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Volumn 2, Issue 12, 2004, Pages 946-953

Iron and microbial infection

Author keywords

[No Author keywords available]

Indexed keywords

IRON; NITROGEN; OXYGEN;

EID: 9444246510     PISSN: 17401526     EISSN: None     Source Type: Journal    
DOI: 10.1038/nrmicro1046     Document Type: Review
Times cited : (770)

References (73)
  • 1
    • 2042546096 scopus 로고    scopus 로고
    • Balancing acts: Molecular control of mammalian iron metabolism
    • Hentze, M. W., Muckenthaler, M. U. & Andrews, N. C. Balancing acts: molecular control of mammalian iron metabolism. Cell 117 285-297 (2004).
    • (2004) Cell , vol.117 , pp. 285-297
    • Hentze, M.W.1    Muckenthaler, M.U.2    Andrews, N.C.3
  • 2
    • 0037184526 scopus 로고    scopus 로고
    • Mechanisms of cellular iron acquisition: Another iron in the fire
    • Kaplan, J. Mechanisms of cellular iron acquisition: another iron in the fire. Cell 111, 603-606 (2002).
    • (2002) Cell , vol.111 , pp. 603-606
    • Kaplan, J.1
  • 4
    • 0034680828 scopus 로고    scopus 로고
    • Nramp 2 (DCT1 /DMT1) expressed at the plasma membrane transports iron and other divalent cations into a calcein-accessible cytoplasmic pool
    • Picard, V., Govoni, G., Jabado, N. & Gros, P. Nramp 2 (DCT1 /DMT1) expressed at the plasma membrane transports iron and other divalent cations into a calcein-accessible cytoplasmic pool. J. Biol. Chem. 275, 35738-35745 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 35738-35745
    • Picard, V.1    Govoni, G.2    Jabado, N.3    Gros, P.4
  • 5
    • 0034677467 scopus 로고    scopus 로고
    • Positional cloning of zebrafish ferroportin1 identifies a conserved vertebrate iron exporter
    • Donovan, A. et al. Positional cloning of zebrafish ferroportin1 identifies a conserved vertebrate iron exporter. Nature 403, 776-781 (2000).
    • (2000) Nature , vol.403 , pp. 776-781
    • Donovan, A.1
  • 6
    • 0041672570 scopus 로고    scopus 로고
    • Hepcidin, a key regulator of iron metabolism and mediator of anemia of inflammation
    • Ganz, T. Hepcidin, a key regulator of iron metabolism and mediator of anemia of inflammation. Blood 102, 783-788 (2003).
    • (2003) Blood , vol.102 , pp. 783-788
    • Ganz, T.1
  • 7
    • 0033103978 scopus 로고    scopus 로고
    • The iron transport protein NRAMP2 is an integral membrane glycoprotein that colocalizes with transferrin in recycling endosomes
    • Gruenheid, S. et al. The iron transport protein NRAMP2 is an integral membrane glycoprotein that colocalizes with transferrin in recycling endosomes. J. Exp. Med. 189, 831-841 (1999).
    • (1999) J. Exp. Med. , vol.189 , pp. 831-841
    • Gruenheid, S.1
  • 8
    • 6344237322 scopus 로고    scopus 로고
    • Recent advances in understanding haemochromatosis: A transition state
    • Robson, K. J. et al. Recent advances in understanding haemochromatosis: a transition state. J. Med. Genet. 41, 721-730 (2004).
    • (2004) J. Med. Genet. , vol.41 , pp. 721-730
    • Robson, K.J.1
  • 9
    • 2542560427 scopus 로고    scopus 로고
    • Hereditary hemochromatosis - A new look at an old disease
    • Pietrangelo, A. Hereditary hemochromatosis - a new look at an old disease. N. Engl. J. Med. 350, 2383-2397 (2004).
    • (2004) N. Engl. J. Med. , vol.350 , pp. 2383-2397
    • Pietrangelo, A.1
  • 11
    • 0034610781 scopus 로고    scopus 로고
    • Crystal structure of the hereditary haemochromatosis protein HFE complexed with transferrin receptor
    • Bennett, M. J., Lebron, J. A. & Bjorkman, P. J. Crystal structure of the hereditary haemochromatosis protein HFE complexed with transferrin receptor. Nature 403, 46-53 (2000).
    • (2000) Nature , vol.403 , pp. 46-53
    • Bennett, M.J.1    Lebron, J.A.2    Bjorkman, P.J.3
  • 12
    • 0035009246 scopus 로고    scopus 로고
    • Pumping iron: The strange partnership of the hemochromatosis protein, a class I MHC homolog, with the transferrin receptor
    • Enns, C. A. Pumping iron: the strange partnership of the hemochromatosis protein, a class I MHC homolog, with the transferrin receptor. Traffic 2, 167-174 (2001).
    • (2001) Traffic , vol.2 , pp. 167-174
    • Enns, C.A.1
  • 13
    • 0037847496 scopus 로고    scopus 로고
    • Constitutive hepcidin expression prevents iron overload in a mouse model of hemochromatosis
    • Nicolas, G. et al. Constitutive hepcidin expression prevents iron overload in a mouse model of hemochromatosis. Nature Genet. 34, 97-101 (2003).
    • (2003) Nature Genet. , vol.34 , pp. 97-101
    • Nicolas, G.1
  • 14
    • 0032779319 scopus 로고    scopus 로고
    • The Nramp1 protein and its role in resistance to infection and macrophage function
    • Canonne-Hergaux, F., Gruenheid, S., Govoni, G. & Gros, P. The Nramp1 protein and its role in resistance to infection and macrophage function. Proc. Assoc. Am. Physicians 111, 283-289 (1999).
    • (1999) Proc. Assoc. Am. Physicians , vol.111 , pp. 283-289
    • Canonne-Hergaux, F.1    Gruenheid, S.2    Govoni, G.3    Gros, P.4
  • 15
    • 0031850526 scopus 로고    scopus 로고
    • Host resistance to intracellular infection: Mutation of natural resistance-associated macrophage protein 1 (Nramp1) impairs phagosomal acidification
    • Hackam, D J. et al. Host resistance to intracellular infection: mutation of natural resistance-associated macrophage protein 1 (Nramp1) impairs phagosomal acidification. J. Exp. Med. 188, 351-364 (1998).
    • (1998) J. Exp. Med. , vol.188 , pp. 351-364
    • Hackam, D.J.1
  • 16
    • 0038284820 scopus 로고    scopus 로고
    • Iron chelators modulate the fusogenic properties of Salmonella-containing phagosomes
    • Jabado, N., Cuellar-Mata, P., Grinstein, S. & Gros, P. Iron chelators modulate the fusogenic properties of Salmonella containing phagosomes. Proc. Natl Acad. Sci. USA 100, 6127-6132 (2003).
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 6127-6132
    • Jabado, N.1    Cuellar-Mata, P.2    Grinstein, S.3    Gros, P.4
  • 17
    • 0036533562 scopus 로고    scopus 로고
    • Iron chelation via deferoxamine exacerbates experimental salmonellosis via inhibition of the nicotinamide adenine dinucleotide phosphate oxidase-dependent respiratory burst
    • Collins, H. L., Kaufmann, S. H. E. & Schaible, U. E. Iron chelation via deferoxamine exacerbates experimental salmonellosis via inhibition of the nicotinamide adenine dinucleotide phosphate oxidase-dependent respiratory burst. J. Immunol. 168, 3458-3463 (2002).
    • (2002) J. Immunol. , vol.168 , pp. 3458-3463
    • Collins, H.L.1    Kaufmann, S.H.E.2    Schaible, U.E.3
  • 18
    • 0035808787 scopus 로고    scopus 로고
    • The relative importance of T cell subsets in immunity and immunopathology of airborne Mycobacterium tuberculosis infection in mice
    • Mogues, T., Goodrich, M. E., Ryan, L., LaCourse, R. & North, R. J. The relative importance of T cell subsets in immunity and immunopathology of airborne Mycobacterium tuberculosis infection in mice. J. Exp. Med. 193, 271-80 (2001)
    • (2001) J. Exp. Med. , vol.193 , pp. 271-280
    • Mogues, T.1    Goodrich, M.E.2    Ryan, L.3    LaCourse, R.4    North, R.J.5
  • 19
    • 0034595617 scopus 로고    scopus 로고
    • Lack of a role for iron in the Lyme disease pathogen
    • Posey, J. E. & Gherardini, F. C. Lack of a role for iron in the Lyme disease pathogen. Science 288, 1651-1653 (2000).
    • (2000) Science , vol.288 , pp. 1651-1653
    • Posey, J.E.1    Gherardini, F.C.2
  • 20
    • 0018102319 scopus 로고
    • Iron and infection
    • Weinberg, E. D. Iron and infection. Microbiol. Rev. 42, 45-66 (1978)
    • (1978) Microbiol. Rev. , vol.42 , pp. 45-66
    • Weinberg, E.D.1
  • 21
    • 0033759220 scopus 로고    scopus 로고
    • Iron metabolism in pathogenic bacteria
    • Ratledge, C. & Dover, L. G. Iron metabolism in pathogenic bacteria. Annu. Rev. Microbiol. 54, 881-941 (2000).
    • (2000) Annu. Rev. Microbiol. , vol.54 , pp. 881-941
    • Ratledge, C.1    Dover, L.G.2
  • 22
    • 0347722524 scopus 로고    scopus 로고
    • Iron, mycobacteria and tuberculosis
    • Ratledge, C. Iron, mycobacteria and tuberculosis. Tuberculosis (Edinb.) 84, 110-130 (2004).
    • (2004) Tuberculosis (Edinb.) , vol.84 , pp. 110-130
    • Ratledge, C.1
  • 23
    • 0036754957 scopus 로고    scopus 로고
    • Iron acquisition by Gram-positive bacterial pathogens
    • Brown, J. S. & Holden, D. W. Iron acquisition by Gram-positive bacterial pathogens. Microbes Infect. 4, 1149-1156 (2002).
    • (2002) Microbes Infect. , vol.4 , pp. 1149-1156
    • Brown, J.S.1    Holden, D.W.2
  • 24
    • 0031981543 scopus 로고    scopus 로고
    • Metal ion homeostasis and intracellular parasitism
    • Agranoff, D. D. & Krishna, S. Metal ion homeostasis and intracellular parasitism. Mol. Microbiol. 28, 403-412 (1998).
    • (1998) Mol. Microbiol. , vol.28 , pp. 403-412
    • Agranoff, D.D.1    Krishna, S.2
  • 25
    • 0037344575 scopus 로고    scopus 로고
    • Mechanisms of iron regulation in mycobacteria: Role in physiology and virulence
    • Rodriguez, G. M. & Smith, I. Mechanisms of iron regulation in mycobacteria: role in physiology and virulence. Mol. Microbiol. 47, 1485-1494 (2003).
    • (2003) Mol. Microbiol. , vol.47 , pp. 1485-1494
    • Rodriguez, G.M.1    Smith, I.2
  • 26
    • 0033607166 scopus 로고    scopus 로고
    • Attenuation of virulence in Mycobacterium tuberculosis expressing a constitutively active iron repressor
    • Manabe, Y. C., Saviola, B. J., Sun, L., Murphy, J. R. & Bishai, W. R. Attenuation of virulence in Mycobacterium tuberculosis expressing a constitutively active iron repressor. Proc. Natl Acad. Sci. USA 96, 12844-12848 (1999).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 12844-12848
    • Manabe, Y.C.1    Saviola, B.J.2    Sun, L.3    Murphy, J.R.4    Bishai, W.R.5
  • 27
    • 0035169902 scopus 로고    scopus 로고
    • The Mycobacterium tuberculosis IdeR is a dual functional regulator that controls transcription of genes involved in iron acquisition, iron storage and survival in macrophages
    • Gold, B., Rodriguez, G. M., Marras, S. A., Pentecost, M. & Smith, I. The Mycobacterium tuberculosis IdeR is a dual functional regulator that controls transcription of genes involved in iron acquisition, iron storage and survival in macrophages. Mol. Microbiol. 42, 851-865 (2001).
    • (2001) Mol. Microbiol. , vol.42 , pp. 851-865
    • Gold, B.1    Rodriguez, G.M.2    Marras, S.A.3    Pentecost, M.4    Smith, I.5
  • 28
    • 4644310922 scopus 로고    scopus 로고
    • Iron-source preference of Staphylococcus aureus infections
    • Skaar, E. P., Humayun, M., Bae, T., DeBord, K. L. & Schneewind, O. Iron-source preference of Staphylococcus aureus infections. Science 305, 1626-1628 (2004).
    • (2004) Science , vol.305 , pp. 1626-1628
    • Skaar, E.P.1    Humayun, M.2    Bae, T.3    DeBord, K.L.4    Schneewind, O.5
  • 30
    • 0025953808 scopus 로고
    • Lactoferrin inhibits or promotes Legionella pneumophila intracellular multiplication in nonactivated and interferon ã-activated human monocytes depending upon its degree of iron saturation. Iron-lactoferrin and nonphysiologic iron chelates reverse monocyte activation against Legionella pneumophila
    • Byrd, T. F. & Horwitz, M. A. Lactoferrin inhibits or promotes Legionella pneumophila intracellular multiplication in nonactivated and interferon ã-activated human monocytes depending upon its degree of iron saturation. Iron-lactoferrin and nonphysiologic iron chelates reverse monocyte activation against Legionella pneumophila. J. Clin. Invest. 88, 1103-1112 (1991).
    • (1991) J. Clin. Invest. , vol.88 , pp. 1103-1112
    • Byrd, T.F.1    Horwitz, M.A.2
  • 31
    • 0033806469 scopus 로고    scopus 로고
    • Gallium disrupts iron metabolism of mycobacteria residing within human macrophages
    • Olakanmi, O., Britigan, B. E. & Schlesinger, L. S. Gallium disrupts iron metabolism of mycobacteria residing within human macrophages. Infect. Immun. 68, 5619-5627 (2000).
    • (2000) Infect. Immun. , vol.68 , pp. 5619-5627
    • Olakanmi, O.1    Britigan, B.E.2    Schlesinger, L.S.3
  • 32
    • 0037011071 scopus 로고    scopus 로고
    • Correction of the iron overload defect in β-2-microglobulin knockout mice by lactoferrin abolishes their increased susceptibility to tuberculosis
    • Schaible, U. E., Collins, H. L., Priem, F. & Kaufmann, S. H. E. Correction of the iron overload defect in β-2-microglobulin knockout mice by lactoferrin abolishes their increased susceptibility to tuberculosis. J. Exp. Med. 196, 1507-1513 (2002).
    • (2002) J. Exp. Med. , vol.196 , pp. 1507-1513
    • Schaible, U.E.1    Collins, H.L.2    Priem, F.3    Kaufmann, S.H.E.4
  • 34
    • 0033492480 scopus 로고    scopus 로고
    • Confrontation between intracellular bacteria and the immune system
    • Schaible, U., Collins, H. & Kaufmann, S. H. E. Confrontation between intracellular bacteria and the immune system. Adv. Immunol. 71, 267-377 (1999).
    • (1999) Adv. Immunol. , vol.71 , pp. 267-377
    • Schaible, U.1    Collins, H.2    Kaufmann, S.H.E.3
  • 35
    • 0037147340 scopus 로고    scopus 로고
    • Intraphagosomal Mycobacterium tuberculosis acquires iron from both extracellular transferrin and intracellular iron pools. Impact of interferon-ã and hemochromatosis
    • Olakanmi, O., Schlesinger, L. S., Ahmed, A. & Britigan, B. E. Intraphagosomal Mycobacterium tuberculosis acquires iron from both extracellular transferrin and intracellular iron pools. Impact of interferon-ã and hemochromatosis. J. Biol. Chem. 277, 49727-49734 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 49727-49734
    • Olakanmi, O.1    Schlesinger, L.S.2    Ahmed, A.3    Britigan, B.E.4
  • 36
    • 0029830548 scopus 로고    scopus 로고
    • Specific binding of the Listeria monocytogenes transcriptional regulator PrfA to target sequences requires additional factor(s) and is influenced by iron
    • Bockmann, R., Dickneite, C., Middendorf, B., Goebel, W. & Sokolovic, Z. Specific binding of the Listeria monocytogenes transcriptional regulator PrfA to target sequences requires additional factor(s) and is influenced by iron. Mol. Microbiol. 22, 643-653 (1996).
    • (1996) Mol. Microbiol. , vol.22 , pp. 643-653
    • Bockmann, R.1    Dickneite, C.2    Middendorf, B.3    Goebel, W.4    Sokolovic, Z.5
  • 37
    • 0029115569 scopus 로고
    • Reduction of exogenous ferric iron by a surface-associated ferric reductase of Listeria spp
    • Deneer, H. G, Healey, V. & Boychuk, I. Reduction of exogenous ferric iron by a surface-associated ferric reductase of Listeria spp. Microbiology 141, 1985-1992 (1995).
    • (1995) Microbiology , vol.141 , pp. 1985-1992
    • Deneer, H.G.1    Healey, V.2    Boychuk, I.3
  • 38
    • 3843101698 scopus 로고    scopus 로고
    • Neisseria meningitidis accelerates ferritin degradation in host epithelial cells to yield an essential iron source
    • Larson, J. A., Howie, H. L. & So, M. Neisseria meningitidis accelerates ferritin degradation in host epithelial cells to yield an essential iron source. Mol. Microbiol. 53, 807-820 (2004).
    • (2004) Mol. Microbiol. , vol.53 , pp. 807-820
    • Larson, J.A.1    Howie, H.L.2    So, M.3
  • 39
    • 0031914958 scopus 로고    scopus 로고
    • Cytokine activation leads to acidification and increases maturation of Mycobacterium avium-containing phagosomes in murine macrophages
    • Schaible, U. E., Sturgill-Koszycki, S., Schlesinger, P. H. & Russell, D. G. Cytokine activation leads to acidification and increases maturation of Mycobacterium avium-containing phagosomes in murine macrophages. J. Immunol. 160, 1290-1296 (1998).
    • (1998) J. Immunol. , vol.160 , pp. 1290-1296
    • Schaible, U.E.1    Sturgill-Koszycki, S.2    Schlesinger, P.H.3    Russell, D.G.4
  • 40
    • 0027476872 scopus 로고
    • Regulation of transferrin receptor expression and ferritin content in human mononuclear phagocytes. Coordinate upregulation by iron transferrin and downregulation by interferon γ
    • Byrd, T. F. & Horwitz, M. A. Regulation of transferrin receptor expression and ferritin content in human mononuclear phagocytes. Coordinate upregulation by iron transferrin and downregulation by interferon γ. J. Clin. Invest. 91, 969-976 (1993).
    • (1993) J. Clin. Invest. , vol.91 , pp. 969-976
    • Byrd, T.F.1    Horwitz, M.A.2
  • 41
    • 10744228285 scopus 로고    scopus 로고
    • Differential expression of iron-, carbon-, and oxygen-responsive mycobacterial genes in the lungs of chronically infected mice and tuberculosis patients
    • Timm, J. et al. Differential expression of iron-, carbon-, and oxygen-responsive mycobacterial genes in the lungs of chronically infected mice and tuberculosis patients. Proc. Natl Acad. Sci. USA 100, 14321-14326 (2003).
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 14321-14326
    • Timm, J.1
  • 42
    • 1642566560 scopus 로고    scopus 로고
    • Hemochromatosis and the enigma of misplaced iron: Implications for infectious disease and survival
    • Moalem, S., Weinberg, E. D. & Percy, M. E. Hemochromatosis and the enigma of misplaced iron: implications for infectious disease and survival. Biometals 17, 135-139 (2004).
    • (2004) Biometals , vol.17 , pp. 135-139
    • Moalem, S.1    Weinberg, E.D.2    Percy, M.E.3
  • 43
    • 0018166595 scopus 로고
    • The adverse effect of iron repletion on the course of certain infections
    • Murray, M. J., Murray, A. B., Murray, M. B. & Murray, C. J. The adverse effect of iron repletion on the course of certain infections. Br. Med. J. 2, 1113-1115 (1978).
    • (1978) Br. Med. J. , vol.2 , pp. 1113-1115
    • Murray, M.J.1    Murray, A.B.2    Murray, M.B.3    Murray, C.J.4
  • 44
    • 0032997261 scopus 로고    scopus 로고
    • Iron loading and disease surveillance
    • Weinberg, E. D. Iron loading and disease surveillance. Emerg. Infect. Dis. 5, 346-352 (1999).
    • (1999) Emerg. Infect. Dis. , vol.5 , pp. 346-352
    • Weinberg, E.D.1
  • 46
    • 0036798949 scopus 로고    scopus 로고
    • African iron overload
    • Gordeuk, V. R. African iron overload. Semin. Hematol. 39, 263-269 (2002).
    • (2002) Semin. Hematol. , vol.39 , pp. 263-269
    • Gordeuk, V.R.1
  • 47
    • 0035479057 scopus 로고    scopus 로고
    • Association of pulmonary tuberculosis with increased dietary iron
    • Gangaidzo, I. T. et al. Association of pulmonary tuberculosis with increased dietary iron. J. Infect. Dis. 184 936-939 (2001).
    • (2001) J. Infect. Dis. , vol.184 , pp. 936-939
    • Gangaidzo, I.T.1
  • 48
    • 0029883690 scopus 로고    scopus 로고
    • Associations of iron overload in Africa with hepatocellular carcinoma and tuberculosis: Strachan's 1929 thesis revisited
    • Gordeuk, V. R., McLaren, C. E., MacPhail, A. P., Deichsel, G. & Bothwell, T. H. Associations of iron overload in Africa with hepatocellular carcinoma and tuberculosis: Strachan's 1929 thesis revisited. Blood 87, 3470-3476 (1996).
    • (1996) Blood , vol.87 , pp. 3470-3476
    • Gordeuk, V.R.1    McLaren, C.E.2    MacPhail, A.P.3    Deichsel, G.4    Bothwell, T.H.5
  • 49
    • 0026342071 scopus 로고
    • Iron overload in Africa. Interaction between a gene and dietary iron content
    • Gordeuk, V. et al. Iron overload in Africa. Interaction between a gene and dietary iron content. N. Engl. J. Med. 326 95-100 (1992).
    • (1992) N. Engl. J. Med. , vol.326 , pp. 95-100
    • Gordeuk, V.1
  • 50
    • 0032523072 scopus 로고    scopus 로고
    • Adaptive response of iron absorption to anemia, increased erythropoiesis, iron deficiency, and iron loading in β 2-microglobulin knockout mice
    • Santos, M., Clevers, H., De Sousa, M. & Marx, J. J. Adaptive response of iron absorption to anemia, increased erythropoiesis, iron deficiency, and iron loading in β2-microglobulin knockout mice. Blood 91, 3059-3065 (1998).
    • (1998) Blood , vol.91 , pp. 3059-3065
    • Santos, M.1    Clevers, H.2    De Sousa, M.3    Marx, J.J.4
  • 51
    • 0034743547 scopus 로고    scopus 로고
    • MHC class Ia-restricted T cells partially account for β2-microglobulin-dependent resistance to Mycobacterium tuberculosis
    • Rolph, M. S. et al. MHC class Ia-restricted T cells partially account for β2-microglobulin-dependent resistance to Mycobacterium tuberculosis. Eur. J. Immunol. 31, 1944-1949 (2001).
    • (2001) Eur. J. Immunol. , vol.31 , pp. 1944-1949
    • Rolph, M.S.1
  • 52
    • 0033591685 scopus 로고    scopus 로고
    • Susceptibility of mice deficient in CD1D or TAP1 to infection with Mycobacterium tuberculosis
    • Behar, S. M., Dascher, C. C., Grusby, M. J., Wang, C. R. & Brenner, M. B. Susceptibility of mice deficient in CD1D or TAP1 to infection with Mycobacterium tuberculosis. J. Exp. Med. 189, 1973-1980 (1999).
    • (1999) J. Exp. Med. , vol.189 , pp. 1973-1980
    • Behar, S.M.1    Dascher, C.C.2    Grusby, M.J.3    Wang, C.R.4    Brenner, M.B.5
  • 53
    • 0034547175 scopus 로고    scopus 로고
    • Systemic oxygen-free radical production in iron-loaded mice
    • Bartfay, W. J. & Bartfay, E. Systemic oxygen-free radical production in iron-loaded mice. West J. Nurs. Res. 22, 927-935 (2000).
    • (2000) West J. Nurs. Res. , vol.22 , pp. 927-935
    • Bartfay, W.J.1    Bartfay, E.2
  • 54
    • 0025815345 scopus 로고
    • Role of transferrin, transferrin receptors, and iron in macrophage listericidal activity
    • Alford, C. E., King, T. E. Jr & Campbell, P. A. Role of transferrin, transferrin receptors, and iron in macrophage listericidal activity. J. Exp. Med. 174, 459-466 (1991).
    • (1991) J. Exp. Med. , vol.174 , pp. 459-466
    • Alford, C.E.1    King Jr., T.E.2    Campbell, P.A.3
  • 56
    • 0032737846 scopus 로고    scopus 로고
    • Lactoferrin: A multifunctional glycoprotein
    • Vorland, L. H. Lactoferrin: a multifunctional glycoprotein. APMIS 107, 971-981 (1999).
    • (1999) APMIS , vol.107 , pp. 971-981
    • Vorland, L.H.1
  • 57
    • 0037198693 scopus 로고    scopus 로고
    • A component of innate immunity prevents bacterial biofilm development
    • Singh, P. K., Parsek, M. R., Greenberg, E. P. & Welsh, M. J. A component of innate immunity prevents bacterial biofilm development. Nature 417, 552-555 (2002).
    • (2002) Nature , vol.417 , pp. 552-555
    • Singh, P.K.1    Parsek, M.R.2    Greenberg, E.P.3    Welsh, M.J.4
  • 58
    • 2942717102 scopus 로고    scopus 로고
    • In vivo effects of bifidobacteria and lactoferrin on gut endotoxin concentration and mucosal immunity in Balb/c mice
    • Griffiths, E. A. et al. In vivo effects of bifidobacteria and lactoferrin on gut endotoxin concentration and mucosal immunity in Balb/c mice. Dig. Dis. Sci. 49, 579-589 (2004).
    • (2004) Dig. Dis. Sci. , vol.49 , pp. 579-589
    • Griffiths, E.A.1
  • 59
    • 0035001420 scopus 로고    scopus 로고
    • Lactoferrin peptide increases the survival of Candida albicans-inoculated mice by upregulating neutrophil and macrophage functions, especially in combination with amphotericin B and granulocyte-macrophage colony-stimulating factor
    • Tanida, T., Rao, F., Hamada, T., Ueta, E. & Osaki, T. Lactoferrin peptide increases the survival of Candida albicans inoculated mice by upregulating neutrophil and macrophage functions, especially in combination with amphotericin B and granulocyte-macrophage colony-stimulating factor. Infect. Immun. 69, 3883-3890 (2001).
    • (2001) Infect. Immun. , vol.69 , pp. 3883-3890
    • Tanida, T.1    Rao, F.2    Hamada, T.3    Ueta, E.4    Osaki, T.5
  • 60
    • 0035083899 scopus 로고    scopus 로고
    • A novel bovine lactoferrin peptide, FKCRRWQWRM, suppresses Candida cell growth and activates neutrophils
    • Ueta, E., Tanida, T., & Osaki, T. A novel bovine lactoferrin peptide, FKCRRWQWRM, suppresses Candida cell growth and activates neutrophils. J. Pept. Res. 57, 240-249 (2001).
    • (2001) J. Pept. Res. , vol.57 , pp. 240-249
    • Ueta, E.1    Tanida, T.2    Osaki, T.3
  • 61
    • 0035001420 scopus 로고    scopus 로고
    • Lactoferrin peptide increases the survival of Candida albicans-inoculated mice by upregulating neutrophil and macrophage functions, especially in combination with amphotericin B and granulocyte-macrophage colony-stimulating factor
    • Tanida, T., Rao, F., Hamada, T., Ueta, E. & Osaki, T. Lactoferrin peptide increases the survival of Candida albicans inoculated mice by upregulating neutrophil and macrophage functions, especially in combination with amphotericin B and granulocyte-macrophage colony-stimulating factor. Infect. Immun. 69, 3883-3890 (2001).
    • (2001) Infect. Immun. , vol.69 , pp. 3883-3890
    • Tanida, T.1    Rao, F.2    Hamada, T.3    Ueta, E.4    Osaki, T.5
  • 62
    • 0027465990 scopus 로고
    • Antibacterial acivity of lactoferrin and a pepsin-derived lactoferrin peptide fragment
    • Yamauchi, K., Tomita, M., Giehl, T. J. & Ellison, R. T. Antibacterial acivity of lactoferrin and a pepsin-derived lactoferrin peptide fragment. Infect. Immun. 61, 719-728 (1993).
    • (1993) Infect. Immun. , vol.61 , pp. 719-728
    • Yamauchi, K.1    Tomita, M.2    Giehl, T.J.3    Ellison, R.T.4
  • 63
    • 0034303318 scopus 로고    scopus 로고
    • Effects of iron overload on the immune system
    • Walker, E. M. Jr & Walker, S. M. Effects of iron overload on the immune system. Ann. Clin. Lab. Sci. 30, 354-365 (2000).
    • (2000) Ann. Clin. Lab. Sci. , vol.30 , pp. 354-365
    • Walker Jr., E.M.1    Walker, S.M.2
  • 64
    • 0042871288 scopus 로고    scopus 로고
    • Iron deficiency and in vitro iron chelation reduce the expression of cluster of differentiation molecule (CD)28 but not CD3 receptors on murine thymocytes and spleen cells
    • Kuvibidila, S. R. & Porretta, C. Iron deficiency and in vitro iron chelation reduce the expression of cluster of differentiation molecule (CD)28 but not CD3 receptors on murine thymocytes and spleen cells. Br. J. Nutr. 90, 179-189 (2003).
    • (2003) Br. J. Nutr. , vol.90 , pp. 179-189
    • Kuvibidila, S.R.1    Porretta, C.2
  • 65
    • 0041709345 scopus 로고    scopus 로고
    • Iron-deficient mice fail to develop autoimmune encephalomyelitis
    • Grant, S. M., Wiesinger, J. A., Beard, J. L. & Cantorna, M. T. Iron-deficient mice fail to develop autoimmune encephalomyelitis. J. Nutr. 133, 2635-2638 (2003).
    • (2003) J. Nutr. , vol.133 , pp. 2635-2638
    • Grant, S.M.1    Wiesinger, J.A.2    Beard, J.L.3    Cantorna, M.T.4
  • 66
    • 0027983998 scopus 로고
    • The IgM and IgG antibody responses in iron-deficient and iron-loaded mice
    • Omara, F. O. & Blakley, B. R. The IgM and IgG antibody responses in iron-deficient and iron-loaded mice. Biol. Trace Elem. Res. 46, 155-161 (1994).
    • (1994) Biol. Trace Elem. Res. , vol.46 , pp. 155-161
    • Omara, F.O.1    Blakley, B.R.2
  • 67
    • 0028576486 scopus 로고
    • The effects of iron deficiency and iron overload on cell-mediated immunity in the mouse
    • Omara, F. O. & Blakley, B. R. The effects of iron deficiency and iron overload on cell-mediated immunity in the mouse. Br. J. Nutr. 72, 899-909 (1994).
    • (1994) Br. J. Nutr. , vol.72 , pp. 899-909
    • Omara, F.O.1    Blakley, B.R.2
  • 68
    • 0033818098 scopus 로고    scopus 로고
    • Effect of transfusional iron overload on immune response
    • Cunningham-Rundles, S. et al. Effect of transfusional iron overload on immune response. J. Infect. Dis. 182, S115-S121 (2000).
    • (2000) J. Infect. Dis. , vol.182
    • Cunningham-Rundles, S.1
  • 70
    • 0031982370 scopus 로고    scopus 로고
    • The immunological system in hemochromatosis
    • de Sousa, M. & Porto, G. The immunological system in hemochromatosis. J. Hepatol. 28, (Suppl. 1) 1-7 (1998).
    • (1998) J. Hepatol. , vol.28 , Issue.SUPPL. 1 , pp. 1-7
    • de Sousa, M.1    Porto, G.2
  • 71
    • 0034534699 scopus 로고    scopus 로고
    • The outcome of Leishmania major experimental infection in BALB/c mice can be modulated by exogenously delivered iron
    • Bisti, S. et al. The outcome of Leishmania major experimental infection in BALB/c mice can be modulated by exogenously delivered iron. Eur. J. Immunol. 30, 3732-3740 (2000).
    • (2000) Eur. J. Immunol. , vol.30 , pp. 3732-3740
    • Bisti, S.1
  • 72
    • 0032721955 scopus 로고    scopus 로고
    • Associations between cellular immune effector function, iron metabolism, and disease activity in patients with chronic hepatitis C virus infection
    • Weiss, G. et al. Associations between cellular immune effector function, iron metabolism, and disease activity in patients with chronic hepatitis C virus infection. J. Infect. Dis. 180, 1452-1458 (1999).
    • (1999) J. Infect. Dis. , vol.180 , pp. 1452-1458
    • Weiss, G.1
  • 73
    • 2342510407 scopus 로고    scopus 로고
    • IL-6 mediates hypoferremia of inflammation by inducing the synthesis of the iron regulatory hormone hepcidin
    • Nemeth, E. et al. IL-6 mediates hypoferremia of inflammation by inducing the synthesis of the iron regulatory hormone hepcidin. J. Clin. Invest. 113, 1271-1276 (2004).
    • (2004) J. Clin. Invest. , vol.113 , pp. 1271-1276
    • Nemeth, E.1


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