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Volumn 113, Issue 2, 2007, Pages 107-116

Molecular characterization of goose-type lysozyme homologue of large yellow croaker and its involvement in immune response induced by trivalent bacterial vaccine as an acute-phase protein

Author keywords

Acute phase protein; Gene expression; Goose type lysozyme; Large yellow croaker Pseudosciana crocea; Trivalent bacterial vaccine

Indexed keywords

ACUTE PHASE PROTEIN; BACTERIAL VACCINE; LYSOZYME; MESSENGER RNA;

EID: 35248885592     PISSN: 01652478     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.imlet.2007.08.001     Document Type: Article
Times cited : (90)

References (46)
  • 1
    • 0021490172 scopus 로고
    • What's new in lysozyme research?
    • Jolles P., and Jolles J. What's new in lysozyme research?. Mol Cell Biochem 63 (1984) 165-189
    • (1984) Mol Cell Biochem , vol.63 , pp. 165-189
    • Jolles, P.1    Jolles, J.2
  • 2
    • 0029687175 scopus 로고    scopus 로고
    • Animal lysozymes c and g: an overview
    • Jolles P. (Ed), Birkhauser Verlag, Basel, Switzerland
    • Prager E.M., and Jolles P. Animal lysozymes c and g: an overview. In: Jolles P. (Ed). Lysozymes: model enzyme in biochemistry and biology vol. 75 (1996), Birkhauser Verlag, Basel, Switzerland 9-31
    • (1996) Lysozymes: model enzyme in biochemistry and biology , vol.75 , pp. 9-31
    • Prager, E.M.1    Jolles, P.2
  • 3
    • 0034255255 scopus 로고    scopus 로고
    • The role of antimicrobial peptides in animal defenses
    • Hancock R., and Scott M.G. The role of antimicrobial peptides in animal defenses. Proc Natl Acad Sci USA 97 (2000) 8856-8861
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 8856-8861
    • Hancock, R.1    Scott, M.G.2
  • 4
    • 0035038578 scopus 로고    scopus 로고
    • Synergy of histone-derived peptides of coho salmon with lysozyme and flounder pleurocidin
    • Patrzykat A., Zhang L., Mendoza V., Iwama G.K., and Hancock R. Synergy of histone-derived peptides of coho salmon with lysozyme and flounder pleurocidin. Antimicrob Agents Chemother 45 (2001) 1337-1342
    • (2001) Antimicrob Agents Chemother , vol.45 , pp. 1337-1342
    • Patrzykat, A.1    Zhang, L.2    Mendoza, V.3    Iwama, G.K.4    Hancock, R.5
  • 5
    • 0035032985 scopus 로고    scopus 로고
    • Synergistic interactions between mammalian antimicrobial defense peptides
    • Yan H., and Hancock R.E. Synergistic interactions between mammalian antimicrobial defense peptides. Antimicrob Agents Chemother 45 (2001) 1558-1560
    • (2001) Antimicrob Agents Chemother , vol.45 , pp. 1558-1560
    • Yan, H.1    Hancock, R.E.2
  • 6
    • 0036213293 scopus 로고    scopus 로고
    • Phylogenetic analysis of invertebrate lysozymes and the evolution of lysozyme function
    • Bachali S., Jager M., Hassanin A., Schoentgen F., Jolles P., Fiala-Medioni A., et al. Phylogenetic analysis of invertebrate lysozymes and the evolution of lysozyme function. J Mol Evol 54 (2002) 652-664
    • (2002) J Mol Evol , vol.54 , pp. 652-664
    • Bachali, S.1    Jager, M.2    Hassanin, A.3    Schoentgen, F.4    Jolles, P.5    Fiala-Medioni, A.6
  • 7
    • 0029689664 scopus 로고    scopus 로고
    • Phage lysozymes
    • Jolles P. (Ed), Birkhauser Verlag, Basel, Switzerland
    • Fastrez J. Phage lysozymes. In: Jolles P. (Ed). Lysozymes: model enzymes in biochemistry and biology vol. 75 (1996), Birkhauser Verlag, Basel, Switzerland 35-64
    • (1996) Lysozymes: model enzymes in biochemistry and biology , vol.75 , pp. 35-64
    • Fastrez, J.1
  • 9
    • 0141922176 scopus 로고    scopus 로고
    • Characterization and function of kuruma shrimp lysozyme possessing lytic activity against Vibrio species
    • Hikima S., Hikima J., Rojtinnakorn J., Hirono I., and Aoki T. Characterization and function of kuruma shrimp lysozyme possessing lytic activity against Vibrio species. Gene 316 (2003) 187-195
    • (2003) Gene , vol.316 , pp. 187-195
    • Hikima, S.1    Hikima, J.2    Rojtinnakorn, J.3    Hirono, I.4    Aoki, T.5
  • 10
    • 0029689192 scopus 로고    scopus 로고
    • Insect lysozymes
    • Jolles P. (Ed), Birkhauser Verlag, Basel, Switzerland
    • Hultmark D. Insect lysozymes. In: Jolles P. (Ed). Lysozymes: model enzyme in biochemistry and biology vol. 75 (1996), Birkhauser Verlag, Basel, Switzerland 87-102
    • (1996) Lysozymes: model enzyme in biochemistry and biology , vol.75 , pp. 87-102
    • Hultmark, D.1
  • 11
    • 0033556162 scopus 로고    scopus 로고
    • Amino acid sequences of lysozymes newly purified from invertebrate simply wide distribution of a novel class in the lysozyme family
    • Ito Y., Yoshikawa A., Hotani T., Fukuda S., Sugimura K., and Imoto T. Amino acid sequences of lysozymes newly purified from invertebrate simply wide distribution of a novel class in the lysozyme family. Eur J Biochem 259 (1999) 456-461
    • (1999) Eur J Biochem , vol.259 , pp. 456-461
    • Ito, Y.1    Yoshikawa, A.2    Hotani, T.3    Fukuda, S.4    Sugimura, K.5    Imoto, T.6
  • 12
    • 0029688888 scopus 로고    scopus 로고
    • From the discovery of lysozyme to the characterization of several lysozyme families
    • Jolles P. From the discovery of lysozyme to the characterization of several lysozyme families. Experientia 75 Suppl (1996) 3-5
    • (1996) Experientia , vol.75 , Issue.SUPPL , pp. 3-5
    • Jolles, P.1
  • 13
    • 0025949805 scopus 로고
    • Goose-type lysozyme gene of the chicken: sequence, genomic organization and expression reveals major differences to chicken-type lysozyme gene
    • Nakano T., and Graf T. Goose-type lysozyme gene of the chicken: sequence, genomic organization and expression reveals major differences to chicken-type lysozyme gene. Biochim Biophys Acta 1090 (1991) 273-276
    • (1991) Biochim Biophys Acta , vol.1090 , pp. 273-276
    • Nakano, T.1    Graf, T.2
  • 14
    • 0029689666 scopus 로고    scopus 로고
    • Adaptive evolution of lysozyme: changes in amino acid sequence, regulation of expression and gene number
    • Jolles P. (Ed), Birkhauser Verlag, Basel
    • Prager E.M. Adaptive evolution of lysozyme: changes in amino acid sequence, regulation of expression and gene number. In: Jolles P. (Ed). Lysozymes: model enzyme in biochemistry and biology vol. 75 (1996), Birkhauser Verlag, Basel 323-345
    • (1996) Lysozymes: model enzyme in biochemistry and biology , vol.75 , pp. 323-345
    • Prager, E.M.1
  • 15
    • 0030800608 scopus 로고    scopus 로고
    • Molecular divergence of lysozymes and lactalbumin
    • Qasba P.K., and Kumar S. Molecular divergence of lysozymes and lactalbumin. Crit Rev Biochem Mol Biol 32 (1997) 255-306
    • (1997) Crit Rev Biochem Mol Biol , vol.32 , pp. 255-306
    • Qasba, P.K.1    Kumar, S.2
  • 16
    • 0028057562 scopus 로고
    • The lysozyme locus in Drosophila melanogaster: an expanded gene family adapted for expression in the digestive tract
    • Daffre S., Kylsten P., Samakovlis C., and Hultmark D. The lysozyme locus in Drosophila melanogaster: an expanded gene family adapted for expression in the digestive tract. Mol Gen Genet 242 (1994) 152-162
    • (1994) Mol Gen Genet , vol.242 , pp. 152-162
    • Daffre, S.1    Kylsten, P.2    Samakovlis, C.3    Hultmark, D.4
  • 17
    • 0034190077 scopus 로고    scopus 로고
    • Molecular cloning and novel repeated sequences of a c-type lysozyme gene in Japanese flounder (Paralichthys olivaceus)
    • Hikima J., Hirono I.I., and Aoki T. Molecular cloning and novel repeated sequences of a c-type lysozyme gene in Japanese flounder (Paralichthys olivaceus). Mar Biotechnol 2 (2000) 241-247
    • (2000) Mar Biotechnol , vol.2 , pp. 241-247
    • Hikima, J.1    Hirono, I.I.2    Aoki, T.3
  • 18
    • 0027420448 scopus 로고
    • Characterization of the cow stomach lysozyme genes: repeated DNA and concerted evolution
    • Irwin D.M., White R.T., and Wilson A.C. Characterization of the cow stomach lysozyme genes: repeated DNA and concerted evolution. J Mol Evol 37 (1993) 355-366
    • (1993) J Mol Evol , vol.37 , pp. 355-366
    • Irwin, D.M.1    White, R.T.2    Wilson, A.C.3
  • 19
    • 0019143031 scopus 로고
    • Exons encode functional and structural units of chicken lysozyme
    • Jung A., Sippel A.E., Grez M., and Schutz G. Exons encode functional and structural units of chicken lysozyme. Proc Natl Acad Sci USA 77 (1980) 5759-5763
    • (1980) Proc Natl Acad Sci USA , vol.77 , pp. 5759-5763
    • Jung, A.1    Sippel, A.E.2    Grez, M.3    Schutz, G.4
  • 20
    • 0024403169 scopus 로고
    • The human lysozyme gene. Sequence organization and chromosomal localization
    • Peters C.W.B., Kruse U., Pollwein R., Grzeschik K.H., and Sippel A.E. The human lysozyme gene. Sequence organization and chromosomal localization. Eur J Biochem 182 (1989) 507-516
    • (1989) Eur J Biochem , vol.182 , pp. 507-516
    • Peters, C.W.B.1    Kruse, U.2    Pollwein, R.3    Grzeschik, K.H.4    Sippel, A.E.5
  • 21
    • 0001470610 scopus 로고
    • Complete amino acid sequence of embden goose (Anser anser) egg-white lysozyme
    • Simpson R.J., and Morgan F.L. Complete amino acid sequence of embden goose (Anser anser) egg-white lysozyme. Biochem Biophys Acta 744 (1983) 349-351
    • (1983) Biochem Biophys Acta , vol.744 , pp. 349-351
    • Simpson, R.J.1    Morgan, F.L.2
  • 22
    • 0019335167 scopus 로고
    • Complete amino acid sequence of the goose-type lysozyme from the egg white of the black swan
    • Richard J.S., Geoffrey S.B., Donna S.D., and Francis J.M. Complete amino acid sequence of the goose-type lysozyme from the egg white of the black swan. Biochemistry 19 (1980) 1814-1819
    • (1980) Biochemistry , vol.19 , pp. 1814-1819
    • Richard, J.S.1    Geoffrey, S.B.2    Donna, S.D.3    Francis, J.M.4
  • 23
    • 0020122109 scopus 로고
    • Complete amino acid sequence of ostrich (Struthio camelus) egg-white lysozyme, a goose-type lysozyme
    • Schoentgen F., Jolles J., and Jolles P. Complete amino acid sequence of ostrich (Struthio camelus) egg-white lysozyme, a goose-type lysozyme. Eur J Biochem 123 (1982) 489-497
    • (1982) Eur J Biochem , vol.123 , pp. 489-497
    • Schoentgen, F.1    Jolles, J.2    Jolles, P.3
  • 25
    • 4544348304 scopus 로고    scopus 로고
    • The primary structure of a novel goose-type lysozyme from rhea egg white
    • Pooart J., Torikata T., and Araki T. The primary structure of a novel goose-type lysozyme from rhea egg white. Biosci Biotechnol Biochem 68 (2004) 159-169
    • (2004) Biosci Biotechnol Biochem , vol.68 , pp. 159-169
    • Pooart, J.1    Torikata, T.2    Araki, T.3
  • 26
    • 0037309920 scopus 로고    scopus 로고
    • Molecular evolution of vertebrate goose-type lysozyme genes
    • Irwin D.M., and Gong Z.Y. Molecular evolution of vertebrate goose-type lysozyme genes. J Mol Evol 56 (2003) 234-242
    • (2003) J Mol Evol , vol.56 , pp. 234-242
    • Irwin, D.M.1    Gong, Z.Y.2
  • 27
    • 0035973859 scopus 로고    scopus 로고
    • Molecular cloning, expression and evolution of the Japanese flounder goose-type lysozyme gene, and the lytic activity of its recombinant protein
    • Hikima J., Minagawa S., Hirono I., and Aoki T. Molecular cloning, expression and evolution of the Japanese flounder goose-type lysozyme gene, and the lytic activity of its recombinant protein. Biochim Biophys Acta 30 (2001) 35-44
    • (2001) Biochim Biophys Acta , vol.30 , pp. 35-44
    • Hikima, J.1    Minagawa, S.2    Hirono, I.3    Aoki, T.4
  • 28
    • 0043074437 scopus 로고    scopus 로고
    • Molecular cloning of G-type lysozyme cDNA in common carp (Cyprinuscarpio L.)
    • Savan R., Aman A., and Sakai M. Molecular cloning of G-type lysozyme cDNA in common carp (Cyprinuscarpio L.). Fish Shellfish Immunol 15 (2003) 263-268
    • (2003) Fish Shellfish Immunol , vol.15 , pp. 263-268
    • Savan, R.1    Aman, A.2    Sakai, M.3
  • 29
    • 32344443468 scopus 로고    scopus 로고
    • Gene structure of goose-type lysozyme in the mandarinfish Sinipercachuatsi with analysis on the lytic activity of its recombinant in Escherichia coli
    • Sun B.J., Wang G.L., Xie H.X., Gao Q., and Nie P. Gene structure of goose-type lysozyme in the mandarinfish Sinipercachuatsi with analysis on the lytic activity of its recombinant in Escherichia coli. Aquaculture 252 (2006) 106-113
    • (2006) Aquaculture , vol.252 , pp. 106-113
    • Sun, B.J.1    Wang, G.L.2    Xie, H.X.3    Gao, Q.4    Nie, P.5
  • 30
    • 33748862602 scopus 로고    scopus 로고
    • Molecular cloning of an invertebrate goose-type lysozyme gene from Chlamys farreri, and lytic activity of the recombinant protein
    • Zhao J.M., Song L.S., Li C.H., Zou H.B., Ni D.J., Wang W., et al. Molecular cloning of an invertebrate goose-type lysozyme gene from Chlamys farreri, and lytic activity of the recombinant protein. Mol Immunol 44 (2007) 1198-1208
    • (2007) Mol Immunol , vol.44 , pp. 1198-1208
    • Zhao, J.M.1    Song, L.S.2    Li, C.H.3    Zou, H.B.4    Ni, D.J.5    Wang, W.6
  • 31
    • 0042267811 scopus 로고    scopus 로고
    • Molecular cloning, expression of orange-spotted grouper goose-type lysozyme cDNA, and lytic activity of its recombinant protein
    • Yin Z.X., He J.G., Deng W.X., and Chan S.M. Molecular cloning, expression of orange-spotted grouper goose-type lysozyme cDNA, and lytic activity of its recombinant protein. Dis Aquat Org 55 (2003) 117-123
    • (2003) Dis Aquat Org , vol.55 , pp. 117-123
    • Yin, Z.X.1    He, J.G.2    Deng, W.X.3    Chan, S.M.4
  • 32
    • 33645891655 scopus 로고    scopus 로고
    • Cloning and expression analysis of interferon-γ-inducible-lysosomal thiol reductase gene in large yellow croaker (Pseudosciaena crocea)
    • Zheng W., and Chen X. Cloning and expression analysis of interferon-γ-inducible-lysosomal thiol reductase gene in large yellow croaker (Pseudosciaena crocea). Mol Immunol 43 (2006) 2135-2141
    • (2006) Mol Immunol , vol.43 , pp. 2135-2141
    • Zheng, W.1    Chen, X.2
  • 33
    • 33745652680 scopus 로고    scopus 로고
    • Expression analysis of immune-relevant genes in the spleen of large yellow croaker, Pseudosciaena crocea, stimulated by polyI:C
    • Zheng W., Liu G., Ao J., and Chen X. Expression analysis of immune-relevant genes in the spleen of large yellow croaker, Pseudosciaena crocea, stimulated by polyI:C. Fish Shellfish Immunol 21 (2006) 414-430
    • (2006) Fish Shellfish Immunol , vol.21 , pp. 414-430
    • Zheng, W.1    Liu, G.2    Ao, J.3    Chen, X.4
  • 34
    • 35248871786 scopus 로고    scopus 로고
    • Sambrook J, Fritsch EF, Maniatis T. A laboratory manual, 3rd ed. Cold Spring Harbor, New York: Cold Spring Harbor Laboratory Press; Molecular Cloning 2001.
  • 35
    • 0035019128 scopus 로고    scopus 로고
    • Expression of Japanese flounder c-type lysozyme cDNA in insect cells
    • Minagawa S., Hikima J., Hirono I., Aoki T., and Mori H. Expression of Japanese flounder c-type lysozyme cDNA in insect cells. Dev Comp Immunol 25 (2001) 439-445
    • (2001) Dev Comp Immunol , vol.25 , pp. 439-445
    • Minagawa, S.1    Hikima, J.2    Hirono, I.3    Aoki, T.4    Mori, H.5
  • 36
    • 33748928226 scopus 로고    scopus 로고
    • Experimental verification of the crucial roles of Glu73 in the catalytic activity and structural stability of goose-type lysozyme
    • Kawamura S., Ohno K., Ohkuma M., Chijiiwa Y., and Torikata T. Experimental verification of the crucial roles of Glu73 in the catalytic activity and structural stability of goose-type lysozyme. J Biochem 140 (2006) 75-85
    • (2006) J Biochem , vol.140 , pp. 75-85
    • Kawamura, S.1    Ohno, K.2    Ohkuma, M.3    Chijiiwa, Y.4    Torikata, T.5
  • 37
    • 0020629394 scopus 로고
    • Goose-type lysozyme structure: an evolutionary link between hen and bacteriophage lysozymes?
    • Grutter M.G., Weaver L.H., and Matthews B.W. Goose-type lysozyme structure: an evolutionary link between hen and bacteriophage lysozymes?. Nature 303 (1983) 828-831
    • (1983) Nature , vol.303 , pp. 828-831
    • Grutter, M.G.1    Weaver, L.H.2    Matthews, B.W.3
  • 38
    • 17444366534 scopus 로고    scopus 로고
    • Early innate immune response and redistribution of inflammatory cells in the bony fish gilthead seabream experimentally infected with Vibrio anguillarum
    • Chaves-Pozo E., Muñoz P., López-Muñoz A., Pelegrín P., Ayala A.G., Mulero V., et al. Early innate immune response and redistribution of inflammatory cells in the bony fish gilthead seabream experimentally infected with Vibrio anguillarum. Cell Tissue Res 320 (2005) 61-68
    • (2005) Cell Tissue Res , vol.320 , pp. 61-68
    • Chaves-Pozo, E.1    Muñoz, P.2    López-Muñoz, A.3    Pelegrín, P.4    Ayala, A.G.5    Mulero, V.6
  • 40
    • 0028127216 scopus 로고
    • The far upstream chicken lysozyme enhancer at -6.1 kilobase, by interacting with NF-M, mediates lipopolysaccharide-induced expression of the chicken lysozyme gene in chicken myelomonocytic cells
    • Goethe R., and Phi-Van L. The far upstream chicken lysozyme enhancer at -6.1 kilobase, by interacting with NF-M, mediates lipopolysaccharide-induced expression of the chicken lysozyme gene in chicken myelomonocytic cells. J Biol Chem 269 (1994) 31302-31309
    • (1994) J Biol Chem , vol.269 , pp. 31302-31309
    • Goethe, R.1    Phi-Van, L.2
  • 41
    • 0030941083 scopus 로고    scopus 로고
    • Evidence for an enhanced transcription-dependent de novo synthesis of C/EBPβ in the LPS activation of the chicken lysozyme gene
    • Goethe R., and Phi-Van L. Evidence for an enhanced transcription-dependent de novo synthesis of C/EBPβ in the LPS activation of the chicken lysozyme gene. J Leukoc Biol 61 (1997) 367-374
    • (1997) J Leukoc Biol , vol.61 , pp. 367-374
    • Goethe, R.1    Phi-Van, L.2
  • 42
    • 0032525001 scopus 로고    scopus 로고
    • Posttranscriptional lipopolysaccharide regulation of the lysozyme gene at processing of the primary transcript in myelomonocytic HD11 cells
    • Goethe R., and Phi-Van L. Posttranscriptional lipopolysaccharide regulation of the lysozyme gene at processing of the primary transcript in myelomonocytic HD11 cells. J Immunol 160 (1998) 4970-4978
    • (1998) J Immunol , vol.160 , pp. 4970-4978
    • Goethe, R.1    Phi-Van, L.2
  • 43
    • 0030020217 scopus 로고    scopus 로고
    • Transcriptional activation of the chicken lysozyme gene by NF-κBp65 (RelA) and c-Rel, but not by NF-κBp50
    • Phi-Van L. Transcriptional activation of the chicken lysozyme gene by NF-κBp65 (RelA) and c-Rel, but not by NF-κBp50. Biochem J 313 (1996) 39-44
    • (1996) Biochem J , vol.313 , pp. 39-44
    • Phi-Van, L.1
  • 44
    • 0035072848 scopus 로고    scopus 로고
    • 2+ in LPS-activated expression of the chicken lysozyme gene
    • 2+ in LPS-activated expression of the chicken lysozyme gene. J Leukoc Biol 69 (2001) 651-658
    • (2001) J Leukoc Biol , vol.69 , pp. 651-658
    • Regenhard, P.1    Goethe, R.2    Phi-Van, L.3
  • 45
    • 0025865317 scopus 로고
    • The inducible transcription activator NF-κB: regulation by distinct protein subunits
    • Baeuerle P.A. The inducible transcription activator NF-κB: regulation by distinct protein subunits. Biochim Biophys Acta 1072 (1991) 63-80
    • (1991) Biochim Biophys Acta , vol.1072 , pp. 63-80
    • Baeuerle, P.A.1
  • 46
    • 0028217586 scopus 로고
    • Lipopolysaccharide induction of tissue factor gene expression in monocytic cells is mediated by binding of c-rel/p65 heterodimers to a κB-like site
    • Oeth P.A., Parry G.C., Kunsch C., Nantermet P., Rosen C.A., and Mackman N. Lipopolysaccharide induction of tissue factor gene expression in monocytic cells is mediated by binding of c-rel/p65 heterodimers to a κB-like site. Mol Cell Biol 14 (1994) 3772-3781
    • (1994) Mol Cell Biol , vol.14 , pp. 3772-3781
    • Oeth, P.A.1    Parry, G.C.2    Kunsch, C.3    Nantermet, P.4    Rosen, C.A.5    Mackman, N.6


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