메뉴 건너뛰기




Volumn 157, Issue 2, 2010, Pages 182-188

CDNA cloning and mRNA expression of a selenium-dependent glutathione peroxidase from Zhikong scallop Chlamys farreri

Author keywords

Chlamys farreri; Expression profile; Gene cloning; Selenium dependent glutathione peroxidase

Indexed keywords

COMPLEMENTARY DNA; GLUTATHIONE PEROXIDASE; GLUTATHIONE PEROXIDASE 3; MESSENGER RNA; SELENIUM; SELENOCYSTEINE; 3' UNTRANSLATED REGION;

EID: 77955096714     PISSN: 10964959     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbpb.2010.06.002     Document Type: Article
Times cited : (20)

References (50)
  • 1
    • 0034489653 scopus 로고    scopus 로고
    • The glutathione peroxidases
    • Arthur J.R. The glutathione peroxidases. Cell. Mol. Life Sci. 2000, 57:1825-1835.
    • (2000) Cell. Mol. Life Sci. , vol.57 , pp. 1825-1835
    • Arthur, J.R.1
  • 2
    • 0031227819 scopus 로고    scopus 로고
    • Glutathione peroxidase revisited-simulation of the catalytic cycle by computer-assisted molecular modelling
    • Aumann K.D., Bedorf N., Brigelius-Flohe R., Schomburg D., Flohe L. Glutathione peroxidase revisited-simulation of the catalytic cycle by computer-assisted molecular modelling. Biomed. Environ. Sci. 1997, 10:136-155.
    • (1997) Biomed. Environ. Sci. , vol.10 , pp. 136-155
    • Aumann, K.D.1    Bedorf, N.2    Brigelius-Flohe, R.3    Schomburg, D.4    Flohe, L.5
  • 4
    • 21244466809 scopus 로고    scopus 로고
    • Selenium-dependent glutathione peroxidases: a highlight of the role of phospholipids hydroperoxide glutathione peroxidase in protection against oxidative damage
    • Bao Y.P., Williamson G. Selenium-dependent glutathione peroxidases: a highlight of the role of phospholipids hydroperoxide glutathione peroxidase in protection against oxidative damage. Prog. Nat. Sci. 2000, 10:321-330.
    • (2000) Prog. Nat. Sci. , vol.10 , pp. 321-330
    • Bao, Y.P.1    Williamson, G.2
  • 5
    • 20444472794 scopus 로고    scopus 로고
    • Knowing when not to stop
    • Berry M.J. Knowing when not to stop. Nat. Struct. Mol. Biol. 2005, 12:389-390.
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , pp. 389-390
    • Berry, M.J.1
  • 6
    • 0025743489 scopus 로고
    • Recognition of UGA as a selenocysteine codon in type I deiodinase requires sequences in the 3' untranslated region
    • Berry M.J., Banu L., Chen Y.Y., Mandel S.J., Kieffer J.D., Harney J.W., Larsen P.R. Recognition of UGA as a selenocysteine codon in type I deiodinase requires sequences in the 3' untranslated region. Nature 1991, 353:273-276.
    • (1991) Nature , vol.353 , pp. 273-276
    • Berry, M.J.1    Banu, L.2    Chen, Y.Y.3    Mandel, S.J.4    Kieffer, J.D.5    Harney, J.W.6    Larsen, P.R.7
  • 7
    • 0025979337 scopus 로고
    • Type I iodothyronine deiodinase is a selenocysteine-containing enzyme
    • Berry M.J., Banu L., Larsen P.R. Type I iodothyronine deiodinase is a selenocysteine-containing enzyme. Nature 1991, 349:438-440.
    • (1991) Nature , vol.349 , pp. 438-440
    • Berry, M.J.1    Banu, L.2    Larsen, P.R.3
  • 8
    • 0027536023 scopus 로고
    • Expression, characterization, and tissue distribution of a new cellular selenium-dependent glutathione peroxidase, GSHPx-GI
    • Chu F.F., Doroshow J.H., Esworthy R.S. Expression, characterization, and tissue distribution of a new cellular selenium-dependent glutathione peroxidase, GSHPx-GI. J. Biol. Chem. 1993, 268:2571-2576.
    • (1993) J. Biol. Chem. , vol.268 , pp. 2571-2576
    • Chu, F.F.1    Doroshow, J.H.2    Esworthy, R.S.3
  • 9
    • 2942527312 scopus 로고    scopus 로고
    • Role of Se-dependent glutathione peroxidases in gastrointestinal inflammation and cancer
    • Chu F.F., Esworthy R.S., Doroshow J.H. Role of Se-dependent glutathione peroxidases in gastrointestinal inflammation and cancer. Free Radic. Biol. Med. 2004, 36:1481-1495.
    • (2004) Free Radic. Biol. Med. , vol.36 , pp. 1481-1495
    • Chu, F.F.1    Esworthy, R.S.2    Doroshow, J.H.3
  • 11
    • 27744455310 scopus 로고    scopus 로고
    • Molecular cloning of a phospholipid-hydroperoxide glutathione peroxidase gene from the tick, Boophilus microplus (Acari: Ixodidae)
    • Cossio-Bayugar R., Miranda E., Holman P.J. Molecular cloning of a phospholipid-hydroperoxide glutathione peroxidase gene from the tick, Boophilus microplus (Acari: Ixodidae). Insect Biochem. Mol. Biol. 2005, 35:1378-1387.
    • (2005) Insect Biochem. Mol. Biol. , vol.35 , pp. 1378-1387
    • Cossio-Bayugar, R.1    Miranda, E.2    Holman, P.J.3
  • 13
    • 33750159082 scopus 로고    scopus 로고
    • Identification, sequencing and expression of selenium-dependent glutathione peroxidase transcript in the freshwater bivalve Unio tumidus exposed to Aroclor 1254
    • Doyen P., Vasseur P., Rodius F. Identification, sequencing and expression of selenium-dependent glutathione peroxidase transcript in the freshwater bivalve Unio tumidus exposed to Aroclor 1254. Comp. Biochem. Physiol. C Toxicol. Pharmacol. 2006, 144:122-129.
    • (2006) Comp. Biochem. Physiol. C Toxicol. Pharmacol. , vol.144 , pp. 122-129
    • Doyen, P.1    Vasseur, P.2    Rodius, F.3
  • 14
    • 36749002700 scopus 로고    scopus 로고
    • 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
    • Doyen P., Bigot A., Vasseur P., Rodius F. 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. Comp. Biochem. Physiol. C Toxicol. Pharmacol. 2008, 147:69-77.
    • (2008) Comp. Biochem. Physiol. C Toxicol. Pharmacol. , vol.147 , pp. 69-77
    • Doyen, P.1    Bigot, A.2    Vasseur, P.3    Rodius, F.4
  • 15
    • 33646193400 scopus 로고    scopus 로고
    • The antioxidant glutathione peroxidase family and spermatozoa: a complex story
    • Drevet J.R. The antioxidant glutathione peroxidase family and spermatozoa: a complex story. Mol. Cell. Endocrinol. 2006, 250:70-79.
    • (2006) Mol. Cell. Endocrinol. , vol.250 , pp. 70-79
    • Drevet, J.R.1
  • 16
    • 22144442380 scopus 로고    scopus 로고
    • Structure, gene expression, and evolution of primate glutathione peroxidases
    • Fukuhara R., Kageyama T. Structure, gene expression, and evolution of primate glutathione peroxidases. Comp. Biochem. Physiol. B Biochem. Mol. Biol. 2005, 141:428-436.
    • (2005) Comp. Biochem. Physiol. B Biochem. Mol. Biol. , vol.141 , pp. 428-436
    • Fukuhara, R.1    Kageyama, T.2
  • 17
    • 0028935020 scopus 로고
    • Glutathione peroxidase and other antioxidant enzyme function in marine invertebrates (Mytilus edulis, Pecten maximus, Carcinus maenas and Asterias rubens)
    • Gamble S.C., Goldfarb P.S., Porte C., Livingstone D.R. Glutathione peroxidase and other antioxidant enzyme function in marine invertebrates (Mytilus edulis, Pecten maximus, Carcinus maenas and Asterias rubens). Mar. Environ. Res. 1995, 39:191-195.
    • (1995) Mar. Environ. Res. , vol.39 , pp. 191-195
    • Gamble, S.C.1    Goldfarb, P.S.2    Porte, C.3    Livingstone, D.R.4
  • 18
  • 19
    • 0026636441 scopus 로고
    • Free radicals, antioxidants, and human disease: where are we now?
    • Halliwell B., Gutteridge J.M., Cross C.E. Free radicals, antioxidants, and human disease: where are we now?. J. Lab. Clin. Med. 1992, 119:598-620.
    • (1992) J. Lab. Clin. Med. , vol.119 , pp. 598-620
    • Halliwell, B.1    Gutteridge, J.M.2    Cross, C.E.3
  • 20
    • 34247342559 scopus 로고    scopus 로고
    • Seleno-independent glutathione peroxidases. More than simple antioxidant scavengers
    • Herbette S., Roeckel-Drevet P., Drevet J.R. Seleno-independent glutathione peroxidases. More than simple antioxidant scavengers. FEBS J. 2007, 274:2163-2180.
    • (2007) FEBS J. , vol.274 , pp. 2163-2180
    • Herbette, S.1    Roeckel-Drevet, P.2    Drevet, J.R.3
  • 21
    • 25144503860 scopus 로고    scopus 로고
    • Selenoprotein synthesis: a unique translational mechanism used by a diverse family of proteins
    • Hoffmann P.R., Berry M.J. Selenoprotein synthesis: a unique translational mechanism used by a diverse family of proteins. Thyroid 2005, 15:769-775.
    • (2005) Thyroid , vol.15 , pp. 769-775
    • Hoffmann, P.R.1    Berry, M.J.2
  • 23
    • 0037438730 scopus 로고    scopus 로고
    • Biological significance of phospholipid hydroperoxide glutathione peroxidase (PHGPx, GPx4) in mammalian cells
    • Imai H., Nakagawa Y. Biological significance of phospholipid hydroperoxide glutathione peroxidase (PHGPx, GPx4) in mammalian cells. Free Radic. Biol. Med. 2003, 34:145-169.
    • (2003) Free Radic. Biol. Med. , vol.34 , pp. 145-169
    • Imai, H.1    Nakagawa, Y.2
  • 24
    • 33646884811 scopus 로고    scopus 로고
    • Plasma glutathione peroxidase by ELISA and relationship to selenium level
    • Jacobson G.A., Narkowicz C., Tong Y.C., Peterson G.M. Plasma glutathione peroxidase by ELISA and relationship to selenium level. Clin. Chim. Acta 2006, 369:100-103.
    • (2006) Clin. Chim. Acta , vol.369 , pp. 100-103
    • Jacobson, G.A.1    Narkowicz, C.2    Tong, Y.C.3    Peterson, G.M.4
  • 26
    • 45949109669 scopus 로고    scopus 로고
    • MEGA: a biologist-centric software for evolutionary analysis of DNA and protein sequences
    • Kumar S., Nei M., Dudley J., Tamura K. MEGA: a biologist-centric software for evolutionary analysis of DNA and protein sequences. Brief. Bioinform. 2008, 9:299-306.
    • (2008) Brief. Bioinform. , vol.9 , pp. 299-306
    • Kumar, S.1    Nei, M.2    Dudley, J.3    Tamura, K.4
  • 27
    • 4644293545 scopus 로고    scopus 로고
    • Biochemical properties of glutathione peroxidase in Gammarus pulex
    • Kutlu M., Susuz F. Biochemical properties of glutathione peroxidase in Gammarus pulex. Bull. Environ. Contam. Toxicol. 2004, 73:432-436.
    • (2004) Bull. Environ. Contam. Toxicol. , vol.73 , pp. 432-436
    • Kutlu, M.1    Susuz, F.2
  • 28
    • 0017067418 scopus 로고
    • Glutathione peroxidase activity in selenium-deficient rat liver
    • Lawrence R.A., Burk R.F. Glutathione peroxidase activity in selenium-deficient rat liver. Biochem. Biophys. Res. Commun. 1976, 71:952-958.
    • (1976) Biochem. Biophys. Res. Commun. , vol.71 , pp. 952-958
    • Lawrence, R.A.1    Burk, R.F.2
  • 29
    • 34247378650 scopus 로고    scopus 로고
    • Identification and cloning of the antioxidant enzyme, glutathione peroxidase, of white shrimp, Litopenaeus vannamei, and its expression following Vibrio alginolyticus infection
    • Liu C.H., Tseng M.C., Cheng W. Identification and cloning of the antioxidant enzyme, glutathione peroxidase, of white shrimp, Litopenaeus vannamei, and its expression following Vibrio alginolyticus infection. Fish Shellfish Immunol. 2007, 23:34-45.
    • (2007) Fish Shellfish Immunol. , vol.23 , pp. 34-45
    • Liu, C.H.1    Tseng, M.C.2    Cheng, W.3
  • 30
    • 0025787017 scopus 로고
    • Phospholipid hydroperoxide glutathione peroxidase is the 18-kDa selenoprotein expressed in human tumor cell lines
    • Maiorino M., Chu F.F., Ursini F., Davies K.J., Doroshow J.H., Esworthy R.S. Phospholipid hydroperoxide glutathione peroxidase is the 18-kDa selenoprotein expressed in human tumor cell lines. J. Biol. Chem. 1991, 266:7728-7732.
    • (1991) J. Biol. Chem. , vol.266 , pp. 7728-7732
    • Maiorino, M.1    Chu, F.F.2    Ursini, F.3    Davies, K.J.4    Doroshow, J.H.5    Esworthy, R.S.6
  • 31
    • 0034676493 scopus 로고    scopus 로고
    • Effects of antioxidant enzymes in the molecular control of reactive oxygen species toxicology
    • Matés J.M. Effects of antioxidant enzymes in the molecular control of reactive oxygen species toxicology. Toxicology 2000, 153:83-104.
    • (2000) Toxicology , vol.153 , pp. 83-104
    • Matés, J.M.1
  • 33
    • 0343963252 scopus 로고    scopus 로고
    • Chemical and biological activity of free radical 'scavengers' in allergic diseases
    • Matés J.M., Pérez-Gómez C., Blanca M. Chemical and biological activity of free radical 'scavengers' in allergic diseases. Clin. Chim. Acta 2000, 296:1-15.
    • (2000) Clin. Chim. Acta , vol.296 , pp. 1-15
    • Matés, J.M.1    Pérez-Gómez, C.2    Blanca, M.3
  • 34
    • 0007246923 scopus 로고
    • The lethal oxidase of leucocytes
    • Michell B. The lethal oxidase of leucocytes. Trends Biochem. Sci. 1983, 8:117-118.
    • (1983) Trends Biochem. Sci. , vol.8 , pp. 117-118
    • Michell, B.1
  • 35
    • 34447622276 scopus 로고    scopus 로고
    • Autophagic and lysosomal reactions to stress in the hepatopancreas of blue mussels
    • Moore M.N., Viarengo A., Donkin P., Hawkins A.J. Autophagic and lysosomal reactions to stress in the hepatopancreas of blue mussels. Aquat. Toxicol. 2007, 84:80-91.
    • (2007) Aquat. Toxicol. , vol.84 , pp. 80-91
    • Moore, M.N.1    Viarengo, A.2    Donkin, P.3    Hawkins, A.J.4
  • 36
    • 0037226793 scopus 로고    scopus 로고
    • 3' UTRs of glutathione peroxidases differentially affect selenium-dependent mRNA stability and selenocysteine incorporation efficiency
    • Muller C., Wingler K., Brigelius-Flohe R. 3' UTRs of glutathione peroxidases differentially affect selenium-dependent mRNA stability and selenocysteine incorporation efficiency. Biol. Chem. 2003, 384:11-18.
    • (2003) Biol. Chem. , vol.384 , pp. 11-18
    • Muller, C.1    Wingler, K.2    Brigelius-Flohe, R.3
  • 37
    • 0031584269 scopus 로고    scopus 로고
    • The crystal structure of seleno-glutathione peroxidase from human plasma at 2.9Å resolution
    • Ren B., Huang W., Akesson B., Ladenstein R. The crystal structure of seleno-glutathione peroxidase from human plasma at 2.9Å resolution. J. Mol. Biol. 1997, 268:869-885.
    • (1997) J. Mol. Biol. , vol.268 , pp. 869-885
    • Ren, B.1    Huang, W.2    Akesson, B.3    Ladenstein, R.4
  • 38
    • 0033106065 scopus 로고    scopus 로고
    • Defense mechanisms and disease prevention in farmed marine invertebrates
    • Roch P. Defense mechanisms and disease prevention in farmed marine invertebrates. Aquaculture 1999, 172:125-145.
    • (1999) Aquaculture , vol.172 , pp. 125-145
    • Roch, P.1
  • 39
    • 0029869567 scopus 로고    scopus 로고
    • Tissue localization and stage-specific expression of the phospholipid hydroperoxide glutathione peroxidase of Schistosoma mansoni
    • Roche C., Liu J.L., LePresle T., Capron A., Pierce R.J. Tissue localization and stage-specific expression of the phospholipid hydroperoxide glutathione peroxidase of Schistosoma mansoni. Mol. Biochem. Parasitol. 1996, 75:187-195.
    • (1996) Mol. Biochem. Parasitol. , vol.75 , pp. 187-195
    • Roche, C.1    Liu, J.L.2    LePresle, T.3    Capron, A.4    Pierce, R.J.5
  • 41
    • 0016810507 scopus 로고
    • Defective microbicidal activity in glutathione peroxidase-deficient neutrophils of selenium-deficient rats
    • Serfass R.E., Ganther H.E. Defective microbicidal activity in glutathione peroxidase-deficient neutrophils of selenium-deficient rats. Nature 1975, 255:640-641.
    • (1975) Nature , vol.255 , pp. 640-641
    • Serfass, R.E.1    Ganther, H.E.2
  • 42
    • 0025288409 scopus 로고
    • Selenium biochemistry
    • Stadtman T.C. Selenium biochemistry. Annu. Rev. Biochem. 1990, 59:111-127.
    • (1990) Annu. Rev. Biochem. , vol.59 , pp. 111-127
    • Stadtman, T.C.1
  • 44
    • 34547781750 scopus 로고    scopus 로고
    • MEGA4: Molecular Evolutionary Genetics Analysis (MEGA) software version 4.0
    • Tamura K., Dudley J., Nei M., Kumar S. MEGA4: Molecular Evolutionary Genetics Analysis (MEGA) software version 4.0. Mol. Biol. Evol. 2007, 24:1596-1599.
    • (2007) Mol. Biol. Evol. , vol.24 , pp. 1596-1599
    • Tamura, K.1    Dudley, J.2    Nei, M.3    Kumar, S.4
  • 45
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson J.D., Gibson T.J., Plewniak F., Jeanmougin F., Higgins D.G. The CLUSTAL X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res. 1997, 25:4876-4882.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 47
    • 0029805895 scopus 로고    scopus 로고
    • A novel RNA structural motif in the selenocysteine insertion element of eukaryotic selenoprotein mRNAs
    • Walczak R., Westhof E., Carbon P., Krol A. A novel RNA structural motif in the selenocysteine insertion element of eukaryotic selenoprotein mRNAs. RNA 1996, 2:367-379.
    • (1996) RNA , vol.2 , pp. 367-379
    • Walczak, R.1    Westhof, E.2    Carbon, P.3    Krol, A.4
  • 48
    • 0025883489 scopus 로고
    • Decreased stability of digestive gland lysosomes from the common mussel Mytilus edulis L. by in vitro generation of oxygen-free radicals
    • Winston G., Moore M., Straatsburg I., Kirchin M. Decreased stability of digestive gland lysosomes from the common mussel Mytilus edulis L. by in vitro generation of oxygen-free radicals. Arch. Environ. Contam. Toxicol. 1991, 21:401-408.
    • (1991) Arch. Environ. Contam. Toxicol. , vol.21 , pp. 401-408
    • Winston, G.1    Moore, M.2    Straatsburg, I.3    Kirchin, M.4
  • 49
    • 67650442054 scopus 로고    scopus 로고
    • Tolliod-like gene in Crassostrea ariakensis: molecular cloning, structural characterization and expression by RLO stimulation
    • Yang S., Wu X. Tolliod-like gene in Crassostrea ariakensis: molecular cloning, structural characterization and expression by RLO stimulation. Fish Shellfish Immunol. 2009, 27:130-135.
    • (2009) Fish Shellfish Immunol. , vol.27 , pp. 130-135
    • Yang, S.1    Wu, X.2
  • 50
    • 0012608077 scopus 로고    scopus 로고
    • Analysis of the causes of mass mortality of farming Chlamys farreri in summer in costal areas of Shandong
    • Zhang F., Yang H. Analysis of the causes of mass mortality of farming Chlamys farreri in summer in costal areas of Shandong. China Mar. Sci. 1999, 1:44-47.
    • (1999) China Mar. Sci. , vol.1 , pp. 44-47
    • Zhang, F.1    Yang, H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.