메뉴 건너뛰기




Volumn 31, Issue 6, 2011, Pages 1154-1161

Molecular mechanisms of hepcidin regulation in sea bass (Dicentrarchus labrax)

Author keywords

Hepcidin; Infection; Iron; Regulation; Sea bass (Dicentrarchus labrax)

Indexed keywords

DICENTRARCHUS LABRAX; MAMMALIA; PHOTOBACTERIUM DAMSELAE; SERRANIDAE; TELEOSTEI;

EID: 81255208438     PISSN: 10504648     EISSN: 10959947     Source Type: Journal    
DOI: 10.1016/j.fsi.2011.10.006     Document Type: Article
Times cited : (31)

References (56)
  • 1
    • 0034284595 scopus 로고    scopus 로고
    • LEAP-1, a novel highly disulfide-bonded human peptide, exhibits antimicrobial activity
    • Krause A., Neitz S., Magert 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(2-3):147-150.
    • (2000) FEBS Lett , vol.480 , Issue.2-3 , pp. 147-150
    • Krause, A.1    Neitz, S.2    Magert, H.J.3    Schulz, A.4    Forssmann, W.G.5    Schulz-Knappe, P.6
  • 2
    • 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(11):7806-7810.
    • (2001) J Biol Chem , vol.276 , Issue.11 , pp. 7806-7810
    • Park, C.H.1    Valore, E.V.2    Waring, A.J.3    Ganz, T.4
  • 3
    • 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(1):328-333.
    • (2006) Blood , vol.107 , Issue.1 , pp. 328-333
    • Nemeth, E.1    Preza, G.C.2    Jung, C.L.3    Kaplan, J.4    Waring, A.J.5    Ganz, T.6
  • 4
    • 69949088488 scopus 로고    scopus 로고
    • Hepcidin, the iron watcher
    • Viatte L., Vaulont S. Hepcidin, the iron watcher. Biochimie 2009, 91(10):1223-1228.
    • (2009) Biochimie , vol.91 , Issue.10 , pp. 1223-1228
    • Viatte, L.1    Vaulont, S.2
  • 5
    • 33750133047 scopus 로고    scopus 로고
    • Regulation of iron metabolism by hepcidin
    • Nemeth E., Ganz T. Regulation of iron metabolism by hepcidin. Annu Rev Nutr 2006, 26323-26342.
    • (2006) Annu Rev Nutr , pp. 26323-26342
    • Nemeth, E.1    Ganz, T.2
  • 6
    • 14644436419 scopus 로고    scopus 로고
    • Anemia of inflammation: the hepcidin link
    • Roy C.N., Andrews N.C. Anemia of inflammation: the hepcidin link. Curr Opin Hematol 2005, 12(2):107-111.
    • (2005) Curr Opin Hematol , vol.12 , Issue.2 , pp. 107-111
    • Roy, C.N.1    Andrews, N.C.2
  • 7
    • 85047693999 scopus 로고    scopus 로고
    • Anemia of inflammation: the cytokine-hepcidin link
    • Andrews N.C. Anemia of inflammation: the cytokine-hepcidin link. J Clin Invest 2004, 113(9):1251-1253.
    • (2004) J Clin Invest , vol.113 , Issue.9 , pp. 1251-1253
    • Andrews, N.C.1
  • 8
    • 67349115201 scopus 로고    scopus 로고
    • Iron metabolism in the anemia of chronic disease
    • Weiss G. Iron metabolism in the anemia of chronic disease. Biochim Biophys Acta 2009, 1790(7):682-693.
    • (2009) Biochim Biophys Acta , vol.1790 , Issue.7 , pp. 682-693
    • Weiss, G.1
  • 9
    • 33751175421 scopus 로고    scopus 로고
    • Interleukin-6 induces hepcidin expression through STAT3
    • Wrighting D.M., Andrews N.C. Interleukin-6 induces hepcidin expression through STAT3. Blood 2006, 108(9):3204-3209.
    • (2006) Blood , vol.108 , Issue.9 , pp. 3204-3209
    • Wrighting, D.M.1    Andrews, N.C.2
  • 12
    • 10244265904 scopus 로고    scopus 로고
    • Diferric transferrin regulates transferrin receptor 2 protein stability
    • Johnson M.B., Enns C.A. Diferric transferrin regulates transferrin receptor 2 protein stability. Blood 2004, 104(13):4287-4293.
    • (2004) Blood , vol.104 , Issue.13 , pp. 4287-4293
    • Johnson, M.B.1    Enns, C.A.2
  • 13
    • 10244255021 scopus 로고    scopus 로고
    • Regulation of transferrin receptor 2 protein levels by transferrin
    • Robb A., Wessling-Resnick M. Regulation of transferrin receptor 2 protein levels by transferrin. Blood 2004, 104(13):4294-4299.
    • (2004) Blood , vol.104 , Issue.13 , pp. 4294-4299
    • Robb, A.1    Wessling-Resnick, M.2
  • 14
    • 0032478524 scopus 로고    scopus 로고
    • Crystal structure of the hemochromatosis protein HFE and characterization of its interaction with transferrin receptor
    • Lebron J.A., Bennett M.J., Vaughn D.E., Chirino A.J., Snow P.M., Mintier G.A., et al. Crystal structure of the hemochromatosis protein HFE and characterization of its interaction with transferrin receptor. Cell 1998, 93(1):111-123.
    • (1998) Cell , vol.93 , Issue.1 , pp. 111-123
    • Lebron, J.A.1    Bennett, M.J.2    Vaughn, D.E.3    Chirino, A.J.4    Snow, P.M.5    Mintier, G.A.6
  • 15
    • 33749393565 scopus 로고    scopus 로고
    • Hereditary hemochromatosis protein, HFE, interaction with transferrin receptor 2 suggests a molecular mechanism for mammalian iron sensing
    • Goswami T., Andrews N.C. Hereditary hemochromatosis protein, HFE, interaction with transferrin receptor 2 suggests a molecular mechanism for mammalian iron sensing. J Biol Chem 2006, 281(39):28494-28498.
    • (2006) J Biol Chem , vol.281 , Issue.39 , pp. 28494-28498
    • Goswami, T.1    Andrews, N.C.2
  • 16
    • 60649103774 scopus 로고    scopus 로고
    • Interaction of the hereditary hemochromatosis protein HFE with transferrin receptor 2 is required for transferrin-induced hepcidin expression
    • Gao J., Chen J., Kramer M., Tsukamoto H., Zhang A.S., Enns C.A. Interaction of the hereditary hemochromatosis protein HFE with transferrin receptor 2 is required for transferrin-induced hepcidin expression. Cell Metab 2009, 9(3):217-227.
    • (2009) Cell Metab , vol.9 , Issue.3 , pp. 217-227
    • Gao, J.1    Chen, J.2    Kramer, M.3    Tsukamoto, H.4    Zhang, A.S.5    Enns, C.A.6
  • 17
    • 39649115776 scopus 로고    scopus 로고
    • The transferrin receptor modulates Hfe-dependent regulation of hepcidin expression
    • Schmidt P.J., Toran P.T., Giannetti A.M., Bjorkman P.J., Andrews N.C. The transferrin receptor modulates Hfe-dependent regulation of hepcidin expression. Cell Metab 2008, 7(3):205-214.
    • (2008) Cell Metab , vol.7 , Issue.3 , pp. 205-214
    • Schmidt, P.J.1    Toran, P.T.2    Giannetti, A.M.3    Bjorkman, P.J.4    Andrews, N.C.5
  • 18
    • 66749183353 scopus 로고    scopus 로고
    • Cross-talk between the mitogen activated protein kinase and bone morphogenetic protein/hemojuvelin pathways is required for the induction of hepcidin by holotransferrin in primary mouse hepatocytes
    • Ramey G., Deschemin J.C., Vaulont S. Cross-talk between the mitogen activated protein kinase and bone morphogenetic protein/hemojuvelin pathways is required for the induction of hepcidin by holotransferrin in primary mouse hepatocytes. Haematologica 2009, 94(6):765-772.
    • (2009) Haematologica , vol.94 , Issue.6 , pp. 765-772
    • Ramey, G.1    Deschemin, J.C.2    Vaulont, S.3
  • 19
    • 36649027658 scopus 로고    scopus 로고
    • Soluble hemojuvelin is released by proprotein convertase-mediated cleavage at a conserved polybasic RNRR site
    • Lin L., Nemeth E., Goodnough J.B., Thapa D.R., Gabayan V., Ganz T. Soluble hemojuvelin is released by proprotein convertase-mediated cleavage at a conserved polybasic RNRR site. Blood Cells Mol Dis 2008, 40(1):122-131.
    • (2008) Blood Cells Mol Dis , vol.40 , Issue.1 , pp. 122-131
    • Lin, L.1    Nemeth, E.2    Goodnough, J.B.3    Thapa, D.R.4    Gabayan, V.5    Ganz, T.6
  • 20
    • 34447137331 scopus 로고    scopus 로고
    • Modulation of bone morphogenetic protein signaling in vivo regulates systemic iron balance
    • Babitt J.L., Huang F.W., Xia Y., Sidis Y., Andrews N.C., Lin H.Y. Modulation of bone morphogenetic protein signaling in vivo regulates systemic iron balance. J Clin Invest 2007, 117(7):1933-1939.
    • (2007) J Clin Invest , vol.117 , Issue.7 , pp. 1933-1939
    • Babitt, J.L.1    Huang, F.W.2    Xia, Y.3    Sidis, Y.4    Andrews, N.C.5    Lin, H.Y.6
  • 21
    • 33745898241 scopus 로고    scopus 로고
    • Bone morphogenetic proteins 2, 4, and 9 stimulate murine hepcidin 1 expression independently of Hfe, transferrin receptor 2 (Tfr2), and IL-6
    • Truksa J., Peng H., Lee P., Beutler E. Bone morphogenetic proteins 2, 4, and 9 stimulate murine hepcidin 1 expression independently of Hfe, transferrin receptor 2 (Tfr2), and IL-6. Proc Natl Acad Sci U S A 2006, 103(27):10289-10293.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , Issue.27 , pp. 10289-10293
    • Truksa, J.1    Peng, H.2    Lee, P.3    Beutler, E.4
  • 22
    • 63449103712 scopus 로고    scopus 로고
    • BMP6 is a key endogenous regulator of hepcidin expression and iron metabolism
    • Andriopoulos B., Corradini E., Xia Y., Faasse S.A., Chen S., Grgurevic L., et al. BMP6 is a key endogenous regulator of hepcidin expression and iron metabolism. Nat Genet 2009, 41(4):482-487.
    • (2009) Nat Genet , vol.41 , Issue.4 , pp. 482-487
    • Andriopoulos, B.1    Corradini, E.2    Xia, Y.3    Faasse, S.A.4    Chen, S.5    Grgurevic, L.6
  • 23
    • 51649096725 scopus 로고    scopus 로고
    • Iron regulates phosphorylation of Smad1/5/8 and gene expression of Bmp6, Smad7, Id1, and Atoh8 in the mouse liver
    • Kautz L., Meynard D., Monnier A., Darnaud V., Bouvet R., Wang R.H., et al. Iron regulates phosphorylation of Smad1/5/8 and gene expression of Bmp6, Smad7, Id1, and Atoh8 in the mouse liver. Blood 2008, 112(4):1503-1509.
    • (2008) Blood , vol.112 , Issue.4 , pp. 1503-1509
    • Kautz, L.1    Meynard, D.2    Monnier, A.3    Darnaud, V.4    Bouvet, R.5    Wang, R.H.6
  • 25
    • 44449177930 scopus 로고    scopus 로고
    • The serine protease TMPRSS6 is required to sense iron deficiency
    • Du X., She E., Gelbart T., Truksa J., Lee P., Xia Y., et al. The serine protease TMPRSS6 is required to sense iron deficiency. Science 2008, 320(5879):1088-1092.
    • (2008) Science , vol.320 , Issue.5879 , pp. 1088-1092
    • Du, X.1    She, E.2    Gelbart, T.3    Truksa, J.4    Lee, P.5    Xia, Y.6
  • 26
    • 56449096622 scopus 로고    scopus 로고
    • The serine protease matriptase-2 (TMPRSS6) inhibits hepcidin activation by cleaving membrane hemojuvelin
    • Silvestri L., Pagani A., Nai A., De Domenico I., Kaplan J., Camaschella C. The serine protease matriptase-2 (TMPRSS6) inhibits hepcidin activation by cleaving membrane hemojuvelin. Cell Metab 2008, 8(6):502-511.
    • (2008) Cell Metab , vol.8 , Issue.6 , pp. 502-511
    • Silvestri, L.1    Pagani, A.2    Nai, A.3    De Domenico, I.4    Kaplan, J.5    Camaschella, C.6
  • 28
    • 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(11):939-950.
    • (2005) Dev Comp Immunol , vol.29 , Issue.11 , pp. 939-950
    • Bao, B.1    Peatman, E.2    Li, P.3    He, C.4    Liu, Z.5
  • 29
    • 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., Vazquez-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(12):1156-1167.
    • (2006) Dev Comp Immunol , vol.30 , Issue.12 , pp. 1156-1167
    • Rodrigues, P.N.1    Vazquez-Dorado, S.2    Neves, J.V.3    Wilson, J.M.4
  • 30
    • 20144376234 scopus 로고    scopus 로고
    • Characterisation and expression analysis of an interleukin 6 homologue in the Japanese pufferfish, Fugu rubripes
    • Bird S., Zou J., Savan R., Kono T., Sakai M., Woo J., et al. Characterisation and expression analysis of an interleukin 6 homologue in the Japanese pufferfish, Fugu rubripes. Dev Comp Immunol 2005, 29(9):775-789.
    • (2005) Dev Comp Immunol , vol.29 , Issue.9 , pp. 775-789
    • Bird, S.1    Zou, J.2    Savan, R.3    Kono, T.4    Sakai, M.5    Woo, J.6
  • 31
    • 33751313845 scopus 로고    scopus 로고
    • Cloning and expression analysis of an IL-6 homolog in rainbow trout (Oncorhynchus mykiss)
    • Iliev D.B., Castellana B., Mackenzie S., Planas J.V., Goetz F.W. Cloning and expression analysis of an IL-6 homolog in rainbow trout (Oncorhynchus mykiss). Mol Immunol 2007, 44(7):1803-1807.
    • (2007) Mol Immunol , vol.44 , Issue.7 , pp. 1803-1807
    • Iliev, D.B.1    Castellana, B.2    Mackenzie, S.3    Planas, J.V.4    Goetz, F.W.5
  • 32
    • 34247502188 scopus 로고    scopus 로고
    • Molecular cloning and characterisation of the flounder (Paralichthys olivaceus) interleukin-6 gene
    • Nam B.H., Byon J.Y., Kim Y.O., Park E.M., Cho Y.C., Cheong J. Molecular cloning and characterisation of the flounder (Paralichthys olivaceus) interleukin-6 gene. Fish Shellfish Immunol 2007, 23(1):231-236.
    • (2007) Fish Shellfish Immunol , vol.23 , Issue.1 , pp. 231-236
    • Nam, B.H.1    Byon, J.Y.2    Kim, Y.O.3    Park, E.M.4    Cho, Y.C.5    Cheong, J.6
  • 33
    • 34249287368 scopus 로고    scopus 로고
    • Vibrio anguillarum evades the immune response of the bony fish sea bass (Dicentrarchus labrax L.) through the inhibition of leukocyte respiratory burst and down-regulation of apoptotic caspases
    • Sepulcre M.P., Sarropoulou E., Kotoulas G., Meseguer J., Mulero V. Vibrio anguillarum evades the immune response of the bony fish sea bass (Dicentrarchus labrax L.) through the inhibition of leukocyte respiratory burst and down-regulation of apoptotic caspases. Mol Immunol 2007, 44(15):3751-3757.
    • (2007) Mol Immunol , vol.44 , Issue.15 , pp. 3751-3757
    • Sepulcre, M.P.1    Sarropoulou, E.2    Kotoulas, G.3    Meseguer, J.4    Mulero, V.5
  • 34
    • 67650506906 scopus 로고    scopus 로고
    • The JAK and STAT family members of the mandarin fish Siniperca chuatsi: molecular cloning, tissues distribution and immunobiological activity
    • Guo C.J., Zhang Y.F., Yang L.S., Yang X.B., Wu Y.Y., Liu D., et al. The JAK and STAT family members of the mandarin fish Siniperca chuatsi: molecular cloning, tissues distribution and immunobiological activity. Fish Shellfish Immunol 2009, 27(2):349-359.
    • (2009) Fish Shellfish Immunol , vol.27 , Issue.2 , pp. 349-359
    • Guo, C.J.1    Zhang, Y.F.2    Yang, L.S.3    Yang, X.B.4    Wu, Y.Y.5    Liu, D.6
  • 35
    • 78650703667 scopus 로고    scopus 로고
    • Signal transducer and activator of transcription 3 (STAT3) homologue in turbot (Scophthalmus maximus): molecular characterization and expression analysis
    • Wang N., Yang C.G., Sun Z.Z., Wang X.L., Chen S.L. Signal transducer and activator of transcription 3 (STAT3) homologue in turbot (Scophthalmus maximus): molecular characterization and expression analysis. Fish Shellfish Immunol 2011, 30(1):255-262.
    • (2011) Fish Shellfish Immunol , vol.30 , Issue.1 , pp. 255-262
    • Wang, N.1    Yang, C.G.2    Sun, Z.Z.3    Wang, X.L.4    Chen, S.L.5
  • 36
    • 0030661703 scopus 로고    scopus 로고
    • Cloning and expression of three members of the zebrafish Bmp family: Bmp2a, Bmp2b and Bmp4
    • Martinez-Barbera J.P., Toresson H., Da Rocha S., Krauss S. Cloning and expression of three members of the zebrafish Bmp family: Bmp2a, Bmp2b and Bmp4. Gene 1997, 198(1-2):53-59.
    • (1997) Gene , vol.198 , Issue.1-2 , pp. 53-59
    • Martinez-Barbera, J.P.1    Toresson, H.2    Da Rocha, S.3    Krauss, S.4
  • 37
    • 79251610627 scopus 로고    scopus 로고
    • BMP signaling modulates hepcidin expression in zebrafish embryos independent of hemojuvelin
    • Gibert Y., Lattanzi V.J., Zhen A.W., Vedder L., Brunet F., Faasse S.A., et al. BMP signaling modulates hepcidin expression in zebrafish embryos independent of hemojuvelin. PLoS One 2011, 6(1):e14553.
    • (2011) PLoS One , vol.6 , Issue.1
    • Gibert, Y.1    Lattanzi, V.J.2    Zhen, A.W.3    Vedder, L.4    Brunet, F.5    Faasse, S.A.6
  • 38
    • 0344549451 scopus 로고    scopus 로고
    • Characterization of zebrafish smad1, smad2 and smad5: the amino-terminus of smad1 and smad5 is required for specific function in the embryo
    • Muller F., Blader P., Rastegar S., Fischer N., Knochel W., Strahle U. Characterization of zebrafish smad1, smad2 and smad5: the amino-terminus of smad1 and smad5 is required for specific function in the embryo. Mech Dev 1999, 88(1):73-88.
    • (1999) Mech Dev , vol.88 , Issue.1 , pp. 73-88
    • Muller, F.1    Blader, P.2    Rastegar, S.3    Fischer, N.4    Knochel, W.5    Strahle, U.6
  • 39
    • 13544257333 scopus 로고    scopus 로고
    • Cloning of Smad2, Smad3, Smad4, and Smad7 from the goldfish pituitary and evidence for their involvement in activin regulation of goldfish FSHbeta promoter activity
    • Lau M.T., Ge W. Cloning of Smad2, Smad3, Smad4, and Smad7 from the goldfish pituitary and evidence for their involvement in activin regulation of goldfish FSHbeta promoter activity. Gen Comp Endocrinol 2005, 141(1):22-38.
    • (2005) Gen Comp Endocrinol , vol.141 , Issue.1 , pp. 22-38
    • Lau, M.T.1    Ge, W.2
  • 40
    • 0024297354 scopus 로고
    • Multiple sequence alignment with hierarchical clustering
    • Corpet F. Multiple sequence alignment with hierarchical clustering. Nucleic Acids Res 1988, 16(22):10881-10890.
    • (1988) Nucleic Acids Res , vol.16 , Issue.22 , pp. 10881-10890
    • Corpet, F.1
  • 41
    • 5344238189 scopus 로고    scopus 로고
    • A model for acute iron overload in sea bass (Dicentrarchus labrax L.)
    • Rodrigues P.N., Pereira F.A. A model for acute iron overload in sea bass (Dicentrarchus labrax L.). Lab Anim 2004, 38(4):418-424.
    • (2004) Lab Anim , vol.38 , Issue.4 , pp. 418-424
    • Rodrigues, P.N.1    Pereira, F.A.2
  • 42
    • 0002413872 scopus 로고
    • Tissue iron stores
    • Churchill Livingston Press, New York, J.D. Cook (Ed.)
    • Torrence J.D., Bothwell T.H. Tissue iron stores. Methods in haematology 1980, 104-109. Churchill Livingston Press, New York. J.D. Cook (Ed.).
    • (1980) Methods in haematology , pp. 104-109
    • Torrence, J.D.1    Bothwell, T.H.2
  • 44
    • 59449104943 scopus 로고    scopus 로고
    • Interacting signals in the control of hepcidin expression
    • Darshan D., Anderson G.J. Interacting signals in the control of hepcidin expression. Biometals 2009, 22(1):77-87.
    • (2009) Biometals , vol.22 , Issue.1 , pp. 77-87
    • Darshan, D.1    Anderson, G.J.2
  • 45
    • 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, 276(11):7811-7819.
    • (2001) J Biol Chem , vol.276 , Issue.11 , pp. 7811-7819
    • Pigeon, C.1    Ilyin, G.2    Courselaud, B.3    Leroyer, P.4    Turlin, B.5    Brissot, P.6
  • 46
    • 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., Jorgensen T.O. Identification, cloning and expression analysis of a hepcidin cDNA of the Atlantic cod (Gadus morhua L.). Fish Shellfish Immunol 2008, 25(3):298-310.
    • (2008) Fish Shellfish Immunol , vol.25 , Issue.3 , pp. 298-310
    • Solstad, T.1    Larsen, A.N.2    Seppola, M.3    Jorgensen, T.O.4
  • 47
    • 1642386686 scopus 로고    scopus 로고
    • Organization and expression analysis of the zebrafish hepcidin gene, an antimicrobial peptide gene conserved among vertebrates
    • Shike H., Shimizu C., Lauth X., Burns J.C. Organization and expression analysis of the zebrafish hepcidin gene, an antimicrobial peptide gene conserved among vertebrates. Dev Comp Immunol 2004, 28(7-8):747-754.
    • (2004) Dev Comp Immunol , vol.28 , Issue.7-8 , pp. 747-754
    • Shike, H.1    Shimizu, C.2    Lauth, X.3    Burns, J.C.4
  • 48
    • 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(6-7):589-601.
    • (2003) Dev Comp Immunol , vol.27 , Issue.6-7 , pp. 589-601
    • Douglas, S.E.1    Gallant, J.W.2    Liebscher, R.S.3    Dacanay, A.4    Tsoi, S.C.5
  • 49
    • 7944223085 scopus 로고    scopus 로고
    • Comparative blood chemistry and histopathology of tilapia infected with Vibrio vulnificus or Streptococcus iniae or exposed to carbon tetrachloride, gentamicin, or copper sulfate
    • Chen C.-Y., Wooster G.A., Bowser P.R. Comparative blood chemistry and histopathology of tilapia infected with Vibrio vulnificus or Streptococcus iniae or exposed to carbon tetrachloride, gentamicin, or copper sulfate. Aquaculture 2004, 239(1-4):421-443.
    • (2004) Aquaculture , vol.239 , Issue.1-4 , pp. 421-443
    • Chen, C.-Y.1    Wooster, G.A.2    Bowser, P.R.3
  • 50
    • 64149131921 scopus 로고    scopus 로고
    • Transferrin and ferritin response to bacterial infection: the role of the liver and brain in fish
    • Neves J.V., Wilson J.M., Rodrigues P.N. Transferrin and ferritin response to bacterial infection: the role of the liver and brain in fish. Dev Comp Immunol 2009, 33(7):848-857.
    • (2009) Dev Comp Immunol , vol.33 , Issue.7 , pp. 848-857
    • Neves, J.V.1    Wilson, J.M.2    Rodrigues, P.N.3
  • 51
    • 43049132128 scopus 로고    scopus 로고
    • A bone morphogenetic protein (BMP)-responsive element in the hepcidin promoter controls HFE2-mediated hepatic hepcidin expression and its response to IL-6 in cultured cells
    • Verga Falzacappa M.V., Casanovas G., Hentze M.W., Muckenthaler M.U. A bone morphogenetic protein (BMP)-responsive element in the hepcidin promoter controls HFE2-mediated hepatic hepcidin expression and its response to IL-6 in cultured cells. J Mol Med 2008, 86(5):531-540.
    • (2008) J Mol Med , vol.86 , Issue.5 , pp. 531-540
    • Verga Falzacappa, M.V.1    Casanovas, G.2    Hentze, M.W.3    Muckenthaler, M.U.4
  • 52
    • 65349173063 scopus 로고    scopus 로고
    • Contribution of STAT3 and SMAD4 pathways to the regulation of hepcidin by opposing stimuli
    • Huang H., Constante M., Layoun A., Santos M.M. Contribution of STAT3 and SMAD4 pathways to the regulation of hepcidin by opposing stimuli. Blood 2009, 113(15):3593-3599.
    • (2009) Blood , vol.113 , Issue.15 , pp. 3593-3599
    • Huang, H.1    Constante, M.2    Layoun, A.3    Santos, M.M.4
  • 53
    • 33947583828 scopus 로고    scopus 로고
    • Molecular cloning and expression analysis of a hepcidin antimicrobial peptide gene from turbot (Scophthalmus maximus)
    • Chen S.L., Li W., Meng L., Sha Z.X., Wang Z.J., Ren G.C. Molecular cloning and expression analysis of a hepcidin antimicrobial peptide gene from turbot (Scophthalmus maximus). Fish Shellfish Immunol 2007, 22(3):172-181.
    • (2007) Fish Shellfish Immunol , vol.22 , Issue.3 , pp. 172-181
    • Chen, S.L.1    Li, W.2    Meng, L.3    Sha, Z.X.4    Wang, Z.J.5    Ren, G.C.6
  • 54
    • 62749144992 scopus 로고    scopus 로고
    • Cloning and expression of a hepcidin gene from a marine fish (Pseudosciaena crocea) and the antimicrobial activity of its synthetic peptide
    • Wang K.J., Cai J.J., Cai L., Qu H.D., Yang M., Zhang M. Cloning and expression of a hepcidin gene from a marine fish (Pseudosciaena crocea) and the antimicrobial activity of its synthetic peptide. Peptides 2009, 30(4):638-646.
    • (2009) Peptides , vol.30 , Issue.4 , pp. 638-646
    • Wang, K.J.1    Cai, J.J.2    Cai, L.3    Qu, H.D.4    Yang, M.5    Zhang, M.6
  • 55
    • 0036791486 scopus 로고    scopus 로고
    • The gene encoding the iron regulatory peptide hepcidin is regulated by anemia, hypoxia, and inflammation
    • Nicolas G., Chauvet C., Viatte L., Danan J.L., Bigard X., Devaux I., et al. The gene encoding the iron regulatory peptide hepcidin is regulated by anemia, hypoxia, and inflammation. J Clin Invest 2002, 110(7):1037-1044.
    • (2002) J Clin Invest , vol.110 , Issue.7 , pp. 1037-1044
    • Nicolas, G.1    Chauvet, C.2    Viatte, L.3    Danan, J.L.4    Bigard, X.5    Devaux, I.6
  • 56
    • 0031009405 scopus 로고    scopus 로고
    • High affinity iron-uptake systems in Vibrio damsela: role in the acquisition of iron from transferrin
    • Fouz B., Biosca E.G., Amaro C. High affinity iron-uptake systems in Vibrio damsela: role in the acquisition of iron from transferrin. J Appl Microbiol 1997, 82(2):157-167.
    • (1997) J Appl Microbiol , vol.82 , Issue.2 , pp. 157-167
    • Fouz, B.1    Biosca, E.G.2    Amaro, C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.