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Volumn 48, Issue 4, 2011, Pages 524-531

Characterization and expression of HLysG2, a basic goose-type lysozyme from the human eye and testis

Author keywords

Antimicrobial activity; Goose type lysozyme; Innate immunity; Tears

Indexed keywords

HUMAN LYSOZYME G LIKE 2; LYSOZYME; UNCLASSIFIED DRUG;

EID: 78650601863     PISSN: 01615890     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molimm.2010.10.008     Document Type: Article
Times cited : (15)

References (43)
  • 1
    • 0015754419 scopus 로고
    • Multiple genes for lysozyme in birds; studies on black swan egg white lysozyme
    • Arnheim N., Hindenbeg A., Begg G.S., Morgan F.J. Multiple genes for lysozyme in birds; studies on black swan egg white lysozyme. J. Biol. Chem. 1973, 248:8036-8042.
    • (1973) J. Biol. Chem. , vol.248 , pp. 8036-8042
    • Arnheim, N.1    Hindenbeg, A.2    Begg, G.S.3    Morgan, F.J.4
  • 2
    • 1642439861 scopus 로고    scopus 로고
    • The lysozyme of the starfish Asterias rubens. A paradygmatic type i lysozyme
    • Bachali S., Bailly X., Jollès J., Jollès P., Deutsch J.S. The lysozyme of the starfish Asterias rubens. A paradygmatic type i lysozyme. Eur. J. Biochem. 2004, 271:237-242.
    • (2004) Eur. J. Biochem. , vol.271 , pp. 237-242
    • Bachali, S.1    Bailly, X.2    Jollès, J.3    Jollès, P.4    Deutsch, J.S.5
  • 4
    • 0014197552 scopus 로고
    • Purification and characterization of a lysozyme from goose egg white
    • Canfield R.E., McMurry S. Purification and characterization of a lysozyme from goose egg white. Biochem. Biophys. Res. Commun. 1967, 26:38-42.
    • (1967) Biochem. Biophys. Res. Commun. , vol.26 , pp. 38-42
    • Canfield, R.E.1    McMurry, S.2
  • 5
    • 0014687514 scopus 로고
    • The dependence of lysozyme activity on pH and ionic strength
    • Davies R.C., Neuberger A., Wilson B.M. The dependence of lysozyme activity on pH and ionic strength. Biochim. Biophys. Acta 1969, 178:294-305.
    • (1969) Biochim. Biophys. Acta , vol.178 , pp. 294-305
    • Davies, R.C.1    Neuberger, A.2    Wilson, B.M.3
  • 6
    • 33748754288 scopus 로고    scopus 로고
    • Identification of 491 proteins in the tear fluid proteome reveals a large number of proteases and protease inhibitors
    • de Souza G.A., Godoy L.M., Mann M. Identification of 491 proteins in the tear fluid proteome reveals a large number of proteases and protease inhibitors. Genome Biol. 2006, 7:R27.
    • (2006) Genome Biol. , vol.7
    • de Souza, G.A.1    Godoy, L.M.2    Mann, M.3
  • 8
    • 0014986596 scopus 로고
    • Antibacterial action of spermine: effect on urinary tract pathogen
    • Fair W.R., Wehner N. Antibacterial action of spermine: effect on urinary tract pathogen. Appl. Microbiol. 1971, 21:6-8.
    • (1971) Appl. Microbiol. , vol.21 , pp. 6-8
    • Fair, W.R.1    Wehner, N.2
  • 9
    • 0345269265 scopus 로고    scopus 로고
    • Mass spectrometric techniques applied to the analysis of human tears: a focus on the peptide and protein constituents
    • Fung K., Morris C., Duncan M. Mass spectrometric techniques applied to the analysis of human tears: a focus on the peptide and protein constituents. Adv. Exp. Med. Biol. 2002, 506:601-605.
    • (2002) Adv. Exp. Med. Biol. , vol.506 , pp. 601-605
    • Fung, K.1    Morris, C.2    Duncan, M.3
  • 10
    • 0038208105 scopus 로고    scopus 로고
    • Lysozyme from the gut of the soft tick Ornithodoros moubata: the sequence, phylogeny and post-feeding regulation
    • Grunclová L., Fouquier H., Hypša V., Kopáček P. Lysozyme from the gut of the soft tick Ornithodoros moubata: the sequence, phylogeny and post-feeding regulation. Dev. Comp. Immunol. 2003, 27:651-660.
    • (2003) Dev. Comp. Immunol. , vol.27 , pp. 651-660
    • Grunclová, L.1    Fouquier, H.2    Hypša, V.3    Kopáček, P.4
  • 11
    • 0020629394 scopus 로고
    • Goose lysozyme structure: an evolutionary link between hen and bacteriophage lysozymes?
    • Grütter M.G., Weaver L.H., Matthews B.W. Goose lysozyme structure: an evolutionary link between hen and bacteriophage lysozymes?. Nature 1983, 303:828-831.
    • (1983) Nature , vol.303 , pp. 828-831
    • Grütter, M.G.1    Weaver, L.H.2    Matthews, B.W.3
  • 12
    • 78650615856 scopus 로고    scopus 로고
    • A unique c lysozyme-like protein has a role in fertilization
    • Herrero M.B., Mandal A., Digilio L., Herr J. A unique c lysozyme-like protein has a role in fertilization. FASEB J. 2004, 18:4-5.
    • (2004) FASEB J. , vol.18 , pp. 4-5
    • Herrero, M.B.1    Mandal, A.2    Digilio, L.3    Herr, J.4
  • 13
    • 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., 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 2001, 1520:35-44.
    • (2001) Biochim. Biophys. Acta , vol.1520 , pp. 35-44
    • Hikima, J.1    Minagawa, S.2    Hirono, I.3    Aoki, T.4
  • 14
    • 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., Aoki T. Characterization and function of kuruma shrimp lysozyme possessing lytic activity against Vibrio species. Gene 2003, 316:187-195.
    • (2003) Gene , vol.316 , pp. 187-195
    • Hikima, S.1    Hikima, J.2    Rojtinnakorn, J.3    Hirono, I.4    Aoki, T.5
  • 16
    • 0035964823 scopus 로고    scopus 로고
    • Genetic evidence that antibacterial activity of lysozyme is independent of its catalytic function
    • Ibrahim H.R., Matsuzaki T., Aoki T. Genetic evidence that antibacterial activity of lysozyme is independent of its catalytic function. FEBS Lett. 2001, 506:27-32.
    • (2001) FEBS Lett. , vol.506 , pp. 27-32
    • Ibrahim, H.R.1    Matsuzaki, T.2    Aoki, T.3
  • 17
    • 0037309920 scopus 로고    scopus 로고
    • Molecular evolution of vertebrate goose-type lysozyme genes
    • Irwin D.M., Gong Z.Y. Molecular evolution of vertebrate goose-type lysozyme genes. J. Mol. Evol. 2003, 56:234-242.
    • (2003) J. Mol. Evol. , vol.56 , pp. 234-242
    • Irwin, D.M.1    Gong, Z.Y.2
  • 18
    • 0029914094 scopus 로고    scopus 로고
    • The ruminant digestion model using bacteria already employed early in evolution by symbiotic molluscs
    • Jollès J., Fiala-Medioni A., Jollès P. The ruminant digestion model using bacteria already employed early in evolution by symbiotic molluscs. J. Mol. Evol. 1996, 43:523-527.
    • (1996) J. Mol. Evol. , vol.43 , pp. 523-527
    • Jollès, J.1    Fiala-Medioni, A.2    Jollès, P.3
  • 19
    • 0021490172 scopus 로고
    • What's new in lysozyme research?
    • Jollès P., Jollès J. What's new in lysozyme research?. Mol. Cell Biochem. 1984, 63:165-189.
    • (1984) Mol. Cell Biochem. , vol.63 , pp. 165-189
    • Jollès, P.1    Jollès, J.2
  • 20
    • 0017227664 scopus 로고
    • Stimulation of phagocytosis by human lysozyme
    • Klockars M., Roberts P. Stimulation of phagocytosis by human lysozyme. Acta Haematol. 1976, 55:289-295.
    • (1976) Acta Haematol. , vol.55 , pp. 289-295
    • Klockars, M.1    Roberts, P.2
  • 21
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of bacteriophage T4. Nature 1970, 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 23
    • 33344459927 scopus 로고    scopus 로고
    • Characterization, organization and expression of AmphiLysC, an acidic c-type lysozyme gene in amphioxus Branchiostoma belcheri tsingtauense
    • Liu M., Zhang S., Liu Z., Li H., Xu A. Characterization, organization and expression of AmphiLysC, an acidic c-type lysozyme gene in amphioxus Branchiostoma belcheri tsingtauense. Gene 2006, 367:110-117.
    • (2006) Gene , vol.367 , pp. 110-117
    • Liu, M.1    Zhang, S.2    Liu, Z.3    Li, H.4    Xu, A.5
  • 24
    • 0035019128 scopus 로고    scopus 로고
    • Expression of Japanese flounder c-type lysozyme cDNA in insect cells
    • Minagawa S., Hikima J., Hirono I., Aoki T., Mori H. Expression of Japanese flounder c-type lysozyme cDNA in insect cells. Dev. Comp. Immunol. 2001, 25:439-445.
    • (2001) Dev. Comp. Immunol. , vol.25 , pp. 439-445
    • Minagawa, S.1    Hikima, J.2    Hirono, I.3    Aoki, T.4    Mori, H.5
  • 25
    • 0025949805 scopus 로고
    • Goose-type lysozyme gene of the chicken: sequence, genomic organization and expression reveals major differences to chickentype lysozyme gene
    • Nakano T., Graf T. Goose-type lysozyme gene of the chicken: sequence, genomic organization and expression reveals major differences to chickentype lysozyme gene. Biochim. Biophys. Acta 1991, 1090:273-276.
    • (1991) Biochim. Biophys. Acta , vol.1090 , pp. 273-276
    • Nakano, T.1    Graf, T.2
  • 26
    • 0015890012 scopus 로고
    • Effects of lysozyme on normal and transformed mammalian cells
    • Osserman E.F., Klockars M., Halper J., Fischel R.E. Effects of lysozyme on normal and transformed mammalian cells. Nature 1973, 243:331-335.
    • (1973) Nature , vol.243 , pp. 331-335
    • Osserman, E.F.1    Klockars, M.2    Halper, J.3    Fischel, R.E.4
  • 28
    • 0029687175 scopus 로고    scopus 로고
    • Animal lysozymes c and g: an overview
    • Birkhäuser Verlag, Basel, Switzerland, P. Jollès (Ed.)
    • Prager E.M., Jollès P. Animal lysozymes c and g: an overview. Lysozymes: Model Enzyme in Biochemistry and Biology 1996, 9-31. Birkhäuser Verlag, Basel, Switzerland. P. Jollès (Ed.).
    • (1996) Lysozymes: Model Enzyme in Biochemistry and Biology , pp. 9-31
    • Prager, E.M.1    Jollès, P.2
  • 29
    • 0032078495 scopus 로고    scopus 로고
    • Molecular adaptation of Drosophila melanogaster lysozymes to a digestive function
    • Regel R., Matioli S.R., Terra W.R. Molecular adaptation of Drosophila melanogaster lysozymes to a digestive function. Insect. Biochem. Mol. Biol. 1998, 28:309-319.
    • (1998) Insect. Biochem. Mol. Biol. , vol.28 , pp. 309-319
    • Regel, R.1    Matioli, S.R.2    Terra, W.R.3
  • 30
    • 34247124903 scopus 로고
    • The measurement of lysozyme activity and the ultraviolet inactivation of lysozyme
    • Shugar D. The measurement of lysozyme activity and the ultraviolet inactivation of lysozyme. Biochim. Biophys. Acta 1952, 8:302-309.
    • (1952) Biochim. Biophys. Acta , vol.8 , pp. 302-309
    • Shugar, D.1
  • 31
    • 0019335167 scopus 로고
    • Complete amino acid sequence of the goose-type lysozyme from the egg white of the black swan
    • Simpson R.J., Begg G.S., Dorow D.S., Morgan F.J. Complete amino acid sequence of the goose-type lysozyme from the egg white of the black swan. Biochemistry 1980, 19:1814-1819.
    • (1980) Biochemistry , vol.19 , pp. 1814-1819
    • Simpson, R.J.1    Begg, G.S.2    Dorow, D.S.3    Morgan, F.J.4
  • 32
    • 8744288933 scopus 로고    scopus 로고
    • Immuneresponsive lysozymes from hemocytes of the American dog tick, Dermacentor variabilis and an embryonic cell line of the Rocky Mountain wood tick, D. andersoni
    • Simser J.A., Macaluso K.R., Mulenga A., Azad A.F. Immuneresponsive lysozymes from hemocytes of the American dog tick, Dermacentor variabilis and an embryonic cell line of the Rocky Mountain wood tick, D. andersoni. Insect. Biochem. Mol. Biol. 2004, 34:1235-1246.
    • (2004) Insect. Biochem. Mol. Biol. , vol.34 , pp. 1235-1246
    • Simser, J.A.1    Macaluso, K.R.2    Mulenga, A.3    Azad, A.F.4
  • 33
    • 0036425270 scopus 로고    scopus 로고
    • Synonymous codon usage bias and the expression of human glucocerebrosidase in the methylotrophic yeast, Pichia pastoris
    • Sinclair G., Choy F.Y. Synonymous codon usage bias and the expression of human glucocerebrosidase in the methylotrophic yeast, Pichia pastoris. Protein Expr. Purif. 2002, 26:96-105.
    • (2002) Protein Expr. Purif. , vol.26 , pp. 96-105
    • Sinclair, G.1    Choy, F.Y.2
  • 34
    • 0042087873 scopus 로고
    • Factors affecting the lytic activity of lysozyme
    • Smolelis A.N., Hartsell S.E. Factors affecting the lytic activity of lysozyme. J. Bacteriol. 1952, 63:665-674.
    • (1952) J. Bacteriol. , vol.63 , pp. 665-674
    • Smolelis, A.N.1    Hartsell, S.E.2
  • 36
    • 0035292701 scopus 로고    scopus 로고
    • Purification and characterization of goose type lysozyme from Cassovary (Casuarius casuarius) egg white
    • Thammasirirak S., Torikata T., Takami K., Murata K., Araki T. Purification and characterization of goose type lysozyme from Cassovary (Casuarius casuarius) egg white. Biosci. Biotechnol. Biochem. 2001, 65:584-592.
    • (2001) Biosci. Biotechnol. Biochem. , vol.65 , pp. 584-592
    • Thammasirirak, S.1    Torikata, T.2    Takami, K.3    Murata, K.4    Araki, T.5
  • 38
    • 0021713792 scopus 로고
    • Comparison of goose-type, chicken-type, and phage-type lysozymes illustrates the changes that occur in both amino acid sequence and three-dimensional structure during evolution
    • Weaver L.H., Grütter M.G., Remington S.J., Gray T.M., Isaacs N.W., Matthews B.W. Comparison of goose-type, chicken-type, and phage-type lysozymes illustrates the changes that occur in both amino acid sequence and three-dimensional structure during evolution. J. Mol. Evol. 1985, 21:97-111.
    • (1985) J. Mol. Evol. , vol.21 , pp. 97-111
    • Weaver, L.H.1    Grütter, M.G.2    Remington, S.J.3    Gray, T.M.4    Isaacs, N.W.5    Matthews, B.W.6
  • 40
    • 0035032985 scopus 로고    scopus 로고
    • Synergistic interactions between mammalian antimicrobial defense peptides
    • Yan H., Hancock R.E. Synergistic interactions between mammalian antimicrobial defense peptides. Antimicrob. Agents Chemother. 2001, 45:1558-1560.
    • (2001) Antimicrob. Agents Chemother. , vol.45 , pp. 1558-1560
    • Yan, H.1    Hancock, R.E.2
  • 41
    • 27144469476 scopus 로고    scopus 로고
    • Molecular cloning and characterization of three novel lysozyme-like genes, predominantly expressed in the male reproductive system of humans, belonging to the c-type lysozyme/alpha-lactalbumin family
    • Zhang K., Gao R., Zhang H., Cai X., Shen C., Wu C., Zhao S., Yu L. Molecular cloning and characterization of three novel lysozyme-like genes, predominantly expressed in the male reproductive system of humans, belonging to the c-type lysozyme/alpha-lactalbumin family. Biol. Reprod. 2005, 73:1064-1071.
    • (2005) Biol. Reprod. , vol.73 , pp. 1064-1071
    • Zhang, K.1    Gao, R.2    Zhang, H.3    Cai, X.4    Shen, C.5    Wu, C.6    Zhao, S.7    Yu, L.8
  • 42
    • 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., Xu W. Molecular cloning of an invertebrate goose-type lysozyme gene from Chlamys farreri, and lytic activity of the recombinant protein. Mol. Immunol. 2007, 44:1198-1208.
    • (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    Xu, W.7
  • 43
    • 23444440822 scopus 로고    scopus 로고
    • Molecular cloning and characterization analysis of cDNA encoding g-type lysozyme from scallop (Argopecten irradians)
    • Zou H., Song L., Xu W., Yang G. Molecular cloning and characterization analysis of cDNA encoding g-type lysozyme from scallop (Argopecten irradians). High Tech. Lett. 2005, 15:101-106.
    • (2005) High Tech. Lett. , vol.15 , pp. 101-106
    • Zou, H.1    Song, L.2    Xu, W.3    Yang, G.4


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