolism. I. Glutathione peroxidase, an erythrocyte enzyme which protects hemoglobin from oxidative breakdown. J. Biol. Chem. 229 (1957) 189-197
    • (1957) J. Biol. Chem. , vol.229 , pp. 189-197
    • Mills, G.C.1
  • 30
    • 33846572885 scopus 로고    scopus 로고
    • Differential responses of biomarkers in tissues of a freshwater mussel, Dreissena polymorpha, to the exposure of sediment extracts with different levels of contamination
    • Osman A.M., van den Heuvel H., and van Noort P.C. Differential responses of biomarkers in tissues of a freshwater mussel, Dreissena polymorpha, to the exposure of sediment extracts with different levels of contamination. J. Appl. Toxicol. 27 (2007) 51-59
    • (2007) J. Appl. Toxicol. , vol.27 , pp. 51-59
    • Osman, A.M.1    van den Heuvel, H.2    van Noort, P.C.3
  • 31
    • 0037073278 scopus 로고    scopus 로고
    • Comparative study of the xenobiotic metabolising system in the digestive gland of the bivalve molluscs in different aquatic ecosystems and in aquaria experiments
    • Petushok N., Gabryelak T., Palecz D., Zavodnik L., Varga I.S., and Deer K.A. Comparative study of the xenobiotic metabolising system in the digestive gland of the bivalve molluscs in different aquatic ecosystems and in aquaria experiments. Aquat. Toxicol. 61 (2002) 65-72
    • (2002) Aquat. Toxicol. , vol.61 , pp. 65-72
    • Petushok, N.1    Gabryelak, T.2    Palecz, D.3    Zavodnik, L.4    Varga, I.S.5    Deer, K.A.6
  • 32
    • 0026722795 scopus 로고
    • Three-dimensional structure of class pi glutathione S-transferase from human placenta in complex with S-hexylglutathione at 2.8 A resolution
    • Reinemer P., Dirr H.W., Ladenstein R., Huber R., Lo Bello M., Federici G., and Parker M.W. Three-dimensional structure of class pi glutathione S-transferase from human placenta in complex with S-hexylglutathione at 2.8 A resolution. J. Mol. Biol. 227 (1992) 214-226
    • (1992) J. Mol. Biol. , vol.227 , pp. 214-226
    • Reinemer, P.1    Dirr, H.W.2    Ladenstein, R.3    Huber, R.4    Lo Bello, M.5    Federici, G.6    Parker, M.W.7
  • 33
    • 0028809193 scopus 로고
    • Site-directed mutagenesis of human glutathione transferase P1-1, mutation of cys-47 induces a positive cooperatively in glutathione transferase P1-1
    • Ricci G., Lo Bello M., Caccuri A.M., Pastore A., Nuccetelli M., Parker M.W., and Federici G. Site-directed mutagenesis of human glutathione transferase P1-1, mutation of cys-47 induces a positive cooperatively in glutathione transferase P1-1. J. Biol. Chem. 270 (1995) 1243-1248
    • (1995) J. Biol. Chem. , vol.270 , pp. 1243-1248
    • Ricci, G.1    Lo Bello, M.2    Caccuri, A.M.3    Pastore, A.4    Nuccetelli, M.5    Parker, M.W.6    Federici, G.7
  • 34
    • 0037674821 scopus 로고    scopus 로고
    • The role of abiotic factors and pesticide levels on enzymatic activity in the freshwater mussel Anodonta cygnea at three different exposure sites
    • Robillard S., Beauchamp G., and Laulier M. The role of abiotic factors and pesticide levels on enzymatic activity in the freshwater mussel Anodonta cygnea at three different exposure sites. Comp. Biochem. Physiol. C Toxicol. Pharmacol. 135 (2003) 49-59
    • (2003) Comp. Biochem. Physiol. C Toxicol. Pharmacol. , vol.135 , pp. 49-59
    • Robillard, S.1    Beauchamp, G.2    Laulier, M.3
  • 37
    • 0035890484 scopus 로고    scopus 로고
    • Structure, function and evolution of glutathione S-transferases: implications for classification of non-mammalian members of an ancient enzyme superfamily
    • Sheehan D., Meade G., Foley V.M., and Dowd C. Structure, function and evolution of glutathione S-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.4
  • 38
    • 0018848050 scopus 로고
    • Selenium-dependent enzymes
    • Stadtman T.C. Selenium-dependent enzymes. Annu. Rev. Biochem. 49 (1980) 93-110
    • (1980) Annu. Rev. Biochem. , vol.49 , pp. 93-110
    • Stadtman, T.C.1
  • 40
    • 0034728774 scopus 로고    scopus 로고
    • Tyrosine 50 at the subunit interface of dimeric human glutathione transferase P1-1 is a structural key residue for modulating protein stability and catalytic function
    • Stenberg G., Abdalla A.M., and Mannervik B. Tyrosine 50 at the subunit interface of dimeric human glutathione transferase P1-1 is a structural key residue for modulating protein stability and catalytic function. Biochem. Biophys. Res. Commun. 271 (2000) 59-63
    • (2000) Biochem. Biophys. Res. Commun. , vol.271 , pp. 59-63
    • Stenberg, G.1    Abdalla, A.M.2    Mannervik, B.3
  • 41
    • 34047186351 scopus 로고    scopus 로고
    • Biochemical markers of oxidative stress in Perna viridis exposed to mercury and temperature
    • Verlecar X.N., Jena K.B., and Chainy G.B. Biochemical markers of oxidative stress in Perna viridis exposed to mercury and temperature. Chem. Biol. Interact. 167 (2007) 219-226
    • (2007) Chem. Biol. Interact. , vol.167 , pp. 219-226
    • Verlecar, X.N.1    Jena, K.B.2    Chainy, G.B.3
  • 42
    • 0035126550 scopus 로고    scopus 로고
    • Potential biomarkers of trichloroethylene and toluene exposure in Corbicula fluminea
    • Vidal M.-L., Basseres A., and Narbonne J.-F. Potential biomarkers of trichloroethylene and toluene exposure in Corbicula fluminea. Environ. Toxicol. Pharmacol. 9 (2001) 87-97
    • (2001) Environ. Toxicol. Pharmacol. , vol.9 , pp. 87-97
    • Vidal, M.-L.1    Basseres, A.2    Narbonne, J.-F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.