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Volumn 33, Issue 2, 2012, Pages 213-219

Identification and characterization of a hepcidin from half-smooth tongue sole Cynoglossus semilaevis

Author keywords

Antimicrobial peptide; Cynoglossus semilaevis; Hepcidin; Innate immunity; Vibrio anguillarum

Indexed keywords

BACTERIA (MICROORGANISMS); CYNOGLOSSIDAE; CYNOGLOSSUS SEMILAEVIS; EDWARDSIELLA TARDA; LISTONELLA ANGUILLARUM; SOLEA SENEGALENSIS;

EID: 84863204512     PISSN: 10504648     EISSN: 10959947     Source Type: Journal    
DOI: 10.1016/j.fsi.2012.04.011     Document Type: Article
Times cited : (45)

References (42)
  • 1
    • 22844435410 scopus 로고    scopus 로고
    • Innate immunity of fish (overview)
    • Magnadottir B. Innate immunity of fish (overview). Fish Shellfish Immunol 2006, 20:137-151.
    • (2006) Fish Shellfish Immunol , vol.20 , pp. 137-151
    • Magnadottir, B.1
  • 2
    • 0035496012 scopus 로고    scopus 로고
    • Cationic peptides: effectors in innate immunity and novel antimicrobials
    • Hancock R.E.W. Cationic peptides: effectors in innate immunity and novel antimicrobials. Lancet Infect Dis 2001, 156-164.
    • (2001) Lancet Infect Dis , pp. 156-164
    • Hancock, R.E.W.1
  • 4
    • 0034284595 scopus 로고    scopus 로고
    • LEAP-1, a novel highly disulfide-bonded human peptide, exhibits antimicrobial activity
    • Krause A., Neitz S., Mägert H.J., Schulz A., Forssmann W.G., Schulz-Knappe P., et al. LEAP-1, a novel highly disulfide-bonded human peptide, exhibits antimicrobial activity. FEBS Lett 2000, 480:147-150.
    • (2000) FEBS Lett , vol.480 , pp. 147-150
    • Krause, A.1    Neitz, S.2    Mägert, H.J.3    Schulz, A.4    Forssmann, W.G.5    Schulz-Knappe, P.6
  • 5
    • 0035896642 scopus 로고    scopus 로고
    • Hepcidin, a urinary antimicrobial peptide synthesized in the liver
    • Park C.H., Valore E.V., Waring A.J., Ganz T. Hepcidin, a urinary antimicrobial peptide synthesized in the liver. J Biol Chem 2001, 276:7806-7810.
    • (2001) J Biol Chem , vol.276 , pp. 7806-7810
    • Park, C.H.1    Valore, E.V.2    Waring, A.J.3    Ganz, T.4
  • 6
    • 0035902605 scopus 로고    scopus 로고
    • Lack of hepcidin gene expression and severe tissue iron overload in upstream stimulatory factor 2 (USF2) knockout mice
    • Nicolas G., Bennoun M., Devaux I., Beaumont C., Grandchamp B., Kahn A., et al. Lack of hepcidin gene expression and severe tissue iron overload in upstream stimulatory factor 2 (USF2) knockout mice. Proc Natl Acad Sci U S A 2001, 98:8780-8785.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 8780-8785
    • Nicolas, G.1    Bennoun, M.2    Devaux, I.3    Beaumont, C.4    Grandchamp, B.5    Kahn, A.6
  • 7
    • 42649123323 scopus 로고    scopus 로고
    • Molecular evolution and characterization of hepcidin gene products in vertebrates
    • Hilton K.B., Lambert L.A. Molecular evolution and characterization of hepcidin gene products in vertebrates. Gene 2008, 415:40-48.
    • (2008) Gene , vol.415 , pp. 40-48
    • Hilton, K.B.1    Lambert, L.A.2
  • 8
    • 10844258104 scopus 로고    scopus 로고
    • Hepcidin regulates cellular iron efflux by binding to ferroportin and inducing its internalization
    • Nemeth E., Tuttle M.S., Powelson J., Vaughn M.B., Donovan A., Ward D.M., et al. Hepcidin regulates cellular iron efflux by binding to ferroportin and inducing its internalization. Science 2004, 306:2090-2093.
    • (2004) Science , vol.306 , pp. 2090-2093
    • Nemeth, E.1    Tuttle, M.S.2    Powelson, J.3    Vaughn, M.B.4    Donovan, A.5    Ward, D.M.6
  • 9
    • 50149110932 scopus 로고    scopus 로고
    • Identification, cloning and expression analysis of a hepcidin cDNA of the Atlantic cod (Gadus morhua L.)
    • Solstad T., Larsen A.N., Seppola M., Jørgensen T.Ø. Identification, cloning and expression analysis of a hepcidin cDNA of the Atlantic cod (Gadus morhua L.). Fish Shellfish Immunol 2008, 25:298-310.
    • (2008) Fish Shellfish Immunol , vol.25 , pp. 298-310
    • Solstad, T.1    Larsen, A.N.2    Seppola, M.3    Jørgensen, T.Ø.4
  • 11
    • 34250824283 scopus 로고    scopus 로고
    • Three different hepcidins from tilapia, Oreochromis mossambicus: analysis of their expressions and biological functions
    • Huang P.H., Chen J.Y., Kuo C.M. Three different hepcidins from tilapia, Oreochromis mossambicus: analysis of their expressions and biological functions. Mol Immunol 2007, 44:1922-1934.
    • (2007) Mol Immunol , vol.44 , pp. 1922-1934
    • Huang, P.H.1    Chen, J.Y.2    Kuo, C.M.3
  • 12
    • 0037409525 scopus 로고    scopus 로고
    • Identification and expression analysis of hepcidin-like antimicrobial peptides in bony fish
    • Douglas S.E., Gallant J.W., Liebscher R.S., Dacanay A., Tsoi S.C. Identification and expression analysis of hepcidin-like antimicrobial peptides in bony fish. Dev Comp Immunol 2003, 27:589-601.
    • (2003) Dev Comp Immunol , vol.27 , pp. 589-601
    • Douglas, S.E.1    Gallant, J.W.2    Liebscher, R.S.3    Dacanay, A.4    Tsoi, S.C.5
  • 13
    • 27144471911 scopus 로고    scopus 로고
    • Two different types of hepcidins from the Japanese flounder Paralichthys olivaceus
    • Hirono I., Hwang J.Y., Ono Y., Kurobe T., Ohira T., Nozaki R., et al. Two different types of hepcidins from the Japanese flounder Paralichthys olivaceus. FEBS J 2005, 272:5257-5264.
    • (2005) FEBS J , vol.272 , pp. 5257-5264
    • Hirono, I.1    Hwang, J.Y.2    Ono, Y.3    Kurobe, T.4    Ohira, T.5    Nozaki, R.6
  • 14
    • 33746312646 scopus 로고    scopus 로고
    • Dual function of fish hepcidin: response to experimental iron overload and bacterial infection in sea bass (Dicentrarchus labrax)
    • Rodrigues P.N., Vázquez-Dorado S., Neves J.V., Wilson J.M. Dual function of fish hepcidin: response to experimental iron overload and bacterial infection in sea bass (Dicentrarchus labrax). Dev Comp Immunol 2006, 30:1156-1167.
    • (2006) Dev Comp Immunol , vol.30 , pp. 1156-1167
    • Rodrigues, P.N.1    Vázquez-Dorado, S.2    Neves, J.V.3    Wilson, J.M.4
  • 15
    • 34548501544 scopus 로고    scopus 로고
    • Genomic organization and tissue-specific expression analysis of hepcidin-like genes from black porgy (Acanthopagrus schlegelii B)
    • Yang M., Wang K.J., Chen J.H., Qu H.D., Li S.J. Genomic organization and tissue-specific expression analysis of hepcidin-like genes from black porgy (Acanthopagrus schlegelii B). Fish Shellfish Immunol 2007, 23:1060-1071.
    • (2007) Fish Shellfish Immunol , vol.23 , pp. 1060-1071
    • Yang, M.1    Wang, K.J.2    Chen, J.H.3    Qu, H.D.4    Li, S.J.5
  • 17
    • 15944388315 scopus 로고    scopus 로고
    • Expressed sequence tags analysis of Atlantic halibut (Hippoglossus hippoglossus) liver, kidney and spleen tissues following vaccination against Vibrio anguillarum and Aeromonas salmonicida
    • Park K.C., Osborne J.A., Tsoi S.C., Brown L.L., Johnson S.C. Expressed sequence tags analysis of Atlantic halibut (Hippoglossus hippoglossus) liver, kidney and spleen tissues following vaccination against Vibrio anguillarum and Aeromonas salmonicida. Fish Shellfish Immunol 2005, 18:393-415.
    • (2005) Fish Shellfish Immunol , vol.18 , pp. 393-415
    • Park, K.C.1    Osborne, J.A.2    Tsoi, S.C.3    Brown, L.L.4    Johnson, S.C.5
  • 18
    • 21444448913 scopus 로고    scopus 로고
    • Catfish hepcidin gene is expressed in a wide range of tissues and exhibits tissue-specific upregulation after bacterial infection
    • Bao B., Peatman E., Li P., He C., Liu Z. Catfish hepcidin gene is expressed in a wide range of tissues and exhibits tissue-specific upregulation after bacterial infection. Dev Comp Immunol 2005, 29:939-950.
    • (2005) Dev Comp Immunol , vol.29 , pp. 939-950
    • Bao, B.1    Peatman, E.2    Li, P.3    He, C.4    Liu, Z.5
  • 19
    • 20144369874 scopus 로고    scopus 로고
    • Bass hepcidin synthesis, solution structure, antimicrobial activities and synergism, and in vivo hepatic response to bacterial infections
    • Lauth X., Babon J.J., Stannard J.A., Singh S., Nizet V., Carlberg J.M., et al. Bass hepcidin synthesis, solution structure, antimicrobial activities and synergism, and in vivo hepatic response to bacterial infections. J Biol Chem 2005, 280:9272-9282.
    • (2005) J Biol Chem , vol.280 , pp. 9272-9282
    • Lauth, X.1    Babon, J.J.2    Stannard, J.A.3    Singh, S.4    Nizet, V.5    Carlberg, J.M.6
  • 20
    • 18144366586 scopus 로고    scopus 로고
    • Expression and preparation of recombinant hepcidin in Escherichia coli
    • Zhang H., Yuan Q., Zhu Y., Ma R. Expression and preparation of recombinant hepcidin in Escherichia coli. Protein Exp Purif 2005, 41:409-416.
    • (2005) Protein Exp Purif , vol.41 , pp. 409-416
    • Zhang, H.1    Yuan, Q.2    Zhu, Y.3    Ma, R.4
  • 22
    • 0842313260 scopus 로고    scopus 로고
    • Prediction of proprotein convertase cleavage sites
    • Duckert P., Brunak S., Blom N. Prediction of proprotein convertase cleavage sites. Protein Eng Des Sel 2004, 17:107-112.
    • (2004) Protein Eng Des Sel , vol.17 , pp. 107-112
    • Duckert, P.1    Brunak, S.2    Blom, N.3
  • 23
    • 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(24):4876-4882.
    • (1997) Nucleic Acids Res , vol.25 , Issue.24 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 24
    • 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
  • 25
    • 0023375195 scopus 로고
    • The neighbor-joining method: a new method for reconstructing phylogenetic trees
    • Saitou N., Nei M. The neighbor-joining method: a new method for reconstructing phylogenetic trees. Mol Biol Evol 1987, 4(4):406-425.
    • (1987) Mol Biol Evol , vol.4 , Issue.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2
  • 26
    • 0022179034 scopus 로고
    • Vibrio anguillarum: prevalence of typical and atypical strains in marine recipients with special reference to carbohydrate pollution
    • Larsen J.L. Vibrio anguillarum: prevalence of typical and atypical strains in marine recipients with special reference to carbohydrate pollution. Acta Vet Scand 1985, 26(4):449-460.
    • (1985) Acta Vet Scand , vol.26 , Issue.4 , pp. 449-460
    • Larsen, J.L.1
  • 28
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding. Anal Biochem 1976, 72:248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 29
    • 0027201086 scopus 로고
    • A novel inducible antibacterial peptide of Drosophila carries an O-glycosylated substitution
    • Bulet P., Dimarcq J.L., Hetru C., Lagueux M., Charlet M., Hegy G., et al. A novel inducible antibacterial peptide of Drosophila carries an O-glycosylated substitution. J Biol Chem 1993, 268:14893-14897.
    • (1993) J Biol Chem , vol.268 , pp. 14893-14897
    • Bulet, P.1    Dimarcq, J.L.2    Hetru, C.3    Lagueux, M.4    Charlet, M.5    Hegy, G.6
  • 30
    • 33746021126 scopus 로고    scopus 로고
    • Hepcidins in amphibians and fishes: antimicrobial peptides or iron-regulatory hormones?
    • Shi J., Camus A.C. Hepcidins in amphibians and fishes: antimicrobial peptides or iron-regulatory hormones?. Dev Comp Immunol 2006, 30:746-755.
    • (2006) Dev Comp Immunol , vol.30 , pp. 746-755
    • Shi, J.1    Camus, A.C.2
  • 31
    • 0035896581 scopus 로고    scopus 로고
    • A new mouse liver-specific gene, encoding a protein homologous to human antimicrobial peptide hepcidin, is overexpressed during iron overload
    • Pigeon C., Ilyin G., Courselaud B., Leroyer P., Turlin B., Brissot P., et al. A new mouse liver-specific gene, encoding a protein homologous to human antimicrobial peptide hepcidin, is overexpressed during iron overload. J Biol Chem 2001, 16(276):7811-7819.
    • (2001) J Biol Chem , vol.16 , Issue.276 , pp. 7811-7819
    • Pigeon, C.1    Ilyin, G.2    Courselaud, B.3    Leroyer, P.4    Turlin, B.5    Brissot, P.6
  • 32
    • 78751650063 scopus 로고    scopus 로고
    • Applications of antimicrobial peptides from fish and perspectives for the future
    • Rajanbabu V., Chen J.Y. Applications of antimicrobial peptides from fish and perspectives for the future. Peptides 2011, 415-420.
    • (2011) Peptides , pp. 415-420
    • Rajanbabu, V.1    Chen, J.Y.2
  • 33
    • 79959796646 scopus 로고    scopus 로고
    • Two hepcidin-like antimicrobial peptides in Barramundi Lates calcarifer exhibit differing tissue tropism and are induced in response to lipopolysaccharide
    • Barnes A.C., Trewin B., Snape N., Kvennefors E.C.E. Two hepcidin-like antimicrobial peptides in Barramundi Lates calcarifer exhibit differing tissue tropism and are induced in response to lipopolysaccharide. Fish Shellfish Immunol 2011, 31:350-357.
    • (2011) Fish Shellfish Immunol , vol.31 , pp. 350-357
    • Barnes, A.C.1    Trewin, B.2    Snape, N.3    Kvennefors, E.C.E.4
  • 34
    • 65649117326 scopus 로고    scopus 로고
    • Identification of centrarchid hepcidins and evidence that 17β-estradiol disrupts constitutive expression of hepcidin-1 and inducible expression of hepcidin-2 in largemouth bass (Micropterus salmoides)
    • Robertson L.S., Iwanowicz L.R., Marranca J.M. Identification of centrarchid hepcidins and evidence that 17β-estradiol disrupts constitutive expression of hepcidin-1 and inducible expression of hepcidin-2 in largemouth bass (Micropterus salmoides). Fish Shellfish Immunol 2009, 26:898-907.
    • (2009) Fish Shellfish Immunol , vol.26 , pp. 898-907
    • Robertson, L.S.1    Iwanowicz, L.R.2    Marranca, J.M.3
  • 35
    • 0037020241 scopus 로고    scopus 로고
    • The solution structure of human hepcidin, a peptide hormone with antimicrobial activity that is involved in iron uptake and hereditary hemochromatosis
    • Hunter H.N., Fulton D.B., Ganz T., Vogel H.J. The solution structure of human hepcidin, a peptide hormone with antimicrobial activity that is involved in iron uptake and hereditary hemochromatosis. J Biol Chem 2002, 277:37597-37603.
    • (2002) J Biol Chem , vol.277 , pp. 37597-37603
    • Hunter, H.N.1    Fulton, D.B.2    Ganz, T.3    Vogel, H.J.4
  • 36
    • 30144432585 scopus 로고    scopus 로고
    • The N-terminus of hepcidin is essential for its interaction with ferroportin: structure-function study
    • Nemeth E., Preza G.C., Jung C.L., Kaplan J., Waring A.J., Ganz T. The N-terminus of hepcidin is essential for its interaction with ferroportin: structure-function study. Blood 2006, 107:328-333.
    • (2006) Blood , vol.107 , pp. 328-333
    • Nemeth, E.1    Preza, G.C.2    Jung, C.L.3    Kaplan, J.4    Waring, A.J.5    Ganz, T.6
  • 37
    • 79960774021 scopus 로고    scopus 로고
    • Identification and differential expression of microRNAs during metamorphosis of the Japanese flounder (Paralichthys olivaceus)
    • Fu Y.S., Shi Z.Y., Wu M.L., Zhang J.L., Jia L., Chen X.W. Identification and differential expression of microRNAs during metamorphosis of the Japanese flounder (Paralichthys olivaceus). PLoS One 2011, 6(7):e22957.
    • (2011) PLoS One , vol.6 , Issue.7
    • Fu, Y.S.1    Shi, Z.Y.2    Wu, M.L.3    Zhang, J.L.4    Jia, L.5    Chen, X.W.6
  • 38
    • 62749142958 scopus 로고    scopus 로고
    • Isolation and characterization of Toll-like receptor 9 in half-smooth tongue sole Cynoglossus semilaevis
    • Yu Y., Zhang Q.Q., Li C.M., Jiang L.M., Yan F.S., Wang Z.G., et al. Isolation and characterization of Toll-like receptor 9 in half-smooth tongue sole Cynoglossus semilaevis. Fish Shellfish Immunol 2009, 26:492-499.
    • (2009) Fish Shellfish Immunol , vol.26 , pp. 492-499
    • Yu, Y.1    Zhang, Q.Q.2    Li, C.M.3    Jiang, L.M.4    Yan, F.S.5    Wang, Z.G.6
  • 39
    • 77953559341 scopus 로고    scopus 로고
    • Isolation, polymorphism and expression study of two distinct major histocompatibility complex class II B genes from half-smooth tongue sole (Cynoglossus semilaevis)
    • Li C.M., Yu Y., Sun Y.Y., Li S., Zhong Q.W., Wang X.B., et al. Isolation, polymorphism and expression study of two distinct major histocompatibility complex class II B genes from half-smooth tongue sole (Cynoglossus semilaevis). Int J Immunogenet 2010, 37(3):185-197.
    • (2010) Int J Immunogenet , vol.37 , Issue.3 , pp. 185-197
    • Li, C.M.1    Yu, Y.2    Sun, Y.Y.3    Li, S.4    Zhong, Q.W.5    Wang, X.B.6
  • 40
    • 65649117325 scopus 로고    scopus 로고
    • Full-length sequence and expression analysis of a myeloid differentiation factor 88 (MyD88) in half-smooth tongue sole Cynoglossus semilaevis
    • Yu Y., Zhong Q.W., Li C.M., Jiang L.M., Yan F.S., Wang Z.G., et al. Full-length sequence and expression analysis of a myeloid differentiation factor 88 (MyD88) in half-smooth tongue sole Cynoglossus semilaevis. Int J Immunogenet 2009, 36:173-182.
    • (2009) Int J Immunogenet , vol.36 , pp. 173-182
    • Yu, Y.1    Zhong, Q.W.2    Li, C.M.3    Jiang, L.M.4    Yan, F.S.5    Wang, Z.G.6
  • 41
    • 46149091263 scopus 로고    scopus 로고
    • Kupffer cells modulate iron homeostasis in mice via regulation of hepcidin expression
    • Theurl M., Theurl I., Hochegger K., Obrist P., Subramaniam N., van Rooijen N., et al. Kupffer cells modulate iron homeostasis in mice via regulation of hepcidin expression. J Mol Med 2008, 86:825-835.
    • (2008) J Mol Med , vol.86 , pp. 825-835
    • Theurl, M.1    Theurl, I.2    Hochegger, K.3    Obrist, P.4    Subramaniam, N.5    van Rooijen, N.6
  • 42
    • 40149102505 scopus 로고    scopus 로고
    • The antimicrobial peptide hepcidin exerts an important role in the innate immunity against bacteria in the bony fish gilthead seabream
    • Cuesta A., Meseguer J., Esteban M.A. The antimicrobial peptide hepcidin exerts an important role in the innate immunity against bacteria in the bony fish gilthead seabream. Mol Immunol 2008, 45:2333-2342.
    • (2008) Mol Immunol , vol.45 , pp. 2333-2342
    • Cuesta, A.1    Meseguer, J.2    Esteban, M.A.3


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