메뉴 건너뛰기




Volumn 24, Issue 1, 2008, Pages 26-34

Molecular cloning and characterization of a catalase gene from Zhikong scallop Chlamys farreri

Author keywords

Catalase; Chlamys farreri; Gene cloning; Quantitative real time PCR

Indexed keywords

ANIMALIA; BACTERIA (MICROORGANISMS); CHLAMYS FARRERI; NEGIBACTERIA; RATTUS; VIBRIO;

EID: 38349165108     PISSN: 10504648     EISSN: 10959947     Source Type: Journal    
DOI: 10.1016/j.fsi.2007.06.010     Document Type: Article
Times cited : (76)

References (42)
  • 1
    • 34248196575 scopus 로고    scopus 로고
    • Immune responses and gene expression in white shrimp, Litopenaeus vannamei, induced by Lactobacillus plantarum
    • Chiu C.H., Guu Y.K., Liu C.H., Pan T.M., and Cheng W. Immune responses and gene expression in white shrimp, Litopenaeus vannamei, induced by Lactobacillus plantarum. Fish Shellfish Immunol 23 (2007) 364-377
    • (2007) Fish Shellfish Immunol , vol.23 , pp. 364-377
    • Chiu, C.H.1    Guu, Y.K.2    Liu, C.H.3    Pan, T.M.4    Cheng, W.5
  • 3
    • 33847786431 scopus 로고    scopus 로고
    • Reactive oxygen species detoxification by catalase is a major determinant of fecundity in the mosquito Anopheles gambiae
    • De Jong R.J., Miller L.M., Molina-Cruz A., Gupta L., Kumar S., and Barillas-Mury C. Reactive oxygen species detoxification by catalase is a major determinant of fecundity in the mosquito Anopheles gambiae. Proc Natl Acad Sci USA 104 (2007) 2121-2126
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 2121-2126
    • De Jong, R.J.1    Miller, L.M.2    Molina-Cruz, A.3    Gupta, L.4    Kumar, S.5    Barillas-Mury, C.6
  • 4
    • 0035476441 scopus 로고    scopus 로고
    • Modulation of the Ras/MAPK signalling pathway by the redox function of selenoproteins in Drosophila melanogaster
    • Morey M., Serras F., Baguñà J., Hafen E., and Corominas M. Modulation of the Ras/MAPK signalling pathway by the redox function of selenoproteins in Drosophila melanogaster. Dev Biol 238 1 (2001) 145-156
    • (2001) Dev Biol , vol.238 , Issue.1 , pp. 145-156
    • Morey, M.1    Serras, F.2    Baguñà, J.3    Hafen, E.4    Corominas, M.5
  • 7
    • 33645220455 scopus 로고    scopus 로고
    • Oxidative stress in marine environments: biochemistry and physiological ecology
    • Lesser M.P. Oxidative stress in marine environments: biochemistry and physiological ecology. Annu Rev Physiol 68 (2006) 253-278
    • (2006) Annu Rev Physiol , vol.68 , pp. 253-278
    • Lesser, M.P.1
  • 9
    • 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., and Benkendorff K. Stress and immune responses in abalone: limitations in current knowledge and investigative methods based on other models. Fish Shellfish Immunol 22 (2007) 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
  • 10
    • 0027284743 scopus 로고
    • Molecular characterization and rescue of acatalasemic mutants of Drosophila melanogaster
    • Griswold C., Mathews A.L., Bewly K.E., and Mahaffey J.M. Molecular characterization and rescue of acatalasemic mutants of Drosophila melanogaster. Genetics 134 (1993) 781-788
    • (1993) Genetics , vol.134 , pp. 781-788
    • Griswold, C.1    Mathews, A.L.2    Bewly, K.E.3    Mahaffey, J.M.4
  • 11
    • 10044248993 scopus 로고    scopus 로고
    • Reactive oxygen species and tendinopathy: do they matter
    • Bestwick C.S., and Maffulli N. Reactive oxygen species and tendinopathy: do they matter. Br J Sports Med 38 (2004) 672-674
    • (2004) Br J Sports Med , vol.38 , pp. 672-674
    • Bestwick, C.S.1    Maffulli, N.2
  • 12
    • 14844311938 scopus 로고    scopus 로고
    • Catalase from the silkworm, Bombyx mori: gene sequence, distribution, and overexpression
    • Yamamoto K., Banno Y., Fujii H., Miake F., Kashige N., and Aso Y. Catalase from the silkworm, Bombyx mori: gene sequence, distribution, and overexpression. Insect Biochem Mol Biol 35 (2005) 277-283
    • (2005) Insect Biochem Mol Biol , vol.35 , pp. 277-283
    • Yamamoto, K.1    Banno, Y.2    Fujii, H.3    Miake, F.4    Kashige, N.5    Aso, Y.6
  • 13
    • 0022179287 scopus 로고
    • The active center of catalase
    • Fita I., and Rossmann M.G. The active center of catalase. J Mol Biol 185 (1985) 21-37
    • (1985) J Mol Biol , vol.185 , pp. 21-37
    • Fita, I.1    Rossmann, M.G.2
  • 14
    • 0022764275 scopus 로고
    • Temporal variation for the expression of catalase in Drosophila melanogaster. Correlations between rates of enzymes synthesis and levels of translatable catalase-messenger RNA
    • Glenn C. Temporal variation for the expression of catalase in Drosophila melanogaster. Correlations between rates of enzymes synthesis and levels of translatable catalase-messenger RNA. Genetics 113 (1986) 919-938
    • (1986) Genetics , vol.113 , pp. 919-938
    • Glenn, C.1
  • 15
    • 0024392669 scopus 로고
    • The genetics of catalase in Drosophila melanogaster: isolation and characterization of acatalasemic mutants
    • Mackay M., and Bewley G.C. The genetics of catalase in Drosophila melanogaster: isolation and characterization of acatalasemic mutants. Genetics 22 (1989) 643-652
    • (1989) Genetics , vol.22 , pp. 643-652
    • Mackay, M.1    Bewley, G.C.2
  • 17
    • 2542643915 scopus 로고    scopus 로고
    • Transcriptional regulation of the Drosophila catalase gene by the DRE/DREF system
    • Park S.Y., Kim Y.S., Yang D.J., and Yoo M.A. Transcriptional regulation of the Drosophila catalase gene by the DRE/DREF system. Nucleic Acids Res 32 4 (2004) 1318-1324
    • (2004) Nucleic Acids Res , vol.32 , Issue.4 , pp. 1318-1324
    • Park, S.Y.1    Kim, Y.S.2    Yang, D.J.3    Yoo, M.A.4
  • 18
    • 0030795327 scopus 로고    scopus 로고
    • Oxidative modification of macromolecules
    • Vaughan M. Oxidative modification of macromolecules. J Biol Chem 272 (1997) 18513
    • (1997) J Biol Chem , vol.272 , pp. 18513
    • Vaughan, M.1
  • 19
    • 4644307153 scopus 로고    scopus 로고
    • Seasonal variations in antioxidant defences in blue mussels Mytilus edulis collected from a polluted area: major contributions in gills of an inducible isoform of Cu/Zn-superoxide dismutase and of glutathione S-transferase
    • Manduzio H., Monsinjon T., Galap C., Leboulenger F., and Rocher B. Seasonal variations in antioxidant defences in blue mussels Mytilus edulis collected from a polluted area: major contributions in gills of an inducible isoform of Cu/Zn-superoxide dismutase and of glutathione S-transferase. Aqua Toxicol 7 1 (2004) 83-93
    • (2004) Aqua Toxicol , vol.7 , Issue.1 , pp. 83-93
    • Manduzio, H.1    Monsinjon, T.2    Galap, C.3    Leboulenger, F.4    Rocher, B.5
  • 20
    • 0032967443 scopus 로고    scopus 로고
    • Molecular and biological mechanisms of antioxidant action
    • Frei B. Molecular and biological mechanisms of antioxidant action. FASEB J 13 (1999) 963-964
    • (1999) FASEB J , vol.13 , pp. 963-964
    • Frei, B.1
  • 21
  • 22
    • 0035145679 scopus 로고    scopus 로고
    • Multiple catalase genes are differentially regulated in Aspergillus nidulans
    • Kawasaki L., and Aguirre J. Multiple catalase genes are differentially regulated in Aspergillus nidulans. J Bacteriol 183 4 (2001) 1434-1440
    • (2001) J Bacteriol , vol.183 , Issue.4 , pp. 1434-1440
    • Kawasaki, L.1    Aguirre, J.2
  • 23
    • 0031428587 scopus 로고    scopus 로고
    • Comparison of catalase in diploid and haploid Rana rugosa using heat and chemical inactivation techniques
    • Kashiwagi A., Kashiwagi K., Takase M., Hanada H., and Nakamura M. Comparison of catalase in diploid and haploid Rana rugosa using heat and chemical inactivation techniques. Comp Biochem Physiol B 118 (1997) 499-503
    • (1997) Comp Biochem Physiol B , vol.118 , pp. 499-503
    • Kashiwagi, A.1    Kashiwagi, K.2    Takase, M.3    Hanada, H.4    Nakamura, M.5
  • 24
    • 0029019526 scopus 로고
    • Differential evolution and expression of murine peroxisomal membrane protein genes
    • Bryant D.D., and Wilson G.N. Differential evolution and expression of murine peroxisomal membrane protein genes. Biochem Mol Med 55 (1995) 22-30
    • (1995) Biochem Mol Med , vol.55 , pp. 22-30
    • Bryant, D.D.1    Wilson, G.N.2
  • 25
    • 0030911678 scopus 로고    scopus 로고
    • Regulation of catalases in Arabidopsis
    • McClung C.R. Regulation of catalases in Arabidopsis. Free Radic Biol Med 23 (1997) 489-496
    • (1997) Free Radic Biol Med , vol.23 , pp. 489-496
    • McClung, C.R.1
  • 26
    • 0026594669 scopus 로고
    • OxyR: a regulator of antioxidant genes
    • Storz G., and Tartaglia L.A. OxyR: a regulator of antioxidant genes. J Nutr 122 (1992) 627-630
    • (1992) J Nutr , vol.122 , pp. 627-630
    • Storz, G.1    Tartaglia, L.A.2
  • 27
    • 0034635333 scopus 로고    scopus 로고
    • Active and inhibited human catalase structures: ligand and NADPH binding and catalytic mechanism
    • Putnam C.D., Arvai A.S., Bourne Y., and Tainer J.A. Active and inhibited human catalase structures: ligand and NADPH binding and catalytic mechanism. J Mol Biol 296 (2000) 295-309
    • (2000) J Mol Biol , vol.296 , pp. 295-309
    • Putnam, C.D.1    Arvai, A.S.2    Bourne, Y.3    Tainer, J.A.4
  • 29
    • 0033936557 scopus 로고    scopus 로고
    • Cloning and expression of a cDNA coding for catalase from zebrafish (Danio rerio)
    • Ken C., Lin C., Wu J., and Shaw J. Cloning and expression of a cDNA coding for catalase from zebrafish (Danio rerio). J Agric Food Chem 48 (2000) 2092-2096
    • (2000) J Agric Food Chem , vol.48 , pp. 2092-2096
    • Ken, C.1    Lin, C.2    Wu, J.3    Shaw, J.4
  • 30
    • 0030854046 scopus 로고    scopus 로고
    • Phylogenetic relationships among prokaryotic and eukaryotic catalases
    • Klotz M.G., Klassen G.R., and Loewen P.C. Phylogenetic relationships among prokaryotic and eukaryotic catalases. Mol Biol Evol 14 (1997) 951-958
    • (1997) Mol Biol Evol , vol.14 , pp. 951-958
    • Klotz, M.G.1    Klassen, G.R.2    Loewen, P.C.3
  • 31
    • 33845737016 scopus 로고    scopus 로고
    • Effects of dietary vitamin A on antioxidant responses of abalone Haliotis discus hannai Ino
    • Fu J., Zhang W., Mai K., Feng X., Xu W., Liufu Z., et al. Effects of dietary vitamin A on antioxidant responses of abalone Haliotis discus hannai Ino. Acta Oceanol Sin 25 (2006) 141-150
    • (2006) Acta Oceanol Sin , vol.25 , pp. 141-150
    • Fu, J.1    Zhang, W.2    Mai, K.3    Feng, X.4    Xu, W.5    Liufu, Z.6
  • 32
    • 0141625786 scopus 로고    scopus 로고
    • Effect of copper exposure on the antioxidant enzymes in bivalve mollusc Scapharca inaequivalvis
    • Isani G., Monari M., Andreani G., Fabbri M., and Carpenè E. Effect of copper exposure on the antioxidant enzymes in bivalve mollusc Scapharca inaequivalvis. Vet Res Commun 27 (2003) 691-693
    • (2003) Vet Res Commun , vol.27 , pp. 691-693
    • Isani, G.1    Monari, M.2    Andreani, G.3    Fabbri, M.4    Carpenè, E.5
  • 34
    • 0028888954 scopus 로고
    • Glutathione, glutathione-dependent and antioxidant enzymes in mussel, Mytilus galloprovincialis, exposed to metals under field and laboratory conditions: implications for the use of biochemical biomarkers
    • Regoli F., and Principato G. Glutathione, glutathione-dependent and antioxidant enzymes in mussel, Mytilus galloprovincialis, exposed to metals under field and laboratory conditions: implications for the use of biochemical biomarkers. Aquat Toxicol 31 (1995) 143-164
    • (1995) Aquat Toxicol , vol.31 , pp. 143-164
    • Regoli, F.1    Principato, G.2
  • 35
    • 34248215727 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a putative lipopolysaccharide-induced TNF-alpha factor (LITAF) gene homologue from Zhikong scallop Chlamys farreri
    • Yu Y., Qiu L., Song L., Zhao J., Ni D., Zhang Y., et al. Molecular cloning and characterization of a putative lipopolysaccharide-induced TNF-alpha factor (LITAF) gene homologue from Zhikong scallop Chlamys farreri. Fish Shellfish Immunol 23 (2007) 419-429
    • (2007) Fish Shellfish Immunol , vol.23 , pp. 419-429
    • Yu, Y.1    Qiu, L.2    Song, L.3    Zhao, J.4    Ni, D.5    Zhang, Y.6
  • 36
    • 0036169929 scopus 로고    scopus 로고
    • Association of nucleotide patterns with gene function classes: application to human 3′ untranslated sequence
    • Conklin D., Jonassen I., Aasland R., and Taylor W. Association of nucleotide patterns with gene function classes: application to human 3′ untranslated sequence. Bioinformatics 18 (2002) 182-189
    • (2002) Bioinformatics , vol.18 , pp. 182-189
    • Conklin, D.1    Jonassen, I.2    Aasland, R.3    Taylor, W.4
  • 37
    • 0033667955 scopus 로고    scopus 로고
    • Immunolocalization of four antioxidant enzymes in digestive glands of mollusks and crustaceans and fish liver
    • Orbea A., Fahimi H.D., and Cajaraville M.P. Immunolocalization of four antioxidant enzymes in digestive glands of mollusks and crustaceans and fish liver. Histochem Cell Biol 114 (2000) 393-404
    • (2000) Histochem Cell Biol , vol.114 , pp. 393-404
    • Orbea, A.1    Fahimi, H.D.2    Cajaraville, M.P.3
  • 38
    • 0033665666 scopus 로고    scopus 로고
    • Molecular cloning and sequence analysis of the Danio rerio catalase gene
    • Gerhard G.S., Kauffman E.J., and Grundy M.A. Molecular cloning and sequence analysis of the Danio rerio catalase gene. Comp Biochem Physiol B 127 (2000) 447-457
    • (2000) Comp Biochem Physiol B , vol.127 , pp. 447-457
    • Gerhard, G.S.1    Kauffman, E.J.2    Grundy, M.A.3
  • 40
    • 0028171293 scopus 로고
    • 2 from the oxidative burst orchestrates the plant hypersensitive disease resistance response
    • 2 from the oxidative burst orchestrates the plant hypersensitive disease resistance response. Cell 79 (1994) 583-593
    • (1994) Cell , vol.79 , pp. 583-593
    • Levine, A.1    Tenhaken, R.2    Dixon, R.3    Lamb, C.4
  • 41
    • 0041571485 scopus 로고    scopus 로고
    • Measurement of Crassostrea gigas hemocyte oxidative metabolism by flow cytometry and the inhibiting capacity of pathogenic vibrios
    • Lambert C., Soudant P., Choquet G., and Paillard C. Measurement of Crassostrea gigas hemocyte oxidative metabolism by flow cytometry and the inhibiting capacity of pathogenic vibrios. Fish Shellfish Immunol 15 (2003) 225-240
    • (2003) Fish Shellfish Immunol , vol.15 , pp. 225-240
    • Lambert, C.1    Soudant, P.2    Choquet, G.3    Paillard, C.4
  • 42
    • 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., Tseng M., and 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 23 (2007) 34-45
    • (2007) Fish Shellfish Immunol , vol.23 , pp. 34-45
    • Liu, C.1    Tseng, M.2    Cheng, W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.