메뉴 건너뛰기




Volumn 14, Issue 3, 2012, Pages 207-216

Iron metabolism and the innate immune response to infection

Author keywords

Hepcidin; Inflammation; Innate immunity

Indexed keywords

CYTOKINE; FERRIC ION; FERRITIN; FERROPORTIN; FERROUS ION; HAPTOGLOBIN; HEME; HEMOGLOBIN; HEMOPEXIN; HEPCIDIN; IRON; LACTOFERRIN; LIPOCALIN; NATURAL RESISTANCE ASSOCIATED MACROPHAGE PROTEIN 1; NATURAL RESISTANCE ASSOCIATED MACROPHAGE PROTEIN 2; SIDEROCALIN; TRANSFERRIN; TRANSFERRIN RECEPTOR; UNCLASSIFIED DRUG;

EID: 84856327464     PISSN: 12864579     EISSN: 1769714X     Source Type: Journal    
DOI: 10.1016/j.micinf.2011.10.001     Document Type: Short Survey
Times cited : (196)

References (117)
  • 1
    • 77953566560 scopus 로고    scopus 로고
    • Innate instruction of adaptive immunity revisited: the inflammasome
    • Eisenbarth S.C., Flavell R.A. Innate instruction of adaptive immunity revisited: the inflammasome. EMBO Mol. Med. 2009, 1:92-98.
    • (2009) EMBO Mol. Med. , vol.1 , pp. 92-98
    • Eisenbarth, S.C.1    Flavell, R.A.2
  • 3
    • 79955491642 scopus 로고    scopus 로고
    • Iron homeostasis and nutritional iron deficiency
    • Theil E.C. Iron homeostasis and nutritional iron deficiency. J. Nutr. 2011, 141:724S-728S.
    • (2011) J. Nutr. , vol.141
    • Theil, E.C.1
  • 4
    • 79952162002 scopus 로고    scopus 로고
    • Regulation of cellular iron metabolism
    • Wang J., Pantopoulos K. Regulation of cellular iron metabolism. Biochem. J. 2011, 434:365-381.
    • (2011) Biochem. J. , vol.434 , pp. 365-381
    • Wang, J.1    Pantopoulos, K.2
  • 5
    • 79955958017 scopus 로고    scopus 로고
    • Hepcidin and iron regulation, 10 years Later
    • Ganz T. Hepcidin and iron regulation, 10 years Later. Blood 2011, 117:4425-4433.
    • (2011) Blood , vol.117 , pp. 4425-4433
    • Ganz, T.1
  • 6
    • 2342510407 scopus 로고    scopus 로고
    • IL-6 mediates hypoferremia of inflammation by inducing the synthesis of the iron regulatory hormone hepcidin
    • Nemeth E., Rivera S., Gabayan V., Keller C., Taudorf S., Pedersen B.K., Ganz T. IL-6 mediates hypoferremia of inflammation by inducing the synthesis of the iron regulatory hormone hepcidin. J. Clin. Invest. 2004, 113:1271-1276.
    • (2004) J. Clin. Invest. , vol.113 , pp. 1271-1276
    • Nemeth, E.1    Rivera, S.2    Gabayan, V.3    Keller, C.4    Taudorf, S.5    Pedersen, B.K.6    Ganz, T.7
  • 7
    • 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., Ganz T., Kaplan J. 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    Ganz, T.7    Kaplan, J.8
  • 9
    • 33746868342 scopus 로고    scopus 로고
    • Hereditary hemochromatosis
    • Pietrangelo A. Hereditary hemochromatosis. Biochim. Biophys. Acta 2006, 1763:700-710.
    • (2006) Biochim. Biophys. Acta , vol.1763 , pp. 700-710
    • Pietrangelo, A.1
  • 10
    • 35448938485 scopus 로고    scopus 로고
    • Association of hemochromatosis with infectious diseases: expanding spectrum
    • Khan F.A., Fisher M.A., Khakoo R.A. Association of hemochromatosis with infectious diseases: expanding spectrum. Int. J. Infect. Dis. 2007, 11:482-487.
    • (2007) Int. J. Infect. Dis. , vol.11 , pp. 482-487
    • Khan, F.A.1    Fisher, M.A.2    Khakoo, R.A.3
  • 11
    • 33845878232 scopus 로고    scopus 로고
    • Hereditary hemochromatosis results in decreased iron acquisition and growth by Mycobacterium tuberculosis within human macrophages
    • Olakanmi O., Schlesinger L.S., Britigan B.E. Hereditary hemochromatosis results in decreased iron acquisition and growth by Mycobacterium tuberculosis within human macrophages. J. Leukoc. Biol. 2007, 81:195-204.
    • (2007) J. Leukoc. Biol. , vol.81 , pp. 195-204
    • Olakanmi, O.1    Schlesinger, L.S.2    Britigan, B.E.3
  • 16
    • 0037011071 scopus 로고    scopus 로고
    • Correction of the iron overload defect in beta-2-microglobulin knockout mice by lactoferrin abolishes their increased susceptibility to tuberculosis
    • Schaible U.E., Collins H.L., Priem F., Kaufmann S.H. Correction of the iron overload defect in beta-2-microglobulin knockout mice by lactoferrin abolishes their increased susceptibility to tuberculosis. J. Exp. Med. 2002, 196:1507-1513.
    • (2002) J. Exp. Med. , vol.196 , pp. 1507-1513
    • Schaible, U.E.1    Collins, H.L.2    Priem, F.3    Kaufmann, S.H.4
  • 17
    • 0027428420 scopus 로고
    • Transferrin and lactoferrin undergo proteolytic cleavage in the Pseudomonas aeruginosa-infected lungs of patients with cystic fibrosis
    • Britigan B.E., Hayek M.B., Doebbeling B.N., Fick R.B. Transferrin and lactoferrin undergo proteolytic cleavage in the Pseudomonas aeruginosa-infected lungs of patients with cystic fibrosis. Infect. Immun. 1993, 61:5049-5055.
    • (1993) Infect. Immun. , vol.61 , pp. 5049-5055
    • Britigan, B.E.1    Hayek, M.B.2    Doebbeling, B.N.3    Fick, R.B.4
  • 18
    • 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 2002, 417:552-555.
    • (2002) Nature , vol.417 , pp. 552-555
    • Singh, P.K.1    Parsek, M.R.2    Greenberg, E.P.3    Welsh, M.J.4
  • 20
    • 42049096101 scopus 로고    scopus 로고
    • Stimulus-dependent impairment of the neutrophil oxidative burst response in lactoferrin-deficient mice
    • Ward P.P., Mendoza-Meneses M., Park P.W., Conneely O.M. Stimulus-dependent impairment of the neutrophil oxidative burst response in lactoferrin-deficient mice. Am. J. Pathol. 2008, 172:1019-1029.
    • (2008) Am. J. Pathol. , vol.172 , pp. 1019-1029
    • Ward, P.P.1    Mendoza-Meneses, M.2    Park, P.W.3    Conneely, O.M.4
  • 21
    • 33646947821 scopus 로고    scopus 로고
    • Neutrophil gelatinase-associated lipocalin, a siderophore-binding eukaryotic protein
    • Borregaard N., Cowland J.B. Neutrophil gelatinase-associated lipocalin, a siderophore-binding eukaryotic protein. Biometals 2006, 19:211-215.
    • (2006) Biometals , vol.19 , pp. 211-215
    • Borregaard, N.1    Cowland, J.B.2
  • 22
    • 0036865552 scopus 로고    scopus 로고
    • The neutrophil lipocalin NGAL is a bacteriostatic agent that interferes with siderophore-mediated iron acquisition
    • Goetz D.H., Holmes M.A., Borregaard N., Bluhm M.E., Raymond K.N., Strong R.K. The neutrophil lipocalin NGAL is a bacteriostatic agent that interferes with siderophore-mediated iron acquisition. Mol. Cell 2002, 10:1033-1043.
    • (2002) Mol. Cell , vol.10 , pp. 1033-1043
    • Goetz, D.H.1    Holmes, M.A.2    Borregaard, N.3    Bluhm, M.E.4    Raymond, K.N.5    Strong, R.K.6
  • 23
    • 11844301598 scopus 로고    scopus 로고
    • Siderocalin (Lcn 2) also binds carboxymycobactins, potentially defending against mycobacterial infections through iron sequestration
    • Holmes M.A., Paulsene W., Jide X., Ratledge C., Strong R.K. Siderocalin (Lcn 2) also binds carboxymycobactins, potentially defending against mycobacterial infections through iron sequestration. Structure 2005, 13:29-41.
    • (2005) Structure , vol.13 , pp. 29-41
    • Holmes, M.A.1    Paulsene, W.2    Jide, X.3    Ratledge, C.4    Strong, R.K.5
  • 29
    • 77953690176 scopus 로고    scopus 로고
    • A mammalian siderophore synthesized by an enzyme with a bacterial homolog involved in enterobactin production
    • Devireddy L.R., Hart D.O., Goetz D.H., Green M.R. A mammalian siderophore synthesized by an enzyme with a bacterial homolog involved in enterobactin production. Cell 2010, 141:1006-1017.
    • (2010) Cell , vol.141 , pp. 1006-1017
    • Devireddy, L.R.1    Hart, D.O.2    Goetz, D.H.3    Green, M.R.4
  • 30
    • 0033614040 scopus 로고    scopus 로고
    • Hemoglobin endocytosis in Leishmania is mediated through a 46-kDa protein located in the flagellar pocket
    • Sengupta S., Tripathi J., Tandon R., Raje M., Roy R.P., Basu S.K., Mukhopadhyay A. Hemoglobin endocytosis in Leishmania is mediated through a 46-kDa protein located in the flagellar pocket. J. Biol. Chem. 1999, 274:2758-2765.
    • (1999) J. Biol. Chem. , vol.274 , pp. 2758-2765
    • Sengupta, S.1    Tripathi, J.2    Tandon, R.3    Raje, M.4    Roy, R.P.5    Basu, S.K.6    Mukhopadhyay, A.7
  • 32
    • 0030879653 scopus 로고    scopus 로고
    • Hemoglobin metabolism in the malaria parasite Plasmodium falciparum
    • Francis S.E., Sullivan D.J., Goldberg D.E. Hemoglobin metabolism in the malaria parasite Plasmodium falciparum. Ann. Rev. Microbiol. 1997, 51:97-123.
    • (1997) Ann. Rev. Microbiol. , vol.51 , pp. 97-123
    • Francis, S.E.1    Sullivan, D.J.2    Goldberg, D.E.3
  • 33
    • 78049442406 scopus 로고    scopus 로고
    • Signaling to heme oxygenase-1 and its anti-inflammatory therapeutic potential
    • Paine A., Eiz-Vesper B., Blasczyk R., Immenschuh S. Signaling to heme oxygenase-1 and its anti-inflammatory therapeutic potential. Biochem. Pharmacol. 2010, 80:1895-1903.
    • (2010) Biochem. Pharmacol. , vol.80 , pp. 1895-1903
    • Paine, A.1    Eiz-Vesper, B.2    Blasczyk, R.3    Immenschuh, S.4
  • 35
    • 54049119637 scopus 로고    scopus 로고
    • Intracellular microbes and haemophagocytosis
    • Silva-Herzog E., Detweiler C.S. Intracellular microbes and haemophagocytosis. Cell Microbiol. 2008, 10:2151-2158.
    • (2008) Cell Microbiol. , vol.10 , pp. 2151-2158
    • Silva-Herzog, E.1    Detweiler, C.S.2
  • 36
    • 0024555386 scopus 로고
    • Interferon gamma-activated human monocytes downregulate transferrin receptors and inhibit the intracellular multiplication of Legionella pneumophila by limiting the availability of iron
    • Byrd T.F., Horwitz M.A. Interferon gamma-activated human monocytes downregulate transferrin receptors and inhibit the intracellular multiplication of Legionella pneumophila by limiting the availability of iron. J. Clin. Invest. 1989, 83:1457-1465.
    • (1989) J. Clin. Invest. , vol.83 , pp. 1457-1465
    • Byrd, T.F.1    Horwitz, M.A.2
  • 37
    • 0027476872 scopus 로고
    • Regulation of transferrin receptor expression and ferritin content in human mononuclear phagocytes. Coordinate upregulation by iron transferrin and downregulation by interferon gamma
    • 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 gamma. J. Clin. Invest. 1993, 91:969-976.
    • (1993) J. Clin. Invest. , vol.91 , pp. 969-976
    • Byrd, T.F.1    Horwitz, M.A.2
  • 38
    • 41449113593 scopus 로고    scopus 로고
    • Innate immunity to intraphagosomal pathogens is mediated by interferon regulatory factor 8 (IRF-8) that stimulates the expression of macrophage-specific Nramp1 through antagonizing repression by c-Myc
    • ter-Koltunoff M., Goren S., Nousbeck J., Feng C.G., Sher A., Ozato K., Azriel A., Levi B.Z. Innate immunity to intraphagosomal pathogens is mediated by interferon regulatory factor 8 (IRF-8) that stimulates the expression of macrophage-specific Nramp1 through antagonizing repression by c-Myc. J. Biol. Chem. 2008, 283:2724-2733.
    • (2008) J. Biol. Chem. , vol.283 , pp. 2724-2733
    • ter-Koltunoff, M.1    Goren, S.2    Nousbeck, J.3    Feng, C.G.4    Sher, A.5    Ozato, K.6    Azriel, A.7    Levi, B.Z.8
  • 39
    • 50549086197 scopus 로고    scopus 로고
    • Interferon-gamma limits the availability of iron for intramacrophage Salmonella typhimurium
    • Nairz M., Fritsche G., Brunner P., Talasz H., Hantke K., Weiss G. Interferon-gamma limits the availability of iron for intramacrophage Salmonella typhimurium. Eur. J. Immunol. 2008, 38:1923-1936.
    • (2008) Eur. J. Immunol. , vol.38 , pp. 1923-1936
    • Nairz, M.1    Fritsche, G.2    Brunner, P.3    Talasz, H.4    Hantke, K.5    Weiss, G.6
  • 40
    • 0029905151 scopus 로고    scopus 로고
    • The Mycobacterium tuberculosis phagosome interacts with early endosomes and is accessible to exogenously administered transferrin
    • Clemens D.L., Horwitz M.A. The Mycobacterium tuberculosis phagosome interacts with early endosomes and is accessible to exogenously administered transferrin. J. Exp. Med. 1996, 184:1349-1355.
    • (1996) J. Exp. Med. , vol.184 , pp. 1349-1355
    • Clemens, D.L.1    Horwitz, M.A.2
  • 42
    • 0027262167 scopus 로고
    • Natural resistance to infection with intracellular parasites: isolation of a candidate for Bcg
    • Vidal S.M., Malo D., Vogan K., Skamene E., Gros P. Natural resistance to infection with intracellular parasites: isolation of a candidate for Bcg. Cell 1993, 73:469-485.
    • (1993) Cell , vol.73 , pp. 469-485
    • Vidal, S.M.1    Malo, D.2    Vogan, K.3    Skamene, E.4    Gros, P.5
  • 45
    • 33947381278 scopus 로고    scopus 로고
    • Nramp1 phagocyte intracellular metal withdrawal defense
    • Cellier M.F., Courville P., Campion C. Nramp1 phagocyte intracellular metal withdrawal defense. Microb. Infect. 2007, 9:1662-1670.
    • (2007) Microb. Infect. , vol.9 , pp. 1662-1670
    • Cellier, M.F.1    Courville, P.2    Campion, C.3
  • 47
    • 0035421993 scopus 로고    scopus 로고
    • Divalent-metal transport by NRAMP proteins at the interface of host-pathogen interactions
    • Forbes J.R., Gros P. Divalent-metal transport by NRAMP proteins at the interface of host-pathogen interactions. Trends Microbiol. 2001, 9:397-403.
    • (2001) Trends Microbiol. , vol.9 , pp. 397-403
    • Forbes, J.R.1    Gros, P.2
  • 48
    • 34547863499 scopus 로고    scopus 로고
    • The co-ordinated regulation of iron homeostasis in murine macrophages limits the availability of iron for intracellular Salmonella typhimurium
    • Nairz M., Theurl I., Ludwiczek S., Theurl M., Mair S.M., Fritsche G., Weiss G. The co-ordinated regulation of iron homeostasis in murine macrophages limits the availability of iron for intracellular Salmonella typhimurium. Cell Microbiol. 2007, 9:2126-2140.
    • (2007) Cell Microbiol. , vol.9 , pp. 2126-2140
    • Nairz, M.1    Theurl, I.2    Ludwiczek, S.3    Theurl, M.4    Mair, S.M.5    Fritsche, G.6    Weiss, G.7
  • 49
    • 70349923239 scopus 로고    scopus 로고
    • Slc11a1 limits intracellular growth of Salmonella enterica sv. Typhimurium by promoting macrophage immune effector functions and impairing bacterial iron acquisition
    • Nairz M., Fritsche G., Crouch M.L., Barton H.C., Fang F.C., Weiss G. Slc11a1 limits intracellular growth of Salmonella enterica sv. Typhimurium by promoting macrophage immune effector functions and impairing bacterial iron acquisition. Cell Microbiol. 2009, 11:1365-1381.
    • (2009) Cell Microbiol. , vol.11 , pp. 1365-1381
    • Nairz, M.1    Fritsche, G.2    Crouch, M.L.3    Barton, H.C.4    Fang, F.C.5    Weiss, G.6
  • 50
    • 50849096115 scopus 로고    scopus 로고
    • The iron export protein ferroportin 1 is differentially expressed in mouse macrophage populations and is present in the mycobacterial-containing phagosome
    • Van Zandt K.E., Sow F.B., Florence W.C., Zwilling B.S., Satoskar A.R., Schlesinger L.S., Lafuse W.P. The iron export protein ferroportin 1 is differentially expressed in mouse macrophage populations and is present in the mycobacterial-containing phagosome. J. Leukoc. Biol. 2008, 84:689-700.
    • (2008) J. Leukoc. Biol. , vol.84 , pp. 689-700
    • Van Zandt, K.E.1    Sow, F.B.2    Florence, W.C.3    Zwilling, B.S.4    Satoskar, A.R.5    Schlesinger, L.S.6    Lafuse, W.P.7
  • 51
    • 48549100053 scopus 로고    scopus 로고
    • Human macrophage host defense against Mycobacterium tuberculosis
    • Liu P.T., Modlin R.L. Human macrophage host defense against Mycobacterium tuberculosis. Curr. Opin. Immunol. 2008, 20:371-376.
    • (2008) Curr. Opin. Immunol. , vol.20 , pp. 371-376
    • Liu, P.T.1    Modlin, R.L.2
  • 52
    • 0030481130 scopus 로고    scopus 로고
    • Mycobacterium-containing phagosomes are accessible to early endosomes and reflect a transitional state in normal phagosome biogenesis
    • Sturgill-Koszycki S., Schaible U.E., Russell D.G. Mycobacterium-containing phagosomes are accessible to early endosomes and reflect a transitional state in normal phagosome biogenesis. EMBO J. 1996, 15:6960-6968.
    • (1996) EMBO J. , vol.15 , pp. 6960-6968
    • Sturgill-Koszycki, S.1    Schaible, U.E.2    Russell, D.G.3
  • 55
    • 0033759220 scopus 로고    scopus 로고
    • Iron metabolism in pathogenic bacteria
    • Ratledge C., Dover L.G. Iron metabolism in pathogenic bacteria. Annu. Rev. Microbiol. 2000, 54:881-941.
    • (2000) Annu. Rev. Microbiol. , vol.54 , pp. 881-941
    • Ratledge, C.1    Dover, L.G.2
  • 56
    • 0033973479 scopus 로고    scopus 로고
    • The salicylate-derived mycobactin siderophores of Mycobacterium tuberculosis are essential for growth in macrophages
    • De Voss J.J., Rutter K., Schroeder B.G., Su H., Zhu Y., Barry C.E. The salicylate-derived mycobactin siderophores of Mycobacterium tuberculosis are essential for growth in macrophages. Proc. Natl. Acad. Sci. U. S. A 2000, 97:1252-1257.
    • (2000) Proc. Natl. Acad. Sci. U. S. A , vol.97 , pp. 1252-1257
    • De Voss, J.J.1    Rutter, K.2    Schroeder, B.G.3    Su, H.4    Zhu, Y.5    Barry, C.E.6
  • 57
    • 22844443827 scopus 로고    scopus 로고
    • Iron and iron chelating agents modulate Mycobacterium tuberculosis growth and monocyte-macrophage viability and effector functions
    • Cronje L., Edmondson N., Eisenach K.D., Bornman L. Iron and iron chelating agents modulate Mycobacterium tuberculosis growth and monocyte-macrophage viability and effector functions. FEMS Immunol. Med. Microbiol. 2005, 45:103-112.
    • (2005) FEMS Immunol. Med. Microbiol. , vol.45 , pp. 103-112
    • Cronje, L.1    Edmondson, N.2    Eisenach, K.D.3    Bornman, L.4
  • 59
    • 0038172355 scopus 로고    scopus 로고
    • Impact of iron loading on the activity of isoniazid or ethambutol in the treatment of murine tuberculosis
    • Lounis N., Maslo C., Truffot-Pernot C., Grosset J., Boelaert R.J. Impact of iron loading on the activity of isoniazid or ethambutol in the treatment of murine tuberculosis. Int. J. Tuberc. Lung Dis. 2003, 7:575-579.
    • (2003) Int. J. Tuberc. Lung Dis. , vol.7 , pp. 575-579
    • Lounis, N.1    Maslo, C.2    Truffot-Pernot, C.3    Grosset, J.4    Boelaert, R.J.5
  • 60
    • 0027331982 scopus 로고
    • Effect of iron on the growth and siderophore production of mycobacteria
    • Raghu B., Sarma G.R., Venkatesan P. Effect of iron on the growth and siderophore production of mycobacteria. Biochem. Mol. Biol. Int. 1993, 31:341-348.
    • (1993) Biochem. Mol. Biol. Int. , vol.31 , pp. 341-348
    • Raghu, B.1    Sarma, G.R.2    Venkatesan, P.3
  • 61
    • 53649106524 scopus 로고    scopus 로고
    • Increased susceptibility to Mycobacterium avium in hemochromatosis protein HFE-deficient mice
    • Gomes-Pereira S., Rodrigues P.N., Appelberg R., Gomes M.S. Increased susceptibility to Mycobacterium avium in hemochromatosis protein HFE-deficient mice. Infect. Immun. 2008, 76:4713-4719.
    • (2008) Infect. Immun. , vol.76 , pp. 4713-4719
    • Gomes-Pereira, S.1    Rodrigues, P.N.2    Appelberg, R.3    Gomes, M.S.4
  • 62
    • 53149123286 scopus 로고    scopus 로고
    • Attenuated inflammatory responses in hemochromatosis reveal a role for iron in the regulation of macrophage cytokine translation
    • Wang L., Johnson E.E., Shi H.N., Walker W.A., Wessling-Resnick M., Cherayil B.J. Attenuated inflammatory responses in hemochromatosis reveal a role for iron in the regulation of macrophage cytokine translation. J. Immunol. 2008, 181:2723-2731.
    • (2008) J. Immunol. , vol.181 , pp. 2723-2731
    • Wang, L.1    Johnson, E.E.2    Shi, H.N.3    Walker, W.A.4    Wessling-Resnick, M.5    Cherayil, B.J.6
  • 63
    • 34547863499 scopus 로고    scopus 로고
    • The co-ordinated regulation of iron homeostasis in murine macrophages limits the availability of iron for intracellular Salmonella typhimurium
    • Nairz M., Theurl I., Ludwiczek S., Theurl M., Mair S.M., Fritsche G., Weiss G. The co-ordinated regulation of iron homeostasis in murine macrophages limits the availability of iron for intracellular Salmonella typhimurium. Cell Microbiol. 2007, 9:2126-2140.
    • (2007) Cell Microbiol. , vol.9 , pp. 2126-2140
    • Nairz, M.1    Theurl, I.2    Ludwiczek, S.3    Theurl, M.4    Mair, S.M.5    Fritsche, G.6    Weiss, G.7
  • 64
    • 50549086197 scopus 로고    scopus 로고
    • Interferon-gamma limits the availability of iron for intramacrophage Salmonella typhimurium
    • Nairz M., Fritsche G., Brunner P., Talasz H., Hantke K., Weiss G. Interferon-gamma limits the availability of iron for intramacrophage Salmonella typhimurium. Eur. J. Immunol. 2008, 38:1923-1936.
    • (2008) Eur. J. Immunol. , vol.38 , pp. 1923-1936
    • Nairz, M.1    Fritsche, G.2    Brunner, P.3    Talasz, H.4    Hantke, K.5    Weiss, G.6
  • 66
    • 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. 1978, 2:1113-1115.
    • (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
  • 69
    • 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 1996, 87:3470-3476.
    • (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
  • 72
    • 0036062256 scopus 로고    scopus 로고
    • Charting HIV's remarkable voyage through the cell: basic science as a passport to future therapy
    • Greene W.C., Peterlin B.M. Charting HIV's remarkable voyage through the cell: basic science as a passport to future therapy. Nat. Med. 2002, 8:673-680.
    • (2002) Nat. Med. , vol.8 , pp. 673-680
    • Greene, W.C.1    Peterlin, B.M.2
  • 73
    • 34247167150 scopus 로고    scopus 로고
    • Iron causes interactions of TAK1, p21ras, and phosphatidylinositol 3-kinase in caveolae to activate IkappaB kinase in hepatic macrophages
    • Chen L., Xiong S., She H., Lin S.W., Wang J., Tsukamoto H. Iron causes interactions of TAK1, p21ras, and phosphatidylinositol 3-kinase in caveolae to activate IkappaB kinase in hepatic macrophages. J. Biol. Chem. 2007, 282:5582-5588.
    • (2007) J. Biol. Chem. , vol.282 , pp. 5582-5588
    • Chen, L.1    Xiong, S.2    She, H.3    Lin, S.W.4    Wang, J.5    Tsukamoto, H.6
  • 77
    • 70450227340 scopus 로고    scopus 로고
    • Inhibition of HIV-1 gene expression by Ciclopirox and Deferiprone, drugs that prevent hypusination of eukaryotic initiation factor 5A
    • Hoque M., Hanauske-Abel H.M., Palumbo P., Saxena D., D'Alliessi G.D., Park M.H., Pe'ery T., Mathews M.B. Inhibition of HIV-1 gene expression by Ciclopirox and Deferiprone, drugs that prevent hypusination of eukaryotic initiation factor 5A. Retrovirology 2009, 6:90.
    • (2009) Retrovirology , vol.6 , pp. 90
    • Hoque, M.1    Hanauske-Abel, H.M.2    Palumbo, P.3    Saxena, D.4    D'Alliessi, G.D.5    Park, M.H.6    Pe'ery, T.7    Mathews, M.B.8
  • 78
    • 2942537827 scopus 로고    scopus 로고
    • Expression of the hereditary hemochromatosis protein HFE increases ferritin levels by inhibiting iron export in HT29 cells
    • Davies P.S., Enns C.A. Expression of the hereditary hemochromatosis protein HFE increases ferritin levels by inhibiting iron export in HT29 cells. J. Biol. Chem. 2004, 279:25085-25092.
    • (2004) J. Biol. Chem. , vol.279 , pp. 25085-25092
    • Davies, P.S.1    Enns, C.A.2
  • 81
    • 0032555601 scopus 로고    scopus 로고
    • Co-trafficking of HFE, a nonclassical major histocompatibility complex class I protein, with the transferrin receptor implies a role in intracellular iron regulation
    • Gross C.N., Irrinki A., Feder J.N., Enns C.A. Co-trafficking of HFE, a nonclassical major histocompatibility complex class I protein, with the transferrin receptor implies a role in intracellular iron regulation. J. Biol. Chem. 1998, 273:22068-22074.
    • (1998) J. Biol. Chem. , vol.273 , pp. 22068-22074
    • Gross, C.N.1    Irrinki, A.2    Feder, J.N.3    Enns, C.A.4
  • 83
    • 0242657708 scopus 로고    scopus 로고
    • Anemia and survival in human immunodeficiency virus
    • Lundgren J.D., Mocroft A. Anemia and survival in human immunodeficiency virus. Clin. Infect. Dis. 2003, 37(Suppl 4):S297-S303.
    • (2003) Clin. Infect. Dis. , vol.37 , Issue.SUPPL. 4
    • Lundgren, J.D.1    Mocroft, A.2
  • 84
    • 0032784036 scopus 로고    scopus 로고
    • Human immunodeficiency virus infection, anemia, and survival
    • Moore R.D. Human immunodeficiency virus infection, anemia, and survival. Clin. Infect. Dis. 1999, 29:44-49.
    • (1999) Clin. Infect. Dis. , vol.29 , pp. 44-49
    • Moore, R.D.1
  • 94
    • 0022410841 scopus 로고
    • Iron deficiency protects inbred mice against infection with Plasmodium chabaudi
    • Harvey P.W., Bell R.G., Nesheim M.C. Iron deficiency protects inbred mice against infection with Plasmodium chabaudi. Infect. Immun. 1985, 50:932-934.
    • (1985) Infect. Immun. , vol.50 , pp. 932-934
    • Harvey, P.W.1    Bell, R.G.2    Nesheim, M.C.3
  • 99
    • 30444459334 scopus 로고    scopus 로고
    • Effects of routine prophylactic supplementation with iron and folic acid on admission to hospital and mortality in preschool children in a high malaria transmission setting: community-based, randomised, placebo-controlled trial
    • Sazawal S., Black R.E., Ramsan M., Chwaya H.M., Stoltzfus R.J., Dutta A., Dhingra U., Kabole I., Deb S., Othman M.K., Kabole F.M. Effects of routine prophylactic supplementation with iron and folic acid on admission to hospital and mortality in preschool children in a high malaria transmission setting: community-based, randomised, placebo-controlled trial. Lancet 2006, 367:133-143.
    • (2006) Lancet , vol.367 , pp. 133-143
    • Sazawal, S.1    Black, R.E.2    Ramsan, M.3    Chwaya, H.M.4    Stoltzfus, R.J.5    Dutta, A.6    Dhingra, U.7    Kabole, I.8    Deb, S.9    Othman, M.K.10    Kabole, F.M.11
  • 101
    • 77953618426 scopus 로고    scopus 로고
    • Iron metabolism in trypanosomatids, and its crucial role in infection
    • Taylor M.C., Kelly J.M. Iron metabolism in trypanosomatids, and its crucial role in infection. Parasitology 2010, 137:899-917.
    • (2010) Parasitology , vol.137 , pp. 899-917
    • Taylor, M.C.1    Kelly, J.M.2
  • 102
    • 0036157819 scopus 로고    scopus 로고
    • The physiological significance of transferrin receptor variations in Trypanosoma brucei
    • Gerrits H., Mussmann R., Bitter W., Kieft R., Borst P. The physiological significance of transferrin receptor variations in Trypanosoma brucei. Mol. Biochem. Parasitol. 2002, 119:237-247.
    • (2002) Mol. Biochem. Parasitol. , vol.119 , pp. 237-247
    • Gerrits, H.1    Mussmann, R.2    Bitter, W.3    Kieft, R.4    Borst, P.5
  • 103
    • 0036176072 scopus 로고    scopus 로고
    • Growth inhibition of bloodstream forms of Trypanosoma brucei by the iron chelator deferoxamine
    • Breidbach T., Scory S., Krauth-Siegel R.L., Steverding D. Growth inhibition of bloodstream forms of Trypanosoma brucei by the iron chelator deferoxamine. Int. J. Parasitol. 2002, 32:473-479.
    • (2002) Int. J. Parasitol. , vol.32 , pp. 473-479
    • Breidbach, T.1    Scory, S.2    Krauth-Siegel, R.L.3    Steverding, D.4
  • 104
    • 33748627441 scopus 로고    scopus 로고
    • Invitro growth inhibition of bloodstream forms of Trypanosoma brucei and Trypanosoma congolense by iron chelators
    • Merschjohann K., Steverding D. Invitro growth inhibition of bloodstream forms of Trypanosoma brucei and Trypanosoma congolense by iron chelators. Kinetoplastid. Biol. Dis. 2006, 5:3.
    • (2006) Kinetoplastid. Biol. Dis. , vol.5 , pp. 3
    • Merschjohann, K.1    Steverding, D.2
  • 106
    • 0025176831 scopus 로고
    • Trypanosoma cruzi receptors for human transferrin and their role
    • Lima M.F., Villalta F. Trypanosoma cruzi receptors for human transferrin and their role. Mol. Biochem. Parasitol. 1990, 38:245-252.
    • (1990) Mol. Biochem. Parasitol. , vol.38 , pp. 245-252
    • Lima, M.F.1    Villalta, F.2
  • 107
    • 0021363538 scopus 로고
    • Role of iron in Trypanosoma cruzi infection of mice
    • Lalonde R.G., Holbein B.E. Role of iron in Trypanosoma cruzi infection of mice. J. Clin. Invest. 1984, 73:470-476.
    • (1984) J. Clin. Invest. , vol.73 , pp. 470-476
    • Lalonde, R.G.1    Holbein, B.E.2
  • 108
    • 0025049393 scopus 로고
    • The effect of iron deficiency and iron overload on the evolution of Chagas disease produced by three strains of Trypanosoma cruzi in CFW mice
    • Pedrosa M.L., Silva M.E., Silva M.E., Silva M.E., Nicoli J.R., Vieira E.C. The effect of iron deficiency and iron overload on the evolution of Chagas disease produced by three strains of Trypanosoma cruzi in CFW mice. Comp. Biochem. Physiol. A: Physiol. 1990, 97:235-243.
    • (1990) Comp. Biochem. Physiol. A: Physiol. , vol.97 , pp. 235-243
    • Pedrosa, M.L.1    Silva, M.E.2    Silva, M.E.3    Silva, M.E.4    Nicoli, J.R.5    Vieira, E.C.6
  • 109
    • 0021257520 scopus 로고
    • Role of iron in intracellular growth of Trypanosoma cruzi
    • Loo V.G., Lalonde R.G. Role of iron in intracellular growth of Trypanosoma cruzi. Infect. Immun. 1984, 45:726-730.
    • (1984) Infect. Immun. , vol.45 , pp. 726-730
    • Loo, V.G.1    Lalonde, R.G.2
  • 110
    • 34547133481 scopus 로고    scopus 로고
    • Trypanosoma cruzi: treatment with the iron chelator desferrioxamine reduces parasitemia and mortality in experimentally infected mice
    • Arantes J.M., Pedrosa M.L., Martins H.R., Veloso V.M., de L.M., Bahia M.T., Tafuri W.L., Carneiro C.M. Trypanosoma cruzi: treatment with the iron chelator desferrioxamine reduces parasitemia and mortality in experimentally infected mice. Exp. Parasitol. 2007, 117:43-50.
    • (2007) Exp. Parasitol. , vol.117 , pp. 43-50
    • Arantes, J.M.1    Pedrosa, M.L.2    Martins, H.R.3    Veloso, V.M.4    de, L.M.5    Bahia, M.T.6    Tafuri, W.L.7    Carneiro, C.M.8
  • 112
    • 58149291350 scopus 로고    scopus 로고
    • Leishmania donovani depletes labile iron pool to exploit iron uptake capacity of macrophage for its intracellular growth
    • Das N.K., Biswas S., Solanki S., Mukhopadhyay C.K. Leishmania donovani depletes labile iron pool to exploit iron uptake capacity of macrophage for its intracellular growth. Cell Microbiol. 2009, 11:83-94.
    • (2009) Cell Microbiol. , vol.11 , pp. 83-94
    • Das, N.K.1    Biswas, S.2    Solanki, S.3    Mukhopadhyay, C.K.4
  • 113
    • 33749325014 scopus 로고    scopus 로고
    • A Leishmania amazonensis ZIP family iron transporter is essential for parasite replication within macrophage phagolysosomes
    • Huynh C., Sacks D.L., Andrews N.W. A Leishmania amazonensis ZIP family iron transporter is essential for parasite replication within macrophage phagolysosomes. J. Exp. Med. 2006, 203:2363-2375.
    • (2006) J. Exp. Med. , vol.203 , pp. 2363-2375
    • Huynh, C.1    Sacks, D.L.2    Andrews, N.W.3
  • 116
    • 79951695676 scopus 로고    scopus 로고
    • Leishmania chagasi: effect of the iron deficiency on the infection in BALB/c mice
    • Malafaia G., Marcon L.N., Pereira L.F., Pedrosa M.L., Rezende S.A. Leishmania chagasi: effect of the iron deficiency on the infection in BALB/c mice. Exp. Parasitol. 2011, 127:719-723.
    • (2011) Exp. Parasitol. , vol.127 , pp. 719-723
    • Malafaia, G.1    Marcon, L.N.2    Pereira, L.F.3    Pedrosa, M.L.4    Rezende, S.A.5
  • 117
    • 33745125427 scopus 로고    scopus 로고
    • The prevention of the growth of Leishmania major progeny in BALB/c iron-loaded mice: a process coupled to increased oxidative burst, the amplitude and duration of which depend on initial parasite developmental stage and dose
    • Bisti S., Konidou G., Boelaert J., Lebastard M., Soteriadou K. The prevention of the growth of Leishmania major progeny in BALB/c iron-loaded mice: a process coupled to increased oxidative burst, the amplitude and duration of which depend on initial parasite developmental stage and dose. Microbes Infect. 2006, 8:1464-1472.
    • (2006) Microbes Infect. , vol.8 , pp. 1464-1472
    • Bisti, S.1    Konidou, G.2    Boelaert, J.3    Lebastard, M.4    Soteriadou, K.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.