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Volumn 45, Issue 2, 2015, Pages 648-655

Two variants of selenium-dependent glutathione peroxidase from the disk abalone Haliotis discus discus: Molecular characterization and immune responses to bacterial and viral stresses

Author keywords

AbSeGPx a; AbSeGPx b; Haliotis discus discus; Immune response; Selenium dependent glutathione peroxidase (SeGPx)

Indexed keywords

ANIMALIA; BACTERIA (MICROORGANISMS); HALIOTIDAE; HALIOTIS DISCUS DISCUS; LISTERIA MONOCYTOGENES; VIBRIO PARAHAEMOLYTICUS; VIRAL HEMORRHAGIC SEPTICEMIA VIRUS;

EID: 84930640651     PISSN: 10504648     EISSN: 10959947     Source Type: Journal    
DOI: 10.1016/j.fsi.2015.05.028     Document Type: Article
Times cited : (16)

References (41)
  • 1
    • 17544404224 scopus 로고    scopus 로고
    • Reactive oxygen and reactive nitrogen intermediates in innate and specific immunity
    • Bogdan C., Rollinghoff M., Diefenbach A. Reactive oxygen and reactive nitrogen intermediates in innate and specific immunity. Curr. Opin. Immunol. 2000, 12:64-76.
    • (2000) Curr. Opin. Immunol. , vol.12 , pp. 64-76
    • Bogdan, C.1    Rollinghoff, M.2    Diefenbach, A.3
  • 2
    • 0033106065 scopus 로고    scopus 로고
    • Defense mechanisms and disease prevention in farmed marine invertebrates
    • Philippe R. Defense mechanisms and disease prevention in farmed marine invertebrates. Aquaculture 1999, 172:125-145.
    • (1999) Aquaculture , vol.172 , pp. 125-145
    • Philippe, R.1
  • 4
    • 0034676493 scopus 로고    scopus 로고
    • Effects of antioxidant enzymes in the molecular control of reactive oxygen species toxicology
    • Mates 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
    • Mates, J.M.1
  • 5
    • 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
  • 6
    • 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
  • 8
    • 0021803196 scopus 로고
    • The selenoenzyme phospholipid hydroperoxide glutathione peroxidase
    • Ursini F., Maiorino M., Gregolin C. The selenoenzyme phospholipid hydroperoxide glutathione peroxidase. Biochimica Biophysica Acta 1985, 839:62-70.
    • (1985) Biochimica Biophysica Acta , vol.839 , pp. 62-70
    • Ursini, F.1    Maiorino, M.2    Gregolin, C.3
  • 9
    • 79952699746 scopus 로고    scopus 로고
    • Aselenium-dependent glutathione peroxidase in the Japanese scallop, Mizuhopecten yessoensis: cDNA cloning, promoter sequence analysis and mRNA expression. Comparative biochemistry and physiology Part B
    • Shan Z., Li H., Bao X., He C., Yu H., Liu W., et al. Aselenium-dependent glutathione peroxidase in the Japanese scallop, Mizuhopecten yessoensis: cDNA cloning, promoter sequence analysis and mRNA expression. Comparative biochemistry and physiology Part B. Biochem. Mol. Biol. 2011, 159:1-9.
    • (2011) Biochem. Mol. Biol. , vol.159 , pp. 1-9
    • Shan, Z.1    Li, H.2    Bao, X.3    He, C.4    Yu, H.5    Liu, W.6
  • 10
    • 77955096714 scopus 로고    scopus 로고
    • CDNA cloning and mRNA expression of a selenium-dependent glutathione peroxidase from Zhikong scallop Chlamys farreri. Comparative biochemistry and physiology Part B
    • Mu C., Ni D., Zhao J., Wang L., Song L., Li L., et al. cDNA cloning and mRNA expression of a selenium-dependent glutathione peroxidase from Zhikong scallop Chlamys farreri. Comparative biochemistry and physiology Part B. Biochem. Mol. Biol. 2010, 157:182-188.
    • (2010) Biochem. Mol. Biol. , vol.157 , pp. 182-188
    • Mu, C.1    Ni, D.2    Zhao, J.3    Wang, L.4    Song, L.5    Li, L.6
  • 11
    • 81255157864 scopus 로고    scopus 로고
    • Transcriptional regulation of selenium-dependent glutathione peroxidase from Venerupis philippinarum in response to pathogen and contaminants challenge
    • Zhang L., Liu X., Chen L., You L., Pei D., Cong M., et al. Transcriptional regulation of selenium-dependent glutathione peroxidase from Venerupis philippinarum in response to pathogen and contaminants challenge. Fish Shellfish Immunol. 2011, 31:831-837.
    • (2011) Fish Shellfish Immunol. , vol.31 , pp. 831-837
    • Zhang, L.1    Liu, X.2    Chen, L.3    You, L.4    Pei, D.5    Cong, M.6
  • 12
    • 51449106300 scopus 로고    scopus 로고
    • Transcriptional up-regulation of disk abalone selenium dependent glutathione peroxidase by H(2)O(2) oxidative stress and Vibrio alginolyticus bacterial infection
    • De Zoysa M., Pushpamali W.A., Oh C., Whang I., Kim S.J., Lee J. Transcriptional up-regulation of disk abalone selenium dependent glutathione peroxidase by H(2)O(2) oxidative stress and Vibrio alginolyticus bacterial infection. Fish Shellfish Immunol. 2008, 25:446-457.
    • (2008) Fish Shellfish Immunol. , vol.25 , pp. 446-457
    • De Zoysa, M.1    Pushpamali, W.A.2    Oh, C.3    Whang, I.4    Kim, S.J.5    Lee, J.6
  • 13
    • 77953615386 scopus 로고    scopus 로고
    • The role of selenium-dependent glutathione peroxidase (Se-GPx) against oxidative and genotoxic effects of mercury in haemocytes of mussel Mytilus galloprovincialis (Lmk.)
    • Chatziargyriou V., Dailianis S. The role of selenium-dependent glutathione peroxidase (Se-GPx) against oxidative and genotoxic effects of mercury in haemocytes of mussel Mytilus galloprovincialis (Lmk.). Toxicol. InVitro Int. J. Publ. Assoc. BIBRA 2010, 24:1363-1372.
    • (2010) Toxicol. InVitro Int. J. Publ. Assoc. BIBRA , vol.24 , pp. 1363-1372
    • Chatziargyriou, V.1    Dailianis, S.2
  • 14
    • 33845673558 scopus 로고    scopus 로고
    • Stress and immune responses in abalone: limitations in current knowledge and investigative methods based on other models
    • Hooper C., Day R., Slocombe R., Handlinger J., Benkendorff K. Stress and immune responses in abalone: limitations in current knowledge and investigative methods based on other models. Fish Shellfish Immunol. 2007, 22:363-379.
    • (2007) Fish Shellfish Immunol. , vol.22 , pp. 363-379
    • Hooper, C.1    Day, R.2    Slocombe, R.3    Handlinger, J.4    Benkendorff, K.5
  • 15
    • 36849047751 scopus 로고    scopus 로고
    • Characterization and identification of virulent Klebsiella oxytoca isolated from abalone (Haliotis diversicolor supertexta) postlarvae with mass mortality in Fujian, China
    • Cai J., Wang Z., Cai C., Zhou Y. Characterization and identification of virulent Klebsiella oxytoca isolated from abalone (Haliotis diversicolor supertexta) postlarvae with mass mortality in Fujian, China. J.Invertebr. Pathol. 2008, 97:70-75.
    • (2008) J.Invertebr. Pathol. , vol.97 , pp. 70-75
    • Cai, J.1    Wang, Z.2    Cai, C.3    Zhou, Y.4
  • 16
    • 22044439259 scopus 로고    scopus 로고
    • Herpes-like virus infection causing mortality of cultured abalone Haliotis diversicolor supertexta in Taiwan
    • Chang P.H., Kuo S.T., Lai S.H., Yang H.S., Ting Y.Y., Hsu C.L., et al. Herpes-like virus infection causing mortality of cultured abalone Haliotis diversicolor supertexta in Taiwan. Dis. Aquatic Org. 2005, 65:23-27.
    • (2005) Dis. Aquatic Org. , vol.65 , pp. 23-27
    • Chang, P.H.1    Kuo, S.T.2    Lai, S.H.3    Yang, H.S.4    Ting, Y.Y.5    Hsu, C.L.6
  • 17
    • 84880630291 scopus 로고    scopus 로고
    • Abifunctional invertebrate-type lysozyme from the disk abalone, Haliotis discus discus: genome organization, transcriptional profiling and biological activities of recombinant protein
    • Bathige S.D., Umasuthan N., Kasthuri S.R., Whang I., Lim B.S., Nam B.H., et al. Abifunctional invertebrate-type lysozyme from the disk abalone, Haliotis discus discus: genome organization, transcriptional profiling and biological activities of recombinant protein. Dev. Comp. Immunol. 2013, 41:282-294.
    • (2013) Dev. Comp. Immunol. , vol.41 , pp. 282-294
    • Bathige, S.D.1    Umasuthan, N.2    Kasthuri, S.R.3    Whang, I.4    Lim, B.S.5    Nam, B.H.6
  • 18
    • 0347823003 scopus 로고    scopus 로고
    • MatGAT: an application that generates similarity/identity matrices using protein or DNA sequences
    • Campanella J.J., Bitincka L., Smalley J. MatGAT: an application that generates similarity/identity matrices using protein or DNA sequences. BMC Bioinforma. 2003, 4:29.
    • (2003) BMC Bioinforma. , vol.4 , pp. 29
    • Campanella, J.J.1    Bitincka, L.2    Smalley, J.3
  • 19
    • 64149097786 scopus 로고    scopus 로고
    • The MIQE guidelines: minimum information for publication of quantitative real-time PCR experiments
    • Bustin S.A., Benes V., Garson J.A., Hellemans J., Huggett J., Kubista M., et al. The MIQE guidelines: minimum information for publication of quantitative real-time PCR experiments. Clin. Chem. 2009, 55:611-622.
    • (2009) Clin. Chem. , vol.55 , pp. 611-622
    • Bustin, S.A.1    Benes, V.2    Garson, J.A.3    Hellemans, J.4    Huggett, J.5    Kubista, M.6
  • 20
    • 79951509964 scopus 로고    scopus 로고
    • Validation of housekeeping genes as internal controls for studying biomarkers of endocrine-disrupting chemicals in disk abalone by real-time PCR
    • Wan Q., Whang I., Choi C.Y., Lee J.S., Lee J. Validation of housekeeping genes as internal controls for studying biomarkers of endocrine-disrupting chemicals in disk abalone by real-time PCR. Comp. Biochem. Physiol. Toxicol. Pharmacol. CBP 2011, 153:259-268.
    • (2011) Comp. Biochem. Physiol. Toxicol. Pharmacol. CBP , vol.153 , pp. 259-268
    • Wan, Q.1    Whang, I.2    Choi, C.Y.3    Lee, J.S.4    Lee, J.5
  • 21
    • 0035710746 scopus 로고    scopus 로고
    • Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) Method
    • Livak K.J., Schmittgen T.D. Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) Method. Methods 2001, 25:402-408.
    • (2001) Methods , vol.25 , pp. 402-408
    • Livak, K.J.1    Schmittgen, T.D.2
  • 22
    • 33750989874 scopus 로고    scopus 로고
    • Selenoprotein synthesis: UGA does not end the story
    • Allmang C., Krol A. Selenoprotein synthesis: UGA does not end the story. Biochimie 2006, 88:1561-1571.
    • (2006) Biochimie , vol.88 , pp. 1561-1571
    • Allmang, C.1    Krol, A.2
  • 23
    • 0029805895 scopus 로고    scopus 로고
    • Anovel RNA structural motif in the selenocysteine insertion element of eukaryotic selenoprotein mRNAs
    • Walczak R., Westhof E., Carbon P., Krol A. Anovel 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
  • 24
    • 0032943632 scopus 로고    scopus 로고
    • Two distinct SECIS structures capable of directing selenocysteine incorporation in eukaryotes
    • Grundner-Culemann E., Martin G.W., Harney J.W., Berry M.J. Two distinct SECIS structures capable of directing selenocysteine incorporation in eukaryotes. Rna 1999, 5:625-635.
    • (1999) Rna , vol.5 , pp. 625-635
    • Grundner-Culemann, E.1    Martin, G.W.2    Harney, J.W.3    Berry, M.J.4
  • 25
    • 77954084614 scopus 로고    scopus 로고
    • Identification and cloning of a selenium-dependent glutathione peroxidase from tiger shrimp, Penaeus monodon, and its transcription following pathogen infection and related to the molt stages
    • Liu K.F., Yeh M.S., Kou G.H., Cheng W., Lo C.F. Identification and cloning of a selenium-dependent glutathione peroxidase from tiger shrimp, Penaeus monodon, and its transcription following pathogen infection and related to the molt stages. Dev. Comp. Immunol. 2010, 34:935-944.
    • (2010) Dev. Comp. Immunol. , vol.34 , pp. 935-944
    • Liu, K.F.1    Yeh, M.S.2    Kou, G.H.3    Cheng, W.4    Lo, C.F.5
  • 26
    • 79956050674 scopus 로고    scopus 로고
    • Molecular characterization of a glutathione peroxidase gene and its expression in the selected Vibrio-resistant population of the clam Meretrix meretrix
    • Wang C., Huan P., Yue X., Yan M., Liu B. Molecular characterization of a glutathione peroxidase gene and its expression in the selected Vibrio-resistant population of the clam Meretrix meretrix. Fish Shellfish Immunol. 2011, 30:1294-1302.
    • (2011) Fish Shellfish Immunol. , vol.30 , pp. 1294-1302
    • Wang, C.1    Huan, P.2    Yue, X.3    Yan, M.4    Liu, B.5
  • 27
    • 84864393395 scopus 로고    scopus 로고
    • Selenium-dependent glutathione peroxidase gene expression during gonad development and its response to LPS and H(2)O(2) challenge in Scylla paramamosain
    • Fu M., Zou Z., Liu S., Lin P., Wang Y., Zhang Z. Selenium-dependent glutathione peroxidase gene expression during gonad development and its response to LPS and H(2)O(2) challenge in Scylla paramamosain. Fish Shellfish Immunol. 2012, 33:532-542.
    • (2012) Fish Shellfish Immunol. , vol.33 , pp. 532-542
    • Fu, M.1    Zou, Z.2    Liu, S.3    Lin, P.4    Wang, Y.5    Zhang, Z.6
  • 28
    • 0031584269 scopus 로고    scopus 로고
    • The crystal structure of seleno-glutathione peroxidase from human plasma at 2.9 A resolution
    • Ren B., Huang W., Akesson B., Ladenstein R. The crystal structure of seleno-glutathione peroxidase from human plasma at 2.9 A 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
  • 29
    • 0020775636 scopus 로고
    • The refined structure of the selenoenzyme glutathione peroxidase at 0.2-nm resolution
    • Epp O., Ladenstein R., Wendel A. The refined structure of the selenoenzyme glutathione peroxidase at 0.2-nm resolution. Eur. J. Biochem./FEBS 1983, 133:51-69.
    • (1983) Eur. J. Biochem./FEBS , vol.133 , pp. 51-69
    • Epp, O.1    Ladenstein, R.2    Wendel, A.3
  • 30
    • 77952742753 scopus 로고    scopus 로고
    • Molecular cloning, characterization and mRNA expression of selenium-dependent glutathione peroxidase from abalone Haliotis discus hannai Ino in response to dietary selenium, zinc and iron
    • Wu C., Mai K., Zhang W., Ai Q., Xu W., Wang X., et al. Molecular cloning, characterization and mRNA expression of selenium-dependent glutathione peroxidase from abalone Haliotis discus hannai Ino in response to dietary selenium, zinc and iron. Comp. Biochem. Physiol. Toxicol. Pharmacol. CBP 2010, 152:121-132.
    • (2010) Comp. Biochem. Physiol. Toxicol. Pharmacol. CBP , vol.152 , pp. 121-132
    • Wu, C.1    Mai, K.2    Zhang, W.3    Ai, Q.4    Xu, W.5    Wang, X.6
  • 31
    • 84855312778 scopus 로고    scopus 로고
    • The Roles of Glutathione Peroxidases during Embryo Development
    • Ufer C., Wang C.C. The Roles of Glutathione Peroxidases during Embryo Development. Front. Mol. Neurosci. 2011, 4:12.
    • (2011) Front. Mol. Neurosci. , vol.4 , pp. 12
    • Ufer, C.1    Wang, C.C.2
  • 32
    • 33745822021 scopus 로고    scopus 로고
    • The role of phospholipid hydroperoxide glutathione peroxidase isoforms in murine embryogenesis
    • Borchert A., Wang C.C., Ufer C., Schiebel H., Savaskan N.E., Kuhn H. The role of phospholipid hydroperoxide glutathione peroxidase isoforms in murine embryogenesis. J.Biol. Chem. 2006, 281:19655-19664.
    • (2006) J.Biol. Chem. , vol.281 , pp. 19655-19664
    • Borchert, A.1    Wang, C.C.2    Ufer, C.3    Schiebel, H.4    Savaskan, N.E.5    Kuhn, H.6
  • 33
    • 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. Toxicol. Pharmacol. CBP 2006, 144:122-129.
    • (2006) Comp. Biochem. physiol. Toxicol. Pharmacol. CBP , vol.144 , pp. 122-129
    • Doyen, P.1    Vasseur, P.2    Rodius, F.3
  • 34
    • 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
  • 35
    • 84882867299 scopus 로고    scopus 로고
    • Expression profiles of selenium dependent glutathione peroxidase and glutathione S-transferase from Exopalaemon carinicauda in response to Vibrio anguillarum and WSSV challenge
    • Duan Y., Liu P., Li J., Li J., Chen P. Expression profiles of selenium dependent glutathione peroxidase and glutathione S-transferase from Exopalaemon carinicauda in response to Vibrio anguillarum and WSSV challenge. Fish Shellfish Immunol. 2013, 35:661-670.
    • (2013) Fish Shellfish Immunol. , vol.35 , pp. 661-670
    • Duan, Y.1    Liu, P.2    Li, J.3    Li, J.4    Chen, P.5
  • 36
    • 0028824075 scopus 로고
    • Anovel membrane glycoprotein involved in ascidian hemocyte aggregation and phagocytosis
    • Takahashi H., Azumi K., Yokosawa H. Anovel membrane glycoprotein involved in ascidian hemocyte aggregation and phagocytosis. Eur. J. Biochem./FEBS 1995, 233:778-783.
    • (1995) Eur. J. Biochem./FEBS , vol.233 , pp. 778-783
    • Takahashi, H.1    Azumi, K.2    Yokosawa, H.3
  • 37
    • 20444506858 scopus 로고    scopus 로고
    • Recent advances in the innate immunity of invertebrate animals
    • Iwanaga S., Lee B.L. Recent advances in the innate immunity of invertebrate animals. J.Biochem. Mol. Biol. 2005, 38:128-150.
    • (2005) J.Biochem. Mol. Biol. , vol.38 , pp. 128-150
    • Iwanaga, S.1    Lee, B.L.2
  • 38
    • 84993865842 scopus 로고
    • Functional and structural characterization of hemocytes of the solitary ascidian, Halocynthia roretzi
    • Azumi K., Satoh N., Yokosawa H. Functional and structural characterization of hemocytes of the solitary ascidian, Halocynthia roretzi. J.Exp. Zool. 1993, 265:309-316.
    • (1993) J.Exp. Zool. , vol.265 , pp. 309-316
    • Azumi, K.1    Satoh, N.2    Yokosawa, H.3
  • 39
    • 0035906330 scopus 로고    scopus 로고
    • The protective role of selenium on genetic damage and on cancer
    • El-Bayoumy K. The protective role of selenium on genetic damage and on cancer. Mutat. Res. 2001, 475:123-139.
    • (2001) Mutat. Res. , vol.475 , pp. 123-139
    • El-Bayoumy, K.1
  • 40
    • 0022260431 scopus 로고
    • Relationships between invitro selenium supply, glutathione peroxidase activity, and phagocytic function in the HL-60 human myeloid cell line
    • Speier C., Baker S.S., Newburger P.E. Relationships between invitro selenium supply, glutathione peroxidase activity, and phagocytic function in the HL-60 human myeloid cell line. J.Biol. Chem. 1985, 260:8951-8955.
    • (1985) J.Biol. Chem. , vol.260 , pp. 8951-8955
    • Speier, C.1    Baker, S.S.2    Newburger, P.E.3
  • 41
    • 0030835589 scopus 로고    scopus 로고
    • Trace minerals in fish nutrition
    • Watanabe T., Kiron V., Satoh S. Trace minerals in fish nutrition. Aquaculture 1997, 151:185-207.
    • (1997) Aquaculture , vol.151 , pp. 185-207
    • Watanabe, T.1    Kiron, V.2    Satoh, S.3


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