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Volumn 48, Issue , 2018, Pages 118-133

Iron and innate antimicrobial immunity—Depriving the pathogen, defending the host

Author keywords

Anaemia of inflammation; Ferroportin; Hepcidin; Hypoferraemia; Infection; Iron; Macrophage

Indexed keywords

BONE MORPHOGENETIC PROTEIN 6; CCAAT ENHANCER BINDING PROTEIN DELTA; CD163 ANTIGEN; FERROPORTIN 1; GAMMA INTERFERON; HAPTOGLOBIN; HEME OXYGENASE 1; HEMOPEXIN; HEPCIDIN; HYPOXIA INDUCIBLE FACTOR; HYPOXIA INDUCIBLE FACTOR 1; HYPOXIA INDUCIBLE FACTOR 2; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INDUCIBLE NITRIC OXIDE SYNTHASE; INTERLEUKIN 22; INTERLEUKIN 6; INTERLEUKIN 8; IRON; MYELOPID; SMAD1 PROTEIN; SMAD5 PROTEIN; SMAD8 PROTEIN; STAT1 PROTEIN; STAT3 PROTEIN; TOLL LIKE RECEPTOR 2; TOLL LIKE RECEPTOR 4; TOLL LIKE RECEPTOR 6; TRANSCRIPTION FACTOR NRF2; TUMOR NECROSIS FACTOR; UNCLASSIFIED DRUG; UNINDEXED DRUG; ANTIINFECTIVE AGENT;

EID: 85044460057     PISSN: 0946672X     EISSN: 18783252     Source Type: Journal    
DOI: 10.1016/j.jtemb.2018.03.007     Document Type: Review
Times cited : (85)

References (319)
  • 1
    • 19044389821 scopus 로고    scopus 로고
    • Iron and immunity: a double-edged sword
    • Weiss, G., Iron and immunity: a double-edged sword. Eur. J. Clin. Invest. 32:Suppl. 1 (2002), 70–78.
    • (2002) Eur. J. Clin. Invest. , vol.32 , pp. 70-78
    • Weiss, G.1
  • 2
    • 0032705369 scopus 로고    scopus 로고
    • Iron-dependent changes in cellular energy metabolism: influence on citric acid cycle and oxidative phosphorylation
    • Oexle, H., Gnaiger, E., Weiss, G., Iron-dependent changes in cellular energy metabolism: influence on citric acid cycle and oxidative phosphorylation. Biochim. Biophys. Acta 1413:3 (1999), 99–107.
    • (1999) Biochim. Biophys. Acta , vol.1413 , Issue.3 , pp. 99-107
    • Oexle, H.1    Gnaiger, E.2    Weiss, G.3
  • 5
    • 0018102319 scopus 로고
    • Iron and infection
    • Weinberg, E.D., Iron and infection. Microbiol. Rev. 42:1 (1978), 45–66.
    • (1978) Microbiol. Rev. , vol.42 , Issue.1 , pp. 45-66
    • Weinberg, E.D.1
  • 9
    • 0842326209 scopus 로고    scopus 로고
    • The ferritin-like Dps protein is required for Salmonella enterica serovar Typhimurium oxidative stress resistance and virulence
    • Halsey, T.A., Vazquez-Torres, A., Gravdahl, D.J., Fang, F.C., Libby, S.J., The ferritin-like Dps protein is required for Salmonella enterica serovar Typhimurium oxidative stress resistance and virulence. Infect. Immun. 72:2 (2004), 1155–1158.
    • (2004) Infect. Immun. , vol.72 , Issue.2 , pp. 1155-1158
    • Halsey, T.A.1    Vazquez-Torres, A.2    Gravdahl, D.J.3    Fang, F.C.4    Libby, S.J.5
  • 10
    • 0345688910 scopus 로고    scopus 로고
    • Iron loading and erythrophagocytosis increase ferroportin 1 (FPN1) expression in J774 macrophages
    • Knutson, M.D., Vafa, M.R., Haile, D.J., Wessling-Resnick, M., Iron loading and erythrophagocytosis increase ferroportin 1 (FPN1) expression in J774 macrophages. Blood 102:12 (2003), 4191–4197.
    • (2003) Blood , vol.102 , Issue.12 , pp. 4191-4197
    • Knutson, M.D.1    Vafa, M.R.2    Haile, D.J.3    Wessling-Resnick, M.4
  • 12
    • 0033571363 scopus 로고    scopus 로고
    • H-ferritin subunit overexpression in erythroid cells reduces the oxidative stress response and induces multidrug resistance properties
    • Epsztejn, S., Glickstein, H., Picard, V., Slotki, I.N., Breuer, W., Beaumont, C., Cabantchik, Z.I., H-ferritin subunit overexpression in erythroid cells reduces the oxidative stress response and induces multidrug resistance properties. Blood 94:10 (1999), 3593–3603.
    • (1999) Blood , vol.94 , Issue.10 , pp. 3593-3603
    • Epsztejn, S.1    Glickstein, H.2    Picard, V.3    Slotki, I.N.4    Breuer, W.5    Beaumont, C.6    Cabantchik, Z.I.7
  • 14
    • 84880374389 scopus 로고    scopus 로고
    • Iron and citrate export by a major facilitator superfamily pump regulates metabolism and stress resistance in Salmonella Typhimurium
    • Frawley, E.R., Crouch, M.L., Bingham-Ramos, L.K., Robbins, H.F., Wang, W., Wright, G.D., Fang, F.C., Iron and citrate export by a major facilitator superfamily pump regulates metabolism and stress resistance in Salmonella Typhimurium. Proc. Natl. Acad. Sci. U. S. A. 110:29 (2013), 12054–12059.
    • (2013) Proc. Natl. Acad. Sci. U. S. A. , vol.110 , Issue.29 , pp. 12054-12059
    • Frawley, E.R.1    Crouch, M.L.2    Bingham-Ramos, L.K.3    Robbins, H.F.4    Wang, W.5    Wright, G.D.6    Fang, F.C.7
  • 15
    • 0029071068 scopus 로고
    • Genetic and redox determinants of nitric oxide cytotoxicity in a Salmonella typhimurium model
    • De Groote, M.A., Granger, D., Xu, Y., Campbell, G., Prince, R., Fang, F.C., Genetic and redox determinants of nitric oxide cytotoxicity in a Salmonella typhimurium model. Proc. Natl. Acad. Sci. U. S. A. 92:14 (1995), 6399–6403.
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , Issue.14 , pp. 6399-6403
    • De Groote, M.A.1    Granger, D.2    Xu, Y.3    Campbell, G.4    Prince, R.5    Fang, F.C.6
  • 17
    • 84860817569 scopus 로고    scopus 로고
    • DksA-dependent resistance of Salmonella enterica serovar Typhimurium against the antimicrobial activity of inducible nitric oxide synthase
    • Henard, C.A., Vazquez-Torres, A., DksA-dependent resistance of Salmonella enterica serovar Typhimurium against the antimicrobial activity of inducible nitric oxide synthase. Infect. Immun. 80:4 (2012), 1373–1380.
    • (2012) Infect. Immun. , vol.80 , Issue.4 , pp. 1373-1380
    • Henard, C.A.1    Vazquez-Torres, A.2
  • 18
    • 84884950378 scopus 로고    scopus 로고
    • The complex interplay of iron metabolism, reactive oxygen species, and reactive nitrogen species: insights into the potential of various iron therapies to induce oxidative and nitrosative stress
    • Koskenkorva-Frank, T.S., Weiss, G., Koppenol, W.H., Burckhardt, S., The complex interplay of iron metabolism, reactive oxygen species, and reactive nitrogen species: insights into the potential of various iron therapies to induce oxidative and nitrosative stress. Free Radic. Biol. Med. 65 (2013), 1174–1194.
    • (2013) Free Radic. Biol. Med. , vol.65 , pp. 1174-1194
    • Koskenkorva-Frank, T.S.1    Weiss, G.2    Koppenol, W.H.3    Burckhardt, S.4
  • 21
    • 84875150524 scopus 로고    scopus 로고
    • Heme and FLVCR-related transporter families SLC48 and SLC49
    • Khan, A.A., Quigley, J.G., Heme and FLVCR-related transporter families SLC48 and SLC49. Mol. Aspects Med. 34:2–3 (2013), 669–682.
    • (2013) Mol. Aspects Med. , vol.34 , Issue.2-3 , pp. 669-682
    • Khan, A.A.1    Quigley, J.G.2
  • 23
    • 33845497171 scopus 로고    scopus 로고
    • Haem carrier protein 1 (HCP1): expression and functional studies in cultured cells
    • Latunde-Dada, G.O., Takeuchi, K., Simpson, R.J., McKie, A.T., Haem carrier protein 1 (HCP1): expression and functional studies in cultured cells. FEBS Lett. 580:30 (2006), 6865–6870.
    • (2006) FEBS Lett. , vol.580 , Issue.30 , pp. 6865-6870
    • Latunde-Dada, G.O.1    Takeuchi, K.2    Simpson, R.J.3    McKie, A.T.4
  • 24
  • 29
    • 84904702237 scopus 로고    scopus 로고
    • Chaperone turns gatekeeper: PCBP2 and DMT1 form an iron-transport pipeline
    • Lane, D.J., Richardson, D.R., Chaperone turns gatekeeper: PCBP2 and DMT1 form an iron-transport pipeline. Biochem. J 462:1 (2014), e1–3.
    • (2014) Biochem. J , vol.462 , Issue.1 , pp. e1-3
    • Lane, D.J.1    Richardson, D.R.2
  • 30
    • 45849123222 scopus 로고    scopus 로고
    • A cytosolic iron chaperone that delivers iron to ferritin
    • Shi, H., Bencze, K.Z., Stemmler, T.L., Philpott, C.C., A cytosolic iron chaperone that delivers iron to ferritin. Science 320:5880 (2008), 1207–1210.
    • (2008) Science , vol.320 , Issue.5880 , pp. 1207-1210
    • Shi, H.1    Bencze, K.Z.2    Stemmler, T.L.3    Philpott, C.C.4
  • 31
    • 84982161525 scopus 로고    scopus 로고
    • Iron export through the transporter ferroportin 1 is modulated by the iron chaperone PCBP2
    • Yanatori, I., Richardson, D.R., Imada, K., Kishi, F., Iron export through the transporter ferroportin 1 is modulated by the iron chaperone PCBP2. J. Biol. Chem. 291:33 (2016), 17303–17318.
    • (2016) J. Biol. Chem. , vol.291 , Issue.33 , pp. 17303-17318
    • Yanatori, I.1    Richardson, D.R.2    Imada, K.3    Kishi, F.4
  • 32
    • 0042324650 scopus 로고    scopus 로고
    • Duodenal cytochrome b and hephaestin expression in patients with iron deficiency and hemochromatosis
    • Zoller, H., Theurl, I., Koch, R.O., McKie, A.T., Vogel, W., Weiss, G., Duodenal cytochrome b and hephaestin expression in patients with iron deficiency and hemochromatosis. Gastroenterology 125:3 (2003), 746–754.
    • (2003) Gastroenterology , vol.125 , Issue.3 , pp. 746-754
    • Zoller, H.1    Theurl, I.2    Koch, R.O.3    McKie, A.T.4    Vogel, W.5    Weiss, G.6
  • 33
    • 0041438849 scopus 로고    scopus 로고
    • Systemic regulation of Hephaestin and Ireg1 revealed in studies of genetic and nutritional iron deficiency
    • Chen, H., Su, T., Attieh, Z.K., Fox, T.C., McKie, A.T., Anderson, G.J., Vulpe, C.D., Systemic regulation of Hephaestin and Ireg1 revealed in studies of genetic and nutritional iron deficiency. Blood 102:5 (2003), 1893–1899.
    • (2003) Blood , vol.102 , Issue.5 , pp. 1893-1899
    • Chen, H.1    Su, T.2    Attieh, Z.K.3    Fox, T.C.4    McKie, A.T.5    Anderson, G.J.6    Vulpe, C.D.7
  • 38
    • 0037126002 scopus 로고    scopus 로고
    • Previously uncharacterized isoforms of divalent metal transporter (DMT)-1: implications for regulation and cellular function
    • Hubert, N., Hentze, M.W., Previously uncharacterized isoforms of divalent metal transporter (DMT)-1: implications for regulation and cellular function. Proc. Natl. Acad. Sci. U. S. A. 99:19 (2002), 12345–12350.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , Issue.19 , pp. 12345-12350
    • Hubert, N.1    Hentze, M.W.2
  • 39
    • 0033103978 scopus 로고    scopus 로고
    • The iron transport protein NRAMP2 is an integral membrane glycoprotein that colocalizes with transferrin in recycling endosomes
    • Gruenheid, S., Canonne-Hergaux, F., Gauthier, S., Hackam, D.J., Grinstein, S., Gros, P., The iron transport protein NRAMP2 is an integral membrane glycoprotein that colocalizes with transferrin in recycling endosomes. J. Exp. Med. 189:5 (1999), 831–841.
    • (1999) J. Exp. Med. , vol.189 , Issue.5 , pp. 831-841
    • Gruenheid, S.1    Canonne-Hergaux, F.2    Gauthier, S.3    Hackam, D.J.4    Grinstein, S.5    Gros, P.6
  • 40
    • 34547804359 scopus 로고    scopus 로고
    • On risks and benefits of iron supplementation recommendations for iron intake revisited
    • Schumann, K., Ettle, T., Szegner, B., Elsenhans, B., Solomons, N.W., On risks and benefits of iron supplementation recommendations for iron intake revisited. J. Trace Elem. Med. Biol. 21:3 (2007), 147–168.
    • (2007) J. Trace Elem. Med. Biol. , vol.21 , Issue.3 , pp. 147-168
    • Schumann, K.1    Ettle, T.2    Szegner, B.3    Elsenhans, B.4    Solomons, N.W.5
  • 41
    • 33748764432 scopus 로고    scopus 로고
    • Molecular and clinical aspects of iron homeostasis: from anemia to hemochromatosis
    • Nairz, M., Weiss, G., Molecular and clinical aspects of iron homeostasis: from anemia to hemochromatosis. Wien. Klin. Wochenschr. 118:15–16 (2006), 442–462.
    • (2006) Wien. Klin. Wochenschr. , vol.118 , Issue.15-16 , pp. 442-462
    • Nairz, M.1    Weiss, G.2
  • 42
    • 84860574815 scopus 로고    scopus 로고
    • Iron sensing and signalling
    • Evstatiev, R., Gasche, C., Iron sensing and signalling. Gut 61:6 (2012), 933–952.
    • (2012) Gut , vol.61 , Issue.6 , pp. 933-952
    • Evstatiev, R.1    Gasche, C.2
  • 43
    • 24744438847 scopus 로고    scopus 로고
    • The macrophage: a cellular factory at the interphase between iron and immunity for the control of infections
    • Theurl, I., Fritsche, G., Ludwiczek, S., Garimorth, K., Bellmann-Weiler, R., Weiss, G., The macrophage: a cellular factory at the interphase between iron and immunity for the control of infections. Biometals 18:4 (2005), 359–367.
    • (2005) Biometals , vol.18 , Issue.4 , pp. 359-367
    • Theurl, I.1    Fritsche, G.2    Ludwiczek, S.3    Garimorth, K.4    Bellmann-Weiler, R.5    Weiss, G.6
  • 44
    • 84866007988 scopus 로고    scopus 로고
    • Macrophages and systemic iron homeostasis
    • Ganz, T., Macrophages and systemic iron homeostasis. J. Innate Immun. 4:5–6 (2012), 446–453.
    • (2012) J. Innate Immun. , vol.4 , Issue.5-6 , pp. 446-453
    • Ganz, T.1
  • 46
    • 13444252281 scopus 로고    scopus 로고
    • Iron release from macrophages after erythrophagocytosis is up-regulated by ferroportin 1 overexpression and down-regulated by hepcidin
    • Knutson, M.D., Oukka, M., Koss, L.M., Aydemir, F., Wessling-Resnick, M., Iron release from macrophages after erythrophagocytosis is up-regulated by ferroportin 1 overexpression and down-regulated by hepcidin. Proc. Natl. Acad. Sci. U. S. A. 102:5 (2005), 1324–1328.
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , Issue.5 , pp. 1324-1328
    • Knutson, M.D.1    Oukka, M.2    Koss, L.M.3    Aydemir, F.4    Wessling-Resnick, M.5
  • 47
    • 24744458603 scopus 로고    scopus 로고
    • Synthetic hepcidin causes rapid dose-dependent hypoferremia and is concentrated in ferroportin-containing organs
    • Rivera, S., Nemeth, E., Gabayan, V., Lopez, M.A., Farshidi, D., Ganz, T., Synthetic hepcidin causes rapid dose-dependent hypoferremia and is concentrated in ferroportin-containing organs. Blood 106:6 (2005), 2196–2199.
    • (2005) Blood , vol.106 , Issue.6 , pp. 2196-2199
    • Rivera, S.1    Nemeth, E.2    Gabayan, V.3    Lopez, M.A.4    Farshidi, D.5    Ganz, T.6
  • 48
    • 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 306:5704 (2004), 2090–2093.
    • (2004) Science , vol.306 , Issue.5704 , 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
  • 51
    • 84892657750 scopus 로고    scopus 로고
    • The liver: conductor of systemic iron balance
    • Meynard, D., Babitt, J.L., Lin, H.Y., The liver: conductor of systemic iron balance. Blood 123:2 (2013), 168–176.
    • (2013) Blood , vol.123 , Issue.2 , pp. 168-176
    • Meynard, D.1    Babitt, J.L.2    Lin, H.Y.3
  • 52
    • 79959562083 scopus 로고    scopus 로고
    • Serum and liver iron differently regulate the bone morphogenetic protein 6 (BMP6)-SMAD signaling pathway in mice
    • Corradini, E., Meynard, D., Wu, Q., Chen, S., Ventura, P., Pietrangelo, A., Babitt, J.L., Serum and liver iron differently regulate the bone morphogenetic protein 6 (BMP6)-SMAD signaling pathway in mice. Hepatology 54:1 (2011), 273–284.
    • (2011) Hepatology , vol.54 , Issue.1 , pp. 273-284
    • Corradini, E.1    Meynard, D.2    Wu, Q.3    Chen, S.4    Ventura, P.5    Pietrangelo, A.6    Babitt, J.L.7
  • 53
    • 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. 7:3 (2008), 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
  • 55
    • 84867578495 scopus 로고    scopus 로고
    • The hemochromatosis proteins HFE TfR2, and HJV form a membrane-associated protein complex for hepcidin regulation
    • D'Alessio, F., Hentze, M.W., Muckenthaler, M.U., The hemochromatosis proteins HFE TfR2, and HJV form a membrane-associated protein complex for hepcidin regulation. J. Hepatol. 57:5 (2012), 1052–1060.
    • (2012) J. Hepatol. , vol.57 , Issue.5 , pp. 1052-1060
    • D'Alessio, F.1    Hentze, M.W.2    Muckenthaler, M.U.3
  • 56
    • 0842263988 scopus 로고    scopus 로고
    • Localization of iron metabolism-related mRNAs in rat liver indicate that HFE is expressed predominantly in hepatocytes
    • Zhang, A.S., Xiong, S., Tsukamoto, H., Enns, C.A., Localization of iron metabolism-related mRNAs in rat liver indicate that HFE is expressed predominantly in hepatocytes. Blood 103:4 (2004), 1509–1514.
    • (2004) Blood , vol.103 , Issue.4 , pp. 1509-1514
    • Zhang, A.S.1    Xiong, S.2    Tsukamoto, H.3    Enns, C.A.4
  • 57
    • 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. 350:23 (2004), 2383–2397.
    • (2004) N. Engl. J. Med. , vol.350 , Issue.23 , pp. 2383-2397
    • Pietrangelo, A.1
  • 58
    • 84856292277 scopus 로고    scopus 로고
    • Iron overload in human disease
    • Fleming, R.E., Ponka, P., Iron overload in human disease. N. Engl. J. Med. 366:4 (2012), 348–359.
    • (2012) N. Engl. J. Med. , vol.366 , Issue.4 , pp. 348-359
    • Fleming, R.E.1    Ponka, P.2
  • 59
    • 33846225653 scopus 로고    scopus 로고
    • Targeted disruption of the hepatic transferrin receptor 2 gene in mice leads to iron overload
    • Wallace, D.F., Summerville, L., Subramaniam, V.N., Targeted disruption of the hepatic transferrin receptor 2 gene in mice leads to iron overload. Gastroenterology 132:1 (2007), 301–310.
    • (2007) Gastroenterology , vol.132 , Issue.1 , pp. 301-310
    • Wallace, D.F.1    Summerville, L.2    Subramaniam, V.N.3
  • 63
    • 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. 117:7 (2007), 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
  • 64
    • 85030172960 scopus 로고    scopus 로고
    • Bone morphogenetic protein 2 controls iron homeostasis in mice independent of Bmp6
    • Canali, S., Wang, C.Y., Zumbrennen-Bullough, K.B., Bayer, A., Babitt, J.L., Bone morphogenetic protein 2 controls iron homeostasis in mice independent of Bmp6. Am. J. Hematol. 92:11 (2017), 1204–1213.
    • (2017) Am. J. Hematol. , vol.92 , Issue.11 , pp. 1204-1213
    • Canali, S.1    Wang, C.Y.2    Zumbrennen-Bullough, K.B.3    Bayer, A.4    Babitt, J.L.5
  • 66
    • 84903578007 scopus 로고    scopus 로고
    • Identification of erythroferrone as an erythroid regulator of iron metabolism
    • Kautz, L., Jung, G., Valore, E.V., Rivella, S., Nemeth, E., Ganz, T., Identification of erythroferrone as an erythroid regulator of iron metabolism. Nat. Genet. 46:7 (2014), 678–684.
    • (2014) Nat. Genet. , vol.46 , Issue.7 , pp. 678-684
    • Kautz, L.1    Jung, G.2    Valore, E.V.3    Rivella, S.4    Nemeth, E.5    Ganz, T.6
  • 67
    • 84944930727 scopus 로고    scopus 로고
    • Erythroferrone contributes to hepcidin suppression and iron overload in a mouse model of beta-thalassemia
    • Kautz, L., Jung, G., Du, X., Gabayan, V., Chapman, J., Nasoff, M., Nemeth, E., Ganz, T., Erythroferrone contributes to hepcidin suppression and iron overload in a mouse model of beta-thalassemia. Blood 126:17 (2015), 2031–2037.
    • (2015) Blood , vol.126 , Issue.17 , pp. 2031-2037
    • Kautz, L.1    Jung, G.2    Du, X.3    Gabayan, V.4    Chapman, J.5    Nasoff, M.6    Nemeth, E.7    Ganz, T.8
  • 69
    • 84856317888 scopus 로고    scopus 로고
    • The pleiotropic effects of erythropoietin in infection and inflammation
    • Nairz, M., Sonnweber, T., Schroll, A., Theurl, I., Weiss, G., The pleiotropic effects of erythropoietin in infection and inflammation. Microbes Infect. 14:3 (2012), 238–246.
    • (2012) Microbes Infect. , vol.14 , Issue.3 , pp. 238-246
    • Nairz, M.1    Sonnweber, T.2    Schroll, A.3    Theurl, I.4    Weiss, G.5
  • 70
    • 4644283464 scopus 로고    scopus 로고
    • Molecular biology of erythropoietin
    • Jelkmann, W., Molecular biology of erythropoietin. Intern. Med. 43:8 (2004), 649–659.
    • (2004) Intern. Med. , vol.43 , Issue.8 , pp. 649-659
    • Jelkmann, W.1
  • 71
    • 0033928280 scopus 로고    scopus 로고
    • Erythroid progenitors differentiate and mature in response to endogenous erythropoietin
    • Sato, T., Maekawa, T., Watanabe, S., Tsuji, K., Nakahata, T., Erythroid progenitors differentiate and mature in response to endogenous erythropoietin. J. Clin. Invest. 106:2 (2000), 263–270.
    • (2000) J. Clin. Invest. , vol.106 , Issue.2 , pp. 263-270
    • Sato, T.1    Maekawa, T.2    Watanabe, S.3    Tsuji, K.4    Nakahata, T.5
  • 72
    • 0037046801 scopus 로고    scopus 로고
    • Apoptosis protection by the Epo target Bcl-X(L) allows factor-independent differentiation of primary erythroblasts
    • Dolznig, H., Habermann, B., Stangl, K., Deiner, E.M., Moriggl, R., Beug, H., Mullner, E.W., Apoptosis protection by the Epo target Bcl-X(L) allows factor-independent differentiation of primary erythroblasts. Curr. Biol. 12:13 (2002), 1076–1085.
    • (2002) Curr. Biol. , vol.12 , Issue.13 , pp. 1076-1085
    • Dolznig, H.1    Habermann, B.2    Stangl, K.3    Deiner, E.M.4    Moriggl, R.5    Beug, H.6    Mullner, E.W.7
  • 73
    • 84906086078 scopus 로고    scopus 로고
    • Intestinal inflammation modulates expression of the iron-regulating hormone hepcidin depending on erythropoietic activity and the commensal microbiota
    • Shanmugam, N.K., Trebicka, E., Fu, L.L., Shi, H.N., Cherayil, B.J., Intestinal inflammation modulates expression of the iron-regulating hormone hepcidin depending on erythropoietic activity and the commensal microbiota. J. Immunol. 193:3 (2014), 1398–1407.
    • (2014) J. Immunol. , vol.193 , Issue.3 , pp. 1398-1407
    • Shanmugam, N.K.1    Trebicka, E.2    Fu, L.L.3    Shi, H.N.4    Cherayil, B.J.5
  • 75
    • 47049116150 scopus 로고    scopus 로고
    • Erythropoietin mediates hepcidin expression in hepatocytes through EPOR signaling and regulation of C/EBPalpha
    • Pinto, J.P., Ribeiro, S., Pontes, H., Thowfeequ, S., Tosh, D., Carvalho, F., Porto, G., Erythropoietin mediates hepcidin expression in hepatocytes through EPOR signaling and regulation of C/EBPalpha. Blood 111:12 (2008), 5727–5733.
    • (2008) Blood , vol.111 , Issue.12 , pp. 5727-5733
    • Pinto, J.P.1    Ribeiro, S.2    Pontes, H.3    Thowfeequ, S.4    Tosh, D.5    Carvalho, F.6    Porto, G.7
  • 76
    • 58149158218 scopus 로고    scopus 로고
    • CD47 on experimentally senescent murine RBCs inhibits phagocytosis following Fcgamma receptor-mediated but not scavenger receptor-mediated recognition by macrophages
    • Olsson, M., Oldenborg, P.A., CD47 on experimentally senescent murine RBCs inhibits phagocytosis following Fcgamma receptor-mediated but not scavenger receptor-mediated recognition by macrophages. Blood 112:10 (2008), 4259–4267.
    • (2008) Blood , vol.112 , Issue.10 , pp. 4259-4267
    • Olsson, M.1    Oldenborg, P.A.2
  • 77
    • 84944676154 scopus 로고    scopus 로고
    • Splenic dendritic cells survey red blood cells for missing self-CD47 to trigger adaptive immune responses
    • Yi, T., Li, J., Chen, H., Wu, J., An, J., Xu, Y., Hu, Y., Lowell, C.A., Cyster, J.G., Splenic dendritic cells survey red blood cells for missing self-CD47 to trigger adaptive immune responses. Immunity 43:4 (2015), 764–775.
    • (2015) Immunity , vol.43 , Issue.4 , pp. 764-775
    • Yi, T.1    Li, J.2    Chen, H.3    Wu, J.4    An, J.5    Xu, Y.6    Hu, Y.7    Lowell, C.A.8    Cyster, J.G.9
  • 78
    • 0035794312 scopus 로고    scopus 로고
    • CD47-signal regulatory protein alpha (SIRPalpha) regulates Fcgamma and complement receptor-mediated phagocytosis
    • Oldenborg, P.A., Gresham, H.D., Lindberg, F.P., CD47-signal regulatory protein alpha (SIRPalpha) regulates Fcgamma and complement receptor-mediated phagocytosis. J. Exp. Med. 193:7 (2001), 855–862.
    • (2001) J. Exp. Med. , vol.193 , Issue.7 , pp. 855-862
    • Oldenborg, P.A.1    Gresham, H.D.2    Lindberg, F.P.3
  • 79
    • 0034653976 scopus 로고    scopus 로고
    • Scavenger receptors on liver Kupffer cells mediate the in vivo uptake of oxidatively damaged red blood cells in mice
    • Terpstra, V., van Berkel, T.J., Scavenger receptors on liver Kupffer cells mediate the in vivo uptake of oxidatively damaged red blood cells in mice. Blood 95:6 (2000), 2157–2163.
    • (2000) Blood , vol.95 , Issue.6 , pp. 2157-2163
    • Terpstra, V.1    van Berkel, T.J.2
  • 85
    • 0030886381 scopus 로고    scopus 로고
    • Heme oxygenase 1 is required for mammalian iron reutilization
    • Poss, K.D., Tonegawa, S., Heme oxygenase 1 is required for mammalian iron reutilization. Proc. Natl. Acad. Sci. U. S. A. 94:20 (1997), 10919–10924.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , Issue.20 , pp. 10919-10924
    • Poss, K.D.1    Tonegawa, S.2
  • 86
    • 0037093202 scopus 로고    scopus 로고
    • Regulation of ferritin genes and protein
    • Torti, F.M., Torti, S.V., Regulation of ferritin genes and protein. Blood 99:10 (2002), 3505–3516.
    • (2002) Blood , vol.99 , Issue.10 , pp. 3505-3516
    • Torti, F.M.1    Torti, S.V.2
  • 90
    • 0029055581 scopus 로고
    • Rapid responses to oxidative stress mediated by iron regulatory protein
    • Pantopoulos, K., Hentze, M.W., Rapid responses to oxidative stress mediated by iron regulatory protein. EMBO J. 14:12 (1995), 2917–2924.
    • (1995) EMBO J. , vol.14 , Issue.12 , pp. 2917-2924
    • Pantopoulos, K.1    Hentze, M.W.2
  • 91
    • 0029960279 scopus 로고    scopus 로고
    • Ferritin translation by interleukin-1and interleukin-6: the role of sequences upstream of the start codons of the heavy and light subunit genes
    • Rogers, J.T., Ferritin translation by interleukin-1and interleukin-6: the role of sequences upstream of the start codons of the heavy and light subunit genes. Blood 87:6 (1996), 2525–2537.
    • (1996) Blood , vol.87 , Issue.6 , pp. 2525-2537
    • Rogers, J.T.1
  • 92
    • 80051840004 scopus 로고    scopus 로고
    • Iron uptake mediated by binding of H-ferritin to the TIM-2 receptor in mouse cells
    • Han, J., Seaman, W.E., Di, X., Wang, W., Willingham, M., Torti, F.M., Torti, S.V., Iron uptake mediated by binding of H-ferritin to the TIM-2 receptor in mouse cells. PLoS One, 6(8), 2011, e23800.
    • (2011) PLoS One , vol.6 , Issue.8 , pp. e23800
    • Han, J.1    Seaman, W.E.2    Di, X.3    Wang, W.4    Willingham, M.5    Torti, F.M.6    Torti, S.V.7
  • 98
    • 0022335256 scopus 로고
    • Binding of horse-spleen ferritin to group A streptococci
    • Ryc, M., Wagner, B., Wagner, M., Petras, P., Havlicek, J., Binding of horse-spleen ferritin to group A streptococci. Microbios 4:181S (1985), 261–269.
    • (1985) Microbios , vol.4 , Issue.181S , pp. 261-269
    • Ryc, M.1    Wagner, B.2    Wagner, M.3    Petras, P.4    Havlicek, J.5
  • 100
    • 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. 53:3 (2004), 807–820.
    • (2004) Mol. Microbiol. , vol.53 , Issue.3 , pp. 807-820
    • Larson, J.A.1    Howie, H.L.2    So, M.3
  • 101
    • 33645049000 scopus 로고    scopus 로고
    • Iron acquisition systems for ferric hydroxamates haemin and haemoglobin in Listeria monocytogenes
    • Jin, B., Newton, S.M., Shao, Y., Jiang, X., Charbit, A., Klebba, P.E., Iron acquisition systems for ferric hydroxamates haemin and haemoglobin in Listeria monocytogenes. Mol. Microbiol. 59:4 (2006), 1185–1198.
    • (2006) Mol. Microbiol. , vol.59 , Issue.4 , pp. 1185-1198
    • Jin, B.1    Newton, S.M.2    Shao, Y.3    Jiang, X.4    Charbit, A.5    Klebba, P.E.6
  • 103
    • 77953713414 scopus 로고    scopus 로고
    • Heme controls ferroportin1 (FPN1) transcription involving Bach1 Nrf2 and a MARE/ARE sequence motif at position -7007 of the FPN1 promoter
    • Marro, S., Chiabrando, D., Messana, E., Stolte, J., Turco, E., Tolosano, E., Muckenthaler, M.U., Heme controls ferroportin1 (FPN1) transcription involving Bach1 Nrf2 and a MARE/ARE sequence motif at position -7007 of the FPN1 promoter. Haematologica 95:8 (2010), 1261–1268.
    • (2010) Haematologica , vol.95 , Issue.8 , pp. 1261-1268
    • Marro, S.1    Chiabrando, D.2    Messana, E.3    Stolte, J.4    Turco, E.5    Tolosano, E.6    Muckenthaler, M.U.7
  • 104
    • 0142126132 scopus 로고    scopus 로고
    • Mechanisms of iron mediated regulation of the duodenal iron transporters divalent metal transporter 1 and ferroportin 1
    • Zoller, H., Theurl, I., Koch, R., Kaser, A., Weiss, G., Mechanisms of iron mediated regulation of the duodenal iron transporters divalent metal transporter 1 and ferroportin 1. Blood Cells. Mol. Dis. 29:3 (2002), 488–497.
    • (2002) Blood Cells. Mol. Dis. , vol.29 , Issue.3 , pp. 488-497
    • Zoller, H.1    Theurl, I.2    Koch, R.3    Kaser, A.4    Weiss, G.5
  • 105
    • 10844282789 scopus 로고    scopus 로고
    • Mammalian tissue oxygen levels modulate iron-regulatory protein activities in vivo
    • Meyron-Holtz, E.G., Ghosh, M.C., Rouault, T.A., Mammalian tissue oxygen levels modulate iron-regulatory protein activities in vivo. Science 306:5704 (2004), 2087–2090.
    • (2004) Science , vol.306 , Issue.5704 , pp. 2087-2090
    • Meyron-Holtz, E.G.1    Ghosh, M.C.2    Rouault, T.A.3
  • 107
    • 50949102412 scopus 로고    scopus 로고
    • Systemic iron homeostasis and the iron-responsive element/iron-regulatory protein (IRE/IRP) regulatory network
    • Muckenthaler, M.U., Galy, B., Hentze, M.W., Systemic iron homeostasis and the iron-responsive element/iron-regulatory protein (IRE/IRP) regulatory network. Annu. Rev. Nutr. 28 (2008), 197–213.
    • (2008) Annu. Rev. Nutr. , vol.28 , pp. 197-213
    • Muckenthaler, M.U.1    Galy, B.2    Hentze, M.W.3
  • 108
    • 0037926880 scopus 로고    scopus 로고
    • Cytokine-mediated regulation of iron transport in human monocytic cells
    • Ludwiczek, S., Aigner, E., Theurl, I., Weiss, G., Cytokine-mediated regulation of iron transport in human monocytic cells. Blood 101:10 (2003), 4148–4154.
    • (2003) Blood , vol.101 , Issue.10 , pp. 4148-4154
    • Ludwiczek, S.1    Aigner, E.2    Theurl, I.3    Weiss, G.4
  • 109
    • 29244492306 scopus 로고    scopus 로고
    • A cell-surface receptor for lipocalin 24p3 selectively mediates apoptosis and iron uptake
    • Devireddy, L.R., Gazin, C., Zhu, X., Green, M.R., A cell-surface receptor for lipocalin 24p3 selectively mediates apoptosis and iron uptake. Cell 123:7 (2005), 1293–1305.
    • (2005) Cell , vol.123 , Issue.7 , pp. 1293-1305
    • Devireddy, L.R.1    Gazin, C.2    Zhu, X.3    Green, M.R.4
  • 110
    • 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 141:6 (2010), 1006–1017.
    • (2010) Cell , vol.141 , Issue.6 , pp. 1006-1017
    • Devireddy, L.R.1    Hart, D.O.2    Goetz, D.H.3    Green, M.R.4
  • 111
    • 84901797293 scopus 로고    scopus 로고
    • Endogenous siderophore 2, 5-dihydroxybenzoic acid deficiency promotes anemia and splenic iron overload in mice
    • Liu, Z., Ciocea, A., Devireddy, L., Endogenous siderophore 2, 5-dihydroxybenzoic acid deficiency promotes anemia and splenic iron overload in mice. Mol. Cell. Biol. 34:13 (2014), 2533–2546.
    • (2014) Mol. Cell. Biol. , vol.34 , Issue.13 , pp. 2533-2546
    • Liu, Z.1    Ciocea, A.2    Devireddy, L.3
  • 113
    • 84922426001 scopus 로고    scopus 로고
    • ‘Ride on the ferrous wheel’-the cycle of iron in macrophages in health and disease
    • Nairz, M., Schroll, A., Demetz, E., Tancevski, I., Theurl, I., Weiss, G., ‘Ride on the ferrous wheel’-the cycle of iron in macrophages in health and disease. Immunobiology 220:2 (2015), 280–294.
    • (2015) Immunobiology , vol.220 , Issue.2 , pp. 280-294
    • Nairz, M.1    Schroll, A.2    Demetz, E.3    Tancevski, I.4    Theurl, I.5    Weiss, G.6
  • 115
    • 0022461970 scopus 로고
    • Murine cytotoxic activated macrophages inhibit aconitase in tumor cells. Inhibition involves the iron-sulfur prosthetic group and is reversible
    • Drapier, J.C., Hibbs, J.B. Jr., Murine cytotoxic activated macrophages inhibit aconitase in tumor cells. Inhibition involves the iron-sulfur prosthetic group and is reversible. J. Clin. Invest. 78:3 (1986), 790–797.
    • (1986) J. Clin. Invest. , vol.78 , Issue.3 , pp. 790-797
    • Drapier, J.C.1    Hibbs, J.B.2
  • 116
    • 0027301897 scopus 로고
    • Biosynthesis of nitric oxide activates iron regulatory factor in macrophages
    • Drapier, J.C., Hirling, H., Wietzerbin, J., Kaldy, P., Kuhn, L.C., Biosynthesis of nitric oxide activates iron regulatory factor in macrophages. EMBO J. 12:9 (1993), 3643–3649.
    • (1993) EMBO J. , vol.12 , Issue.9 , pp. 3643-3649
    • Drapier, J.C.1    Hirling, H.2    Wietzerbin, J.3    Kaldy, P.4    Kuhn, L.C.5
  • 117
    • 0028784211 scopus 로고
    • The effect of redox-related species of nitrogen monoxide on transferrin and iron uptake and cellular proliferation of erythroleukemia (K562) cells
    • Richardson, D.R., Neumannova, V., Nagy, E., Ponka, P., The effect of redox-related species of nitrogen monoxide on transferrin and iron uptake and cellular proliferation of erythroleukemia (K562) cells. Blood 86:8 (1995), 3211–3219.
    • (1995) Blood , vol.86 , Issue.8 , pp. 3211-3219
    • Richardson, D.R.1    Neumannova, V.2    Nagy, E.3    Ponka, P.4
  • 118
  • 119
    • 0033563095 scopus 로고    scopus 로고
    • Central role of transcription factor NF-IL6 for cytokine and iron-mediated regulation of murine inducible nitric oxide synthase expression
    • Dlaska, M., Weiss, G., Central role of transcription factor NF-IL6 for cytokine and iron-mediated regulation of murine inducible nitric oxide synthase expression. J. Immunol. 162:10 (1999), 6171–6177.
    • (1999) J. Immunol. , vol.162 , Issue.10 , pp. 6171-6177
    • Dlaska, M.1    Weiss, G.2
  • 120
    • 0030911247 scopus 로고    scopus 로고
    • Functional requirement of the hypoxia-responsive element in the activation of the inducible nitric oxide synthase promoter by the iron chelator desferrioxamine
    • Melillo, G., Taylor, L.S., Brooks, A., Musso, T., Cox, G.W., Varesio, L., Functional requirement of the hypoxia-responsive element in the activation of the inducible nitric oxide synthase promoter by the iron chelator desferrioxamine. J. Biol. Chem. 272:18 (1997), 12236–12243.
    • (1997) J. Biol. Chem. , vol.272 , Issue.18 , pp. 12236-12243
    • Melillo, G.1    Taylor, L.S.2    Brooks, A.3    Musso, T.4    Cox, G.W.5    Varesio, L.6
  • 121
    • 85007610433 scopus 로고    scopus 로고
    • A nitric oxide storage and transport system that protects activated macrophages from endogenous nitric oxide cytotoxicity
    • Lok, H.C., Sahni, S., Jansson, P.J., Kovacevic, Z., Hawkins, C.L., Richardson, D.R., A nitric oxide storage and transport system that protects activated macrophages from endogenous nitric oxide cytotoxicity. J. Biol. Chem. 291:53 (2016), 27042–27061.
    • (2016) J. Biol. Chem. , vol.291 , Issue.53 , pp. 27042-27061
    • Lok, H.C.1    Sahni, S.2    Jansson, P.J.3    Kovacevic, Z.4    Hawkins, C.L.5    Richardson, D.R.6
  • 122
    • 85014074992 scopus 로고    scopus 로고
    • Pumping iron-how macrophages handle iron at the systemic, microenvironmental, and cellular levels
    • Nairz, M., Theurl, I., Swirski, F.K., Weiss, G., Pumping iron-how macrophages handle iron at the systemic, microenvironmental, and cellular levels. Pflugers Arch. 469:3–4 (2017), 397–418.
    • (2017) Pflugers Arch. , vol.469 , Issue.3-4 , pp. 397-418
    • Nairz, M.1    Theurl, I.2    Swirski, F.K.3    Weiss, G.4
  • 123
    • 0019161779 scopus 로고
    • The role of superoxide in the destruction of erythrocyte targets by human neutrophils
    • Weiss, S.J., The role of superoxide in the destruction of erythrocyte targets by human neutrophils. J. Biol. Chem. 255:20 (1980), 9912–9917.
    • (1980) J. Biol. Chem. , vol.255 , Issue.20 , pp. 9912-9917
    • Weiss, S.J.1
  • 124
    • 84862316869 scopus 로고    scopus 로고
    • Alteration of intracellular secretory acute phase response proteins expressed in human hepatocyte induced by exposure with interleukin-6
    • Nakata, K., Saitoh, R., Amano, J., Koshiyama, A., Ichibangase, T., Murao, N., Ohta, K., Aso, Y., Ishigai, M., Imai, K., Alteration of intracellular secretory acute phase response proteins expressed in human hepatocyte induced by exposure with interleukin-6. Cytokine 59:2 (2012), 317–323.
    • (2012) Cytokine , vol.59 , Issue.2 , pp. 317-323
    • Nakata, K.1    Saitoh, R.2    Amano, J.3    Koshiyama, A.4    Ichibangase, T.5    Murao, N.6    Ohta, K.7    Aso, Y.8    Ishigai, M.9    Imai, K.10
  • 126
    • 30144435054 scopus 로고    scopus 로고
    • CD163 is the macrophage scavenger receptor for native and chemically modified hemoglobins in the absence of haptoglobin
    • Schaer, D.J., Schaer, C.A., Buehler, P.W., Boykins, R.A., Schoedon, G., Alayash, A.I., Schaffner, A., CD163 is the macrophage scavenger receptor for native and chemically modified hemoglobins in the absence of haptoglobin. Blood 107:1 (2006), 373–380.
    • (2006) Blood , vol.107 , Issue.1 , pp. 373-380
    • Schaer, D.J.1    Schaer, C.A.2    Buehler, P.W.3    Boykins, R.A.4    Schoedon, G.5    Alayash, A.I.6    Schaffner, A.7
  • 130
    • 84903643644 scopus 로고    scopus 로고
    • Investigating the real role of HIF-1 and HIF-2 in iron recycling by macrophages
    • Mathieu, J.R., Heinis, M., Zumerle, S., Delga, S., Le Bon, A., Peyssonnaux, C., Investigating the real role of HIF-1 and HIF-2 in iron recycling by macrophages. Haematologica 99:7 (2016), e112–4.
    • (2016) Haematologica , vol.99 , Issue.7 , pp. e112-4
    • Mathieu, J.R.1    Heinis, M.2    Zumerle, S.3    Delga, S.4    Le Bon, A.5    Peyssonnaux, C.6
  • 131
    • 84921284050 scopus 로고    scopus 로고
    • Liver-resident macrophage necroptosis orchestrates type 1 microbicidal inflammation and type-2-mediated tissue repair during bacterial infection
    • Bleriot, C., Dupuis, T., Jouvion, G., Eberl, G., Disson, O., Lecuit, M., Liver-resident macrophage necroptosis orchestrates type 1 microbicidal inflammation and type-2-mediated tissue repair during bacterial infection. Immunity 42:1 (2014), 145–158.
    • (2014) Immunity , vol.42 , Issue.1 , pp. 145-158
    • Bleriot, C.1    Dupuis, T.2    Jouvion, G.3    Eberl, G.4    Disson, O.5    Lecuit, M.6
  • 133
    • 0036127426 scopus 로고    scopus 로고
    • Heme oxygenase-1 mediates the anti-inflammatory effect of interleukin-10 in mice
    • Lee, T.S., Chau, L.Y., Heme oxygenase-1 mediates the anti-inflammatory effect of interleukin-10 in mice. Nat. Med. 8:3 (2002), 240–246.
    • (2002) Nat. Med. , vol.8 , Issue.3 , pp. 240-246
    • Lee, T.S.1    Chau, L.Y.2
  • 137
    • 77955412821 scopus 로고    scopus 로고
    • Heme oxygenase-1 expression in M-CSF-polarized M2 macrophages contributes to LPS-induced IL-10 release
    • Sierra-Filardi, E., Vega, M.A., Sanchez-Mateos, P., Corbi, A.L., Puig-Kroger, A., Heme oxygenase-1 expression in M-CSF-polarized M2 macrophages contributes to LPS-induced IL-10 release. Immunobiology 215:9–10 (2010), 788–795.
    • (2010) Immunobiology , vol.215 , Issue.9-10 , pp. 788-795
    • Sierra-Filardi, E.1    Vega, M.A.2    Sanchez-Mateos, P.3    Corbi, A.L.4    Puig-Kroger, A.5
  • 138
    • 84901298804 scopus 로고    scopus 로고
    • Malaria parasite infection compromises control of concurrent systemic non-typhoidal Salmonella infection via IL-10-mediated alteration of myeloid cell function
    • Lokken, K.L., Mooney, J.P., Butler, B.P., Xavier, M.N., Chau, J.Y., Schaltenberg, N., Begum, R.H., Muller, W., Luckhart, S., Tsolis, R.M., Malaria parasite infection compromises control of concurrent systemic non-typhoidal Salmonella infection via IL-10-mediated alteration of myeloid cell function. PLoS Pathog., 10(5), 2014, e1004049.
    • (2014) PLoS Pathog. , vol.10 , Issue.5 , pp. e1004049
    • Lokken, K.L.1    Mooney, J.P.2    Butler, B.P.3    Xavier, M.N.4    Chau, J.Y.5    Schaltenberg, N.6    Begum, R.H.7    Muller, W.8    Luckhart, S.9    Tsolis, R.M.10
  • 142
    • 84936745321 scopus 로고    scopus 로고
    • NK-, NKT- and CD8-derived IFNgamma drives myeloid cell activation and erythrophagocytosis, resulting in trypanosomosis-associated acute anemia
    • Cnops, J., De Trez, C., Stijlemans, B., Keirsse, J., Kauffmann, F., Barkhuizen, M., Keeton, R., Boon, L., Brombacher, F., Magez, S., NK-, NKT- and CD8-derived IFNgamma drives myeloid cell activation and erythrophagocytosis, resulting in trypanosomosis-associated acute anemia. PLoS Pathog., 11(6), 2015, e1004964.
    • (2015) PLoS Pathog. , vol.11 , Issue.6 , pp. e1004964
    • Cnops, J.1    De Trez, C.2    Stijlemans, B.3    Keirsse, J.4    Kauffmann, F.5    Barkhuizen, M.6    Keeton, R.7    Boon, L.8    Brombacher, F.9    Magez, S.10
  • 143
    • 0038662619 scopus 로고    scopus 로고
    • Hepcidin, a putative mediator of anemia of inflammation, is a type II acute-phase protein
    • Nemeth, E., Valore, E.V., Territo, M., Schiller, G., Lichtenstein, A., Ganz, T., Hepcidin, a putative mediator of anemia of inflammation, is a type II acute-phase protein. Blood 101:7 (2003), 2461–2463.
    • (2003) Blood , vol.101 , Issue.7 , pp. 2461-2463
    • Nemeth, E.1    Valore, E.V.2    Territo, M.3    Schiller, G.4    Lichtenstein, A.5    Ganz, T.6
  • 145
    • 33646427702 scopus 로고    scopus 로고
    • TLR-4 dependent hepcidin expression by myeloid cells in response to bacterial pathogens
    • Peyssonnaux, C., Zinkernagel, A.S., Datta, V., Lauth, X., Johnson, R.S., Nizet, V., TLR-4 dependent hepcidin expression by myeloid cells in response to bacterial pathogens. Blood 107:9 (2006), 3727–3732.
    • (2006) Blood , vol.107 , Issue.9 , pp. 3727-3732
    • Peyssonnaux, C.1    Zinkernagel, A.S.2    Datta, V.3    Lauth, X.4    Johnson, R.S.5    Nizet, V.6
  • 146
    • 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. 113:9 (2004), 1271–1276.
    • (2004) J. Clin. Invest. , vol.113 , Issue.9 , 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
  • 147
    • 84892956031 scopus 로고    scopus 로고
    • Hepcidin induction by pathogens and pathogen-derived molecules is strongly dependent on interleukin-6
    • Rodriguez, R., Jung, C.L., Gabayan, V., Deng, J.C., Ganz, T., Nemeth, E., Bulut, Y., Hepcidin induction by pathogens and pathogen-derived molecules is strongly dependent on interleukin-6. Infect. Immun. 82:2 (2014), 745–752.
    • (2014) Infect. Immun. , vol.82 , Issue.2 , pp. 745-752
    • Rodriguez, R.1    Jung, C.L.2    Gabayan, V.3    Deng, J.C.4    Ganz, T.5    Nemeth, E.6    Bulut, Y.7
  • 151
    • 84960540727 scopus 로고    scopus 로고
    • Activin B induces noncanonical SMAD1/5/8 signaling via BMP type I receptors in hepatocytes: evidence for a role in hepcidin induction by inflammation in male mice
    • Canali, S., Core, A.B., Zumbrennen-Bullough, K.B., Merkulova, M., Wang, C.Y., Schneyer, A.L., Pietrangelo, A., Babitt, J.L., Activin B induces noncanonical SMAD1/5/8 signaling via BMP type I receptors in hepatocytes: evidence for a role in hepcidin induction by inflammation in male mice. Endocrinology 157:3 (2016), 1146–1162.
    • (2016) Endocrinology , vol.157 , Issue.3 , pp. 1146-1162
    • Canali, S.1    Core, A.B.2    Zumbrennen-Bullough, K.B.3    Merkulova, M.4    Wang, C.Y.5    Schneyer, A.L.6    Pietrangelo, A.7    Babitt, J.L.8
  • 152
    • 85020934597 scopus 로고    scopus 로고
    • Interleukin-1beta (IL-1beta) transcriptionally activates hepcidin by inducing CCAAT enhancer-binding protein delta (C/EBPdelta) expression in hepatocytes
    • Kanamori, Y., Murakami, M., Sugiyama, M., Hashimoto, O., Matsui, T., Funaba, M., Interleukin-1beta (IL-1beta) transcriptionally activates hepcidin by inducing CCAAT enhancer-binding protein delta (C/EBPdelta) expression in hepatocytes. J. Biol. Chem. 292:24 (2017), 10275–10287.
    • (2017) J. Biol. Chem. , vol.292 , Issue.24 , pp. 10275-10287
    • Kanamori, Y.1    Murakami, M.2    Sugiyama, M.3    Hashimoto, O.4    Matsui, T.5    Funaba, M.6
  • 153
    • 85034838754 scopus 로고    scopus 로고
    • Deletion of BMP6 worsens the phenotype of HJV-deficient mice and attenuates hepcidin levels reached after LPS challenge
    • Latour, C., Besson-Fournier, C., Gourbeyre, O., Meynard, D., Roth, M.P., Coppin, H., Deletion of BMP6 worsens the phenotype of HJV-deficient mice and attenuates hepcidin levels reached after LPS challenge. Blood 130:21 (2017), 2339–2343.
    • (2017) Blood , vol.130 , Issue.21 , pp. 2339-2343
    • Latour, C.1    Besson-Fournier, C.2    Gourbeyre, O.3    Meynard, D.4    Roth, M.P.5    Coppin, H.6
  • 158
    • 21544449756 scopus 로고    scopus 로고
    • Regulation of hepcidin and ferroportin expression by lipopolysaccharide in splenic macrophages
    • Liu, X.B., Nguyen, N.B., Marquess, K.D., Yang, F., Haile, D.J., Regulation of hepcidin and ferroportin expression by lipopolysaccharide in splenic macrophages. Blood Cells. Mol. Dis., 2005.
    • (2005) Blood Cells. Mol. Dis.
    • Liu, X.B.1    Nguyen, N.B.2    Marquess, K.D.3    Yang, F.4    Haile, D.J.5
  • 159
    • 0037131264 scopus 로고    scopus 로고
    • Regulation of reticuloendothelial iron transporter MTP1 (Slc11a3) by inflammation
    • Yang, F., Liu, X.B., Quinones, M., Melby, P.C., Ghio, A., Haile, D.J., Regulation of reticuloendothelial iron transporter MTP1 (Slc11a3) by inflammation. J. Biol. Chem. 277:42 (2002), 39786–39791.
    • (2002) J. Biol. Chem. , vol.277 , Issue.42 , pp. 39786-39791
    • Yang, F.1    Liu, X.B.2    Quinones, M.3    Melby, P.C.4    Ghio, A.5    Haile, D.J.6
  • 162
    • 0030666932 scopus 로고    scopus 로고
    • Interleukin-8 can mediate acute-phase protein production by isolated human hepatocytes
    • Wigmore, S.J., Fearon, K.C., Maingay, J.P., Lai, P.B., Ross, J.A., Interleukin-8 can mediate acute-phase protein production by isolated human hepatocytes. Am. J. Physiol. 73:4 Pt 1 (1997), E720–6.
    • (1997) Am. J. Physiol. , vol.73 , Issue.4 , pp. E720-6
    • Wigmore, S.J.1    Fearon, K.C.2    Maingay, J.P.3    Lai, P.B.4    Ross, J.A.5
  • 165
    • 78650736463 scopus 로고    scopus 로고
    • Role of the Yersinia pestis yersiniabactin iron acquisition system in the incidence of flea-borne plague
    • Sebbane, F., Jarrett, C., Gardner, D., Long, D., Hinnebusch, B.J., Role of the Yersinia pestis yersiniabactin iron acquisition system in the incidence of flea-borne plague. PLoS One, 5(12), 2016, e14379.
    • (2016) PLoS One , vol.5 , Issue.12 , pp. e14379
    • Sebbane, F.1    Jarrett, C.2    Gardner, D.3    Long, D.4    Hinnebusch, B.J.5
  • 166
    • 0036734286 scopus 로고    scopus 로고
    • Epidemic pathogenic selection: an explanation for hereditary hemochromatosis?
    • Moalem, S., Percy, M.E., Kruck, T.P., Gelbart, R.R., Epidemic pathogenic selection: an explanation for hereditary hemochromatosis?. Med. Hypotheses 59:3 (2002), 325–329.
    • (2002) Med. Hypotheses , vol.59 , Issue.3 , pp. 325-329
    • Moalem, S.1    Percy, M.E.2    Kruck, T.P.3    Gelbart, R.R.4
  • 167
    • 79961121513 scopus 로고    scopus 로고
    • Klebsiella pneumoniae yersiniabactin promotes respiratory tract infection through evasion of lipocalin 2
    • Bachman, M.A., Oyler, J.E., Burns, S.H., Caza, M., Lepine, F., Dozois, C.M., Weiser, J.N., Klebsiella pneumoniae yersiniabactin promotes respiratory tract infection through evasion of lipocalin 2. Infect. Immun. 79:8 (2011), 3309–3316.
    • (2011) Infect. Immun. , vol.79 , Issue.8 , pp. 3309-3316
    • Bachman, M.A.1    Oyler, J.E.2    Burns, S.H.3    Caza, M.4    Lepine, F.5    Dozois, C.M.6    Weiser, J.N.7
  • 168
    • 0036070597 scopus 로고    scopus 로고
    • Characterization of pit a Streptococcus pneumoniae iron uptake ABC transporter
    • Brown, J.S., Gilliland, S.M., Ruiz-Albert, J., Holden, D.W., Characterization of pit a Streptococcus pneumoniae iron uptake ABC transporter. Infect. Immun. 70:8 (2002), 4389–4398.
    • (2002) Infect. Immun. , vol.70 , Issue.8 , pp. 4389-4398
    • Brown, J.S.1    Gilliland, S.M.2    Ruiz-Albert, J.3    Holden, D.W.4
  • 169
    • 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 305:5690 (2004), 1626–1628.
    • (2004) Science , vol.305 , Issue.5690 , pp. 1626-1628
    • Skaar, E.P.1    Humayun, M.2    Bae, T.3    DeBord, K.L.4    Schneewind, O.5
  • 170
    • 0029846868 scopus 로고    scopus 로고
    • Acquisition of iron from host proteins by the group A streptococcus
    • Eichenbaum, Z., Muller, E., Morse, S.A., Scott, J.R., Acquisition of iron from host proteins by the group A streptococcus. Infect. Immun. 64:12 (1996), 5428–5429.
    • (1996) Infect. Immun. , vol.64 , Issue.12 , pp. 5428-5429
    • Eichenbaum, Z.1    Muller, E.2    Morse, S.A.3    Scott, J.R.4
  • 171
    • 84879557888 scopus 로고    scopus 로고
    • Streptococcus pneumoniae requires iron for its viability and expresses two membrane proteins that bind haemoglobin and haem
    • Romero-Espejel, M.E., Gonzalez-Lopez, M.A., Olivares-Trejo Jde, J., Streptococcus pneumoniae requires iron for its viability and expresses two membrane proteins that bind haemoglobin and haem. Metallomics 5:4 (2013), 384–389.
    • (2013) Metallomics , vol.5 , Issue.4 , pp. 384-389
    • Romero-Espejel, M.E.1    Gonzalez-Lopez, M.A.2    Olivares-Trejo Jde, J.3
  • 173
    • 14744278436 scopus 로고    scopus 로고
    • Anemia of chronic disease
    • Weiss, G., Goodnough, L.T., Anemia of chronic disease. N. Engl. J. Med. 352:10 (2005), 1011–1023.
    • (2005) N. Engl. J. Med. , vol.352 , Issue.10 , pp. 1011-1023
    • Weiss, G.1    Goodnough, L.T.2
  • 176
    • 84958078769 scopus 로고    scopus 로고
    • Hemopexin therapy reverts heme-induced proinflammatory phenotypic switching of macrophages in a mouse model of sickle cell disease
    • Vinchi, F., Costa da Silva, M., Ingoglia, G., Petrillo, S., Brinkman, N., Zuercher, A., Cerwenka, A., Tolosano, E., Muckenthaler, M.U., Hemopexin therapy reverts heme-induced proinflammatory phenotypic switching of macrophages in a mouse model of sickle cell disease. Blood 127:4 (2016), 473–486.
    • (2016) Blood , vol.127 , Issue.4 , pp. 473-486
    • Vinchi, F.1    Costa da Silva, M.2    Ingoglia, G.3    Petrillo, S.4    Brinkman, N.5    Zuercher, A.6    Cerwenka, A.7    Tolosano, E.8    Muckenthaler, M.U.9
  • 180
    • 79952169985 scopus 로고    scopus 로고
    • Impact of iron treatment on immune effector function and cellular iron status of circulating monocytes in dialysis patients
    • Sonnweber, T., Theurl, I., Seifert, M., Schroll, A., Eder, S., Mayer, G., Weiss, G., Impact of iron treatment on immune effector function and cellular iron status of circulating monocytes in dialysis patients. Nephrol. Dial. Transplant. 26:3 (2011), 977–987.
    • (2011) Nephrol. Dial. Transplant. , vol.26 , Issue.3 , pp. 977-987
    • Sonnweber, T.1    Theurl, I.2    Seifert, M.3    Schroll, A.4    Eder, S.5    Mayer, G.6    Weiss, G.7
  • 181
    • 85009187552 scopus 로고    scopus 로고
    • 30 years of NF-kappaB: a blossoming of relevance to human pathobiology
    • Zhang, Q., Lenardo, M.J., Baltimore, D., 30 years of NF-kappaB: a blossoming of relevance to human pathobiology. Cell 168:1–2 (2017), 37–57.
    • (2017) Cell , vol.168 , Issue.1-2 , pp. 37-57
    • Zhang, Q.1    Lenardo, M.J.2    Baltimore, D.3
  • 182
    • 63349103637 scopus 로고    scopus 로고
    • Ferritin functions as a proinflammatory cytokine via iron-independent protein kinase C zeta/nuclear factor kappaB-regulated signaling in rat hepatic stellate cells
    • Ruddell, R.G., Hoang-Le, D., Barwood, J.M., Rutherford, P.S., Piva, T.J., Watters, D.J., Santambrogio, P., Arosio, P., Ramm, G.A., Ferritin functions as a proinflammatory cytokine via iron-independent protein kinase C zeta/nuclear factor kappaB-regulated signaling in rat hepatic stellate cells. Hepatology 49:3 (2009), 887–900.
    • (2009) Hepatology , vol.49 , Issue.3 , pp. 887-900
    • Ruddell, R.G.1    Hoang-Le, D.2    Barwood, J.M.3    Rutherford, P.S.4    Piva, T.J.5    Watters, D.J.6    Santambrogio, P.7    Arosio, P.8    Ramm, G.A.9
  • 183
    • 0028981059 scopus 로고
    • Role for NF-kappa B in the regulation of ferritin H by tumor necrosis factor-alpha
    • Kwak, E.L., Larochelle, D.A., Beaumont, C., Torti, S.V., Torti, F.M., Role for NF-kappa B in the regulation of ferritin H by tumor necrosis factor-alpha. J. Biol. Chem. 270:25 (1995), 15285–15293.
    • (1995) J. Biol. Chem. , vol.270 , Issue.25 , pp. 15285-15293
    • Kwak, E.L.1    Larochelle, D.A.2    Beaumont, C.3    Torti, S.V.4    Torti, F.M.5
  • 185
    • 68249162072 scopus 로고    scopus 로고
    • Bone morphogenetic protein-6 induces the expression of inducible nitric oxide synthase in macrophages
    • Kwon, S.J., Lee, G.T., Lee, J.H., Kim, W.J., Kim, I.Y., Bone morphogenetic protein-6 induces the expression of inducible nitric oxide synthase in macrophages. Immunology 28:Suppl. 1 (2009), e758–65.
    • (2009) Immunology , vol.28 , pp. e758-65
    • Kwon, S.J.1    Lee, G.T.2    Lee, J.H.3    Kim, W.J.4    Kim, I.Y.5
  • 187
    • 84922485491 scopus 로고    scopus 로고
    • HIF-1alpha restricts NF-kappaB-dependent gene expression to control innate immunity signals
    • Bandarra, D., Biddlestone, J., Mudie, S., Muller, H.A., Rocha, S., HIF-1alpha restricts NF-kappaB-dependent gene expression to control innate immunity signals. Dis Model Mech 8:2 (2015), 169–181.
    • (2015) Dis Model Mech , vol.8 , Issue.2 , pp. 169-181
    • Bandarra, D.1    Biddlestone, J.2    Mudie, S.3    Muller, H.A.4    Rocha, S.5
  • 188
    • 70249099576 scopus 로고    scopus 로고
    • Interdependence of hypoxic and innate immune responses
    • Nizet, V., Johnson, R.S., Interdependence of hypoxic and innate immune responses. Nat. Rev. Immunol. 9:9 (2009), 609–617.
    • (2009) Nat. Rev. Immunol. , vol.9 , Issue.9 , pp. 609-617
    • Nizet, V.1    Johnson, R.S.2
  • 190
    • 84933183002 scopus 로고    scopus 로고
    • Anaemia in kidney disease: harnessing hypoxia responses for therapy
    • Koury, M.J., Haase, V.H., Anaemia in kidney disease: harnessing hypoxia responses for therapy. Nat. Rev. Nephrol. 11:7 (2015), 394–410.
    • (2015) Nat. Rev. Nephrol. , vol.11 , Issue.7 , pp. 394-410
    • Koury, M.J.1    Haase, V.H.2
  • 194
    • 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 403:6765 (2000), 46–53.
    • (2000) Nature , vol.403 , Issue.6765 , pp. 46-53
    • Bennett, M.J.1    Lebron, J.A.2    Bjorkman, P.J.3
  • 196
    • 85044480323 scopus 로고    scopus 로고
    • unpublished observations.
    • M. Nairz, G. Weiss, unpublished observations.
    • Nairz, M.1    Weiss, G.2
  • 197
    • 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. 181:4 (2008), 2723–2731.
    • (2008) J. Immunol. , vol.181 , Issue.4 , 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
  • 199
    • 33646427702 scopus 로고    scopus 로고
    • TLR4-dependent hepcidin expression by myeloid cells in response to bacterial pathogens
    • Peyssonnaux, C., Zinkernagel, A.S., Datta, V., Lauth, X., Johnson, R.S., Nizet, V., TLR4-dependent hepcidin expression by myeloid cells in response to bacterial pathogens. Blood 107:9 (2006), 3727–3732.
    • (2006) Blood , vol.107 , Issue.9 , pp. 3727-3732
    • Peyssonnaux, C.1    Zinkernagel, A.S.2    Datta, V.3    Lauth, X.4    Johnson, R.S.5    Nizet, V.6
  • 201
    • 79960681867 scopus 로고    scopus 로고
    • Low hepcidin accounts for the proinflammatory status associated with iron deficiency
    • Pagani, A., Nai, A., Corna, G., Bosurgi, L., Rovere-Querini, P., Camaschella, C., Silvestri, L., Low hepcidin accounts for the proinflammatory status associated with iron deficiency. Blood 118:3 (2011), 736–746.
    • (2011) Blood , vol.118 , Issue.3 , pp. 736-746
    • Pagani, A.1    Nai, A.2    Corna, G.3    Bosurgi, L.4    Rovere-Querini, P.5    Camaschella, C.6    Silvestri, L.7
  • 205
    • 57749120460 scopus 로고    scopus 로고
    • Nrf1 and Nrf2 play distinct roles in activation of antioxidant response element-dependent genes
    • Ohtsuji, M., Katsuoka, F., Kobayashi, A., Aburatani, H., Hayes, J.D., Yamamoto, M., Nrf1 and Nrf2 play distinct roles in activation of antioxidant response element-dependent genes. J. Biol. Chem. 283:48 (2008), 33554–33562.
    • (2008) J. Biol. Chem. , vol.283 , Issue.48 , pp. 33554-33562
    • Ohtsuji, M.1    Katsuoka, F.2    Kobayashi, A.3    Aburatani, H.4    Hayes, J.D.5    Yamamoto, M.6
  • 206
    • 20444480956 scopus 로고    scopus 로고
    • Bach1 competes with Nrf2 leading to negative regulation of the antioxidant response element (ARE)-mediated NAD(P)H:quinone oxidoreductase 1 gene expression and induction in response to antioxidants
    • Dhakshinamoorthy, S., Jain, A.K., Bloom, D.A., Jaiswal, A.K., Bach1 competes with Nrf2 leading to negative regulation of the antioxidant response element (ARE)-mediated NAD(P)H:quinone oxidoreductase 1 gene expression and induction in response to antioxidants. J. Biol. Chem. 280:17 (2005), 16891–16900.
    • (2005) J. Biol. Chem. , vol.280 , Issue.17 , pp. 16891-16900
    • Dhakshinamoorthy, S.1    Jain, A.K.2    Bloom, D.A.3    Jaiswal, A.K.4
  • 208
    • 0037462675 scopus 로고    scopus 로고
    • Nrf2 mediates the induction of ferritin H in response to xenobiotics and cancer chemopreventive dithiolethiones
    • Pietsch, E.C., Chan, J.Y., Torti, F.M., Torti, S.V., Nrf2 mediates the induction of ferritin H in response to xenobiotics and cancer chemopreventive dithiolethiones. J. Biol. Chem. 278:4 (2003), 2361–2369.
    • (2003) J. Biol. Chem. , vol.278 , Issue.4 , pp. 2361-2369
    • Pietsch, E.C.1    Chan, J.Y.2    Torti, F.M.3    Torti, S.V.4
  • 210
    • 67349234858 scopus 로고    scopus 로고
    • Iron availability and infection
    • Weinberg, E.D., Iron availability and infection. Biochim. Biophys. Acta 1790:7 (2009), 600–605.
    • (2009) Biochim. Biophys. Acta , vol.1790 , Issue.7 , pp. 600-605
    • Weinberg, E.D.1
  • 211
    • 84868526205 scopus 로고    scopus 로고
    • Hepcidin and the iron-infection axis
    • Drakesmith, H., Prentice, A.M., Hepcidin and the iron-infection axis. Science 338:6108 (2012), 768–772.
    • (2012) Science , vol.338 , Issue.6108 , pp. 768-772
    • Drakesmith, H.1    Prentice, A.M.2
  • 212
    • 84877869322 scopus 로고    scopus 로고
    • Iron in infection and immunity
    • Cassat, J.E., Skaar, E.P., Iron in infection and immunity. Cell Host Microbe 13:5 (2013), 509–519.
    • (2013) Cell Host Microbe , vol.13 , Issue.5 , pp. 509-519
    • Cassat, J.E.1    Skaar, E.P.2
  • 213
    • 84937979159 scopus 로고    scopus 로고
    • Iron homeostasis in host defence and inflammation
    • Ganz, T., Nemeth, E., Iron homeostasis in host defence and inflammation. Nat. Rev. Immunol. 15:8 (2015), 500–510.
    • (2015) Nat. Rev. Immunol. , vol.15 , Issue.8 , pp. 500-510
    • Ganz, T.1    Nemeth, E.2
  • 214
    • 84946068281 scopus 로고    scopus 로고
    • The Iron age of host-microbe interactions
    • Soares, M.P., Weiss, G., The Iron age of host-microbe interactions. EMBO Rep. 16:11 (2015), 1482–1500.
    • (2015) EMBO Rep. , vol.16 , Issue.11 , pp. 1482-1500
    • Soares, M.P.1    Weiss, G.2
  • 216
    • 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 288:5471 (2000), 1651–1653.
    • (2000) Science , vol.288 , Issue.5471 , pp. 1651-1653
    • Posey, J.E.1    Gherardini, F.C.2
  • 219
    • 0142012132 scopus 로고    scopus 로고
    • Severe bacterial infection in transfusion-dependent patients with thalassemia major
    • Wang, S.C., Lin, K.H., Chern, J.P., Lu, M.Y., Jou, S.T., Lin, D.T., Lin, K.S., Severe bacterial infection in transfusion-dependent patients with thalassemia major. Clin. Infect. Dis. 37:7 (2003), 984–988.
    • (2003) Clin. Infect. Dis. , vol.37 , Issue.7 , pp. 984-988
    • Wang, S.C.1    Lin, K.H.2    Chern, J.P.3    Lu, M.Y.4    Jou, S.T.5    Lin, D.T.6    Lin, K.S.7
  • 220
    • 84920905125 scopus 로고    scopus 로고
    • Hepcidin-induced hypoferremia is a critical host defense mechanism against the siderophilic bacterium Vibrio vulnificus
    • Arezes, J., Jung, G., Gabayan, V., Valore, E., Ruchala, P., Gulig, P.A., Ganz, T., Nemeth, E., Bulut, Y., Hepcidin-induced hypoferremia is a critical host defense mechanism against the siderophilic bacterium Vibrio vulnificus. Cell Host Microbe 17:1 (2015), 47–57.
    • (2015) Cell Host Microbe , vol.17 , Issue.1 , pp. 47-57
    • Arezes, J.1    Jung, G.2    Gabayan, V.3    Valore, E.4    Ruchala, P.5    Gulig, P.A.6    Ganz, T.7    Nemeth, E.8    Bulut, Y.9
  • 224
  • 225
    • 14544294358 scopus 로고    scopus 로고
    • Modification of iron regulation by the inflammatory response
    • Weiss, G., Modification of iron regulation by the inflammatory response. Best Pract. Res. Clin. Haematol. 18:2 (2005), 183–201.
    • (2005) Best Pract. Res. Clin. Haematol. , vol.18 , Issue.2 , pp. 183-201
    • Weiss, G.1
  • 227
    • 11144314814 scopus 로고    scopus 로고
    • Lipocalin 2 mediates an innate immune response to bacterial infection by sequestrating iron
    • Flo, T.H., Smith, K.D., Sato, S., Rodriguez, D.J., Holmes, M.A., Strong, R.K., Akira, S., Aderem, A., Lipocalin 2 mediates an innate immune response to bacterial infection by sequestrating iron. Nature 432:7019 (2004), 917–921.
    • (2004) Nature , vol.432 , Issue.7019 , pp. 917-921
    • Flo, T.H.1    Smith, K.D.2    Sato, S.3    Rodriguez, D.J.4    Holmes, M.A.5    Strong, R.K.6    Akira, S.7    Aderem, A.8
  • 228
    • 84872169461 scopus 로고    scopus 로고
    • Interaction of lipocalin 2 transferrin, and siderophores determines the replicative niche of Klebsiella pneumoniae during pneumonia
    • Bachman, M.A., Lenio, S., Schmidt, L., Oyler, J.E., Weiser, J.N., Interaction of lipocalin 2 transferrin, and siderophores determines the replicative niche of Klebsiella pneumoniae during pneumonia. MBio 3:6 (2012), e00224–11.
    • (2012) MBio , vol.3 , Issue.6 , pp. e00224-11
    • Bachman, M.A.1    Lenio, S.2    Schmidt, L.3    Oyler, J.E.4    Weiser, J.N.5
  • 229
    • 34548242283 scopus 로고    scopus 로고
    • Iron metabolism at the host pathogen interface: lipocalin 2 and the pathogen-associated iroA gene cluster
    • Smith, K.D., Iron metabolism at the host pathogen interface: lipocalin 2 and the pathogen-associated iroA gene cluster. Int. J. Biochem. Cell Biol. 39:10 (2007), 1776–1780.
    • (2007) Int. J. Biochem. Cell Biol. , vol.39 , Issue.10 , pp. 1776-1780
    • Smith, K.D.1
  • 231
    • 84931074436 scopus 로고    scopus 로고
    • Diverging roles of bacterial siderophores during infection
    • Holden, V.I., Bachman, M.A., Diverging roles of bacterial siderophores during infection. Metallomics 7:6 (2015), 986–995.
    • (2015) Metallomics , vol.7 , Issue.6 , pp. 986-995
    • Holden, V.I.1    Bachman, M.A.2
  • 232
    • 85007518242 scopus 로고    scopus 로고
    • Siderophores more than stealing iron
    • Behnsen, J., Raffatellu, M., Siderophores more than stealing iron. MBio 7:6 (2016), e01906–16.
    • (2016) MBio , vol.7 , Issue.6 , pp. e01906-16
    • Behnsen, J.1    Raffatellu, M.2
  • 233
    • 0141483164 scopus 로고    scopus 로고
    • Molecular genetics of fungal siderophore biosynthesis and uptake: the role of siderophores in iron uptake and storage
    • Haas, H., Molecular genetics of fungal siderophore biosynthesis and uptake: the role of siderophores in iron uptake and storage. Appl. Microbiol. Biotechnol. 62:4 (2003), 316–330.
    • (2003) Appl. Microbiol. Biotechnol. , vol.62 , Issue.4 , pp. 316-330
    • Haas, H.1
  • 234
    • 8644220677 scopus 로고    scopus 로고
    • Siderophore biosynthesis but not reductive iron assimilation is essential for Aspergillus fumigatus virulence
    • Schrettl, M., Bignell, E., Kragl, C., Joechl, C., Rogers, T., Arst, H.N. Jr., Haynes, K., Haas, H., Siderophore biosynthesis but not reductive iron assimilation is essential for Aspergillus fumigatus virulence. J. Exp. Med. 200:9 (2004), 1213–1219.
    • (2004) J. Exp. Med. , vol.200 , Issue.9 , pp. 1213-1219
    • Schrettl, M.1    Bignell, E.2    Kragl, C.3    Joechl, C.4    Rogers, T.5    Arst, H.N.6    Haynes, K.7    Haas, H.8
  • 236
    • 52749097757 scopus 로고    scopus 로고
    • Effects of the Aspergillus fumigatus siderophore systems on the regulation of macrophage immune effector pathways and iron homeostasis
    • Seifert, M., Nairz, M., Schroll, A., Schrettl, M., Haas, H., Weiss, G., Effects of the Aspergillus fumigatus siderophore systems on the regulation of macrophage immune effector pathways and iron homeostasis. Immunobiology 213:9–10 (2008), 767–778.
    • (2008) Immunobiology , vol.213 , Issue.9-10 , pp. 767-778
    • Seifert, M.1    Nairz, M.2    Schroll, A.3    Schrettl, M.4    Haas, H.5    Weiss, G.6
  • 237
    • 84929223565 scopus 로고    scopus 로고
    • Interplay between enterobactin, myeloperoxidase and lipocalin 2 regulates E. coli survival in the inflamed gut
    • Singh, V., Yeoh, B.S., Xiao, X., Kumar, M., Bachman, M., Borregaard, N., Joe, B., Vijay-Kumar, M., Interplay between enterobactin, myeloperoxidase and lipocalin 2 regulates E. coli survival in the inflamed gut. Nat. Commun., 6, 2015, 7113.
    • (2015) Nat. Commun. , vol.6 , pp. 7113
    • Singh, V.1    Yeoh, B.S.2    Xiao, X.3    Kumar, M.4    Bachman, M.5    Borregaard, N.6    Joe, B.7    Vijay-Kumar, M.8
  • 239
    • 84876783277 scopus 로고    scopus 로고
    • Impaired neutrophil function in 24p3 null mice contributes to enhanced susceptibility to bacterial infections
    • Liu, Z., Petersen, R., Devireddy, L., Impaired neutrophil function in 24p3 null mice contributes to enhanced susceptibility to bacterial infections. J. Immunol. 190:9 (2013), 4692–4706.
    • (2013) J. Immunol. , vol.190 , Issue.9 , pp. 4692-4706
    • Liu, Z.1    Petersen, R.2    Devireddy, L.3
  • 240
    • 73449084865 scopus 로고    scopus 로고
    • Mucosal lipocalin 2 has pro-inflammatory and iron-sequestering effects in response to bacterial enterobactin
    • Bachman, M.A., Miller, V.L., Weiser, J.N., Mucosal lipocalin 2 has pro-inflammatory and iron-sequestering effects in response to bacterial enterobactin. PLoS Pathog., 5(10), 2009, e1000622.
    • (2009) PLoS Pathog. , vol.5 , Issue.10 , pp. e1000622
    • Bachman, M.A.1    Miller, V.L.2    Weiser, J.N.3
  • 244
    • 84879827121 scopus 로고    scopus 로고
    • Lipocalin-2 expressed in innate immune cells is an endogenous inhibitor of inflammation in murine nephrotoxic serum nephritis
    • Eller, K., Schroll, A., Banas, M., Kirsch, A.H., Huber, J.M., Nairz, M., Skvortsov, S., Weiss, G., Rosenkranz, A.R., Theurl, I., Lipocalin-2 expressed in innate immune cells is an endogenous inhibitor of inflammation in murine nephrotoxic serum nephritis. PLoS One, 8(7), 2013, e67693.
    • (2013) PLoS One , vol.8 , Issue.7 , pp. e67693
    • Eller, K.1    Schroll, A.2    Banas, M.3    Kirsch, A.H.4    Huber, J.M.5    Nairz, M.6    Skvortsov, S.7    Weiss, G.8    Rosenkranz, A.R.9    Theurl, I.10
  • 245
    • 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 10:5 (2002), 1033–1043.
    • (2002) Mol. Cell , vol.10 , Issue.5 , 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
  • 247
    • 14144253168 scopus 로고    scopus 로고
    • In vitro characterization of IroB a pathogen-associated C-glycosyltransferase
    • Fischbach, M.A., Lin, H., Liu, D.R., Walsh, C.T., In vitro characterization of IroB a pathogen-associated C-glycosyltransferase. Proc. Natl. Acad. Sci. U. S. A. 102:3 (2005), 571–576.
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , Issue.3 , pp. 571-576
    • Fischbach, M.A.1    Lin, H.2    Liu, D.R.3    Walsh, C.T.4
  • 248
    • 38849128160 scopus 로고    scopus 로고
    • Biosynthesis and IroC-dependent export of the siderophore salmochelin are essential for virulence of Salmonella enterica serovar Typhimurium
    • Crouch, M.L., Castor, M., Karlinsey, J.E., Kalhorn, T., Fang, F.C., Biosynthesis and IroC-dependent export of the siderophore salmochelin are essential for virulence of Salmonella enterica serovar Typhimurium. Mol. Microbiol. 67:5 (2008), 971–983.
    • (2008) Mol. Microbiol. , vol.67 , Issue.5 , pp. 971-983
    • Crouch, M.L.1    Castor, M.2    Karlinsey, J.E.3    Kalhorn, T.4    Fang, F.C.5
  • 249
    • 0037388150 scopus 로고    scopus 로고
    • Salmochelins siderophores of Salmonella enterica and uropathogenic Escherichia coli strains, are recognized by the outer membrane receptor IroN
    • Hantke, K., Nicholson, G., Rabsch, W., Winkelmann, G., Salmochelins siderophores of Salmonella enterica and uropathogenic Escherichia coli strains, are recognized by the outer membrane receptor IroN. Proc. Natl. Acad. Sci. U. S. A. 100:7 (2003), 3677–3682.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , Issue.7 , pp. 3677-3682
    • Hantke, K.1    Nicholson, G.2    Rabsch, W.3    Winkelmann, G.4
  • 256
    • 0023713907 scopus 로고
    • Amastigotes of Trypanosoma cruzi sustain an infective cycle in mammalian cells
    • Ley, V., Andrews, N.W., Robbins, E.S., Nussenzweig, V., Amastigotes of Trypanosoma cruzi sustain an infective cycle in mammalian cells. J. Exp. Med. 168:2 (1988), 649–659.
    • (1988) J. Exp. Med. , vol.168 , Issue.2 , pp. 649-659
    • Ley, V.1    Andrews, N.W.2    Robbins, E.S.3    Nussenzweig, V.4
  • 259
    • 50949104554 scopus 로고    scopus 로고
    • Iron depletion limits intracellular bacterial growth in macrophages
    • Paradkar, P.N., De Domenico, I., Durchfort, N., Zohn, I., Kaplan, J., Ward, D.M., Iron depletion limits intracellular bacterial growth in macrophages. Blood 112:3 (2008), 866–874.
    • (2008) Blood , vol.112 , Issue.3 , pp. 866-874
    • Paradkar, P.N.1    De Domenico, I.2    Durchfort, N.3    Zohn, I.4    Kaplan, J.5    Ward, D.M.6
  • 262
    • 85029754682 scopus 로고    scopus 로고
    • Synthetic porcine hepcidin exhibits different roles in Escherichia coli and Salmonella infections
    • AAC. 02638-16
    • Liu, D., Gan, Z.S., Ma, W., Xiong, H.T., Li, Y.Q., Wang, Y.Z., Du, H.H., Synthetic porcine hepcidin exhibits different roles in Escherichia coli and Salmonella infections. Antimicrob. Agents Chemother., 61(10), 2017 AAC. 02638-16.
    • (2017) Antimicrob. Agents Chemother. , vol.61 , Issue.10
    • Liu, D.1    Gan, Z.S.2    Ma, W.3    Xiong, H.T.4    Li, Y.Q.5    Wang, Y.Z.6    Du, H.H.7
  • 263
    • 84877150279 scopus 로고    scopus 로고
    • Neutrophil gelatinase-associated lipocalin and interleukin-10 regulate intramacrophage Chlamydia pneumoniae replication by modulating intracellular iron homeostasis
    • Bellmann-Weiler, R., Schroll, A., Engl, S., Nairz, M., Talasz, H., Seifert, M., Weiss, G., Neutrophil gelatinase-associated lipocalin and interleukin-10 regulate intramacrophage Chlamydia pneumoniae replication by modulating intracellular iron homeostasis. Immunobiology 218:7 (2013), 969–978.
    • (2013) Immunobiology , vol.218 , Issue.7 , pp. 969-978
    • Bellmann-Weiler, R.1    Schroll, A.2    Engl, S.3    Nairz, M.4    Talasz, H.5    Seifert, M.6    Weiss, G.7
  • 264
    • 84931056812 scopus 로고    scopus 로고
    • Contrasting regulation of macrophage iron homeostasis in response to infection with Listeria monocytogenes depending on localization of bacteria
    • Haschka, D., Nairz, M., Demetz, E., Wienerroither, S., Decker, T., Weiss, G., Contrasting regulation of macrophage iron homeostasis in response to infection with Listeria monocytogenes depending on localization of bacteria. Metallomics 7:6 (2015), 1036–1045.
    • (2015) Metallomics , vol.7 , Issue.6 , pp. 1036-1045
    • Haschka, D.1    Nairz, M.2    Demetz, E.3    Wienerroither, S.4    Decker, T.5    Weiss, G.6
  • 265
    • 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. 9:9 (2007), 2126–2140.
    • (2007) Cell. Microbiol. , vol.9 , Issue.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
  • 270
    • 85027514055 scopus 로고    scopus 로고
    • Hepcidin-(in)dependent mechanisms of iron metabolism regulation during infection by Listeria and Salmonella
    • IAI. 00353-17
    • Moreira, A.C., Neves, J.V., Silva, T., Oliveira, P., Gomes, M.S., Rodrigues, P.N., Hepcidin-(in)dependent mechanisms of iron metabolism regulation during infection by Listeria and Salmonella. Infect. Immun., 85(9), 2017 IAI. 00353-17.
    • (2017) Infect. Immun. , vol.85 , Issue.9
    • Moreira, A.C.1    Neves, J.V.2    Silva, T.3    Oliveira, P.4    Gomes, M.S.5    Rodrigues, P.N.6
  • 271
    • 85035000514 scopus 로고    scopus 로고
    • An iron-rich diet decreases the mycobacterial burden and correlates with hepcidin upregulation lower levels of proinflammatory mediators, and increased T-cell recruitment in a model of Mycobacterium bovis Bacille Calmette-Guerin infection
    • Agoro, R., Benmerzoug, S., Rose, S., Bouyer, M., Gozzelino, R., Garcia, I., Ryffel, B., Quesniaux, V.F.J., Mura, C., An iron-rich diet decreases the mycobacterial burden and correlates with hepcidin upregulation lower levels of proinflammatory mediators, and increased T-cell recruitment in a model of Mycobacterium bovis Bacille Calmette-Guerin infection. J. Infect. Dis. 216:7 (2017), 907–918.
    • (2017) J. Infect. Dis. , vol.216 , Issue.7 , pp. 907-918
    • Agoro, R.1    Benmerzoug, S.2    Rose, S.3    Bouyer, M.4    Gozzelino, R.5    Garcia, I.6    Ryffel, B.7    Quesniaux, V.F.J.8    Mura, C.9
  • 272
    • 34848888911 scopus 로고    scopus 로고
    • Expression and localization of hepcidin in macrophages: a role in host defense against tuberculosis
    • Sow, F.B., Florence, W.C., Satoskar, A.R., Schlesinger, L.S., Zwilling, B.S., Lafuse, W.P., Expression and localization of hepcidin in macrophages: a role in host defense against tuberculosis. J. Leukoc. Biol. 82:4 (2007), 934–945.
    • (2007) J. Leukoc. Biol. , vol.82 , Issue.4 , pp. 934-945
    • Sow, F.B.1    Florence, W.C.2    Satoskar, A.R.3    Schlesinger, L.S.4    Zwilling, B.S.5    Lafuse, W.P.6
  • 273
    • 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. 9:8 (2001), 397–403.
    • (2001) Trends Microbiol. , vol.9 , Issue.8 , pp. 397-403
    • Forbes, J.R.1    Gros, P.2
  • 274
    • 0037460107 scopus 로고    scopus 로고
    • Divalent cation transport and susceptibility to infectious and autoimmune disease: continuation of the Ity/Lsh/Bcg/Nramp1/Slc11a1 gene story
    • Blackwell, J.M., Searle, S., Mohamed, H., White, J.K., Divalent cation transport and susceptibility to infectious and autoimmune disease: continuation of the Ity/Lsh/Bcg/Nramp1/Slc11a1 gene story. Immunol. Lett. 85:2 (2003), 197–203.
    • (2003) Immunol. Lett. , vol.85 , Issue.2 , pp. 197-203
    • Blackwell, J.M.1    Searle, S.2    Mohamed, H.3    White, J.K.4
  • 275
    • 0043136713 scopus 로고    scopus 로고
    • Nramp1 functionality increases inducible nitric oxide synthase transcription via stimulation of IFN regulatory factor 1 expression
    • Fritsche, G., Dlaska, M., Barton, H., Theurl, I., Garimorth, K., Weiss, G., Nramp1 functionality increases inducible nitric oxide synthase transcription via stimulation of IFN regulatory factor 1 expression. J. Immunol. 171:4 (2003), 1994–1998.
    • (2003) J. Immunol. , vol.171 , Issue.4 , pp. 1994-1998
    • Fritsche, G.1    Dlaska, M.2    Barton, H.3    Theurl, I.4    Garimorth, K.5    Weiss, G.6
  • 276
    • 84864768441 scopus 로고    scopus 로고
    • Slc11a1 (Nramp1) impairs growth of Salmonella enterica serovar typhimurium in macrophages via stimulation of lipocalin-2 expression
    • Fritsche, G., Nairz, M., Libby, S.J., Fang, F.C., Weiss, G., Slc11a1 (Nramp1) impairs growth of Salmonella enterica serovar typhimurium in macrophages via stimulation of lipocalin-2 expression. J. Leukoc. Biol. 92:2 (2012), 353–359.
    • (2012) J. Leukoc. Biol. , vol.92 , Issue.2 , pp. 353-359
    • Fritsche, G.1    Nairz, M.2    Libby, S.J.3    Fang, F.C.4    Weiss, G.5
  • 278
    • 58149345129 scopus 로고    scopus 로고
    • Nramp1-functionality increases iNOS expression via repression of IL-10 formation
    • Fritsche, G., Nairz, M., Werner, E.R., Barton, H.C., Weiss, G., Nramp1-functionality increases iNOS expression via repression of IL-10 formation. Eur. J. Immunol. 38:11 (2008), 3060–3067.
    • (2008) Eur. J. Immunol. , vol.38 , Issue.11 , pp. 3060-3067
    • Fritsche, G.1    Nairz, M.2    Werner, E.R.3    Barton, H.C.4    Weiss, G.5
  • 279
    • 0032485353 scopus 로고    scopus 로고
    • Variations in the NRAMP1 gene and susceptibility to tuberculosis in West Africans
    • Bellamy, R., Ruwende, C., Corrah, T., McAdam, K.P., Whittle, H.C., Hill, A.V., Variations in the NRAMP1 gene and susceptibility to tuberculosis in West Africans. N. Engl. J. Med. 338:10 (1998), 640–644.
    • (1998) N. Engl. J. Med. , vol.338 , Issue.10 , pp. 640-644
    • Bellamy, R.1    Ruwende, C.2    Corrah, T.3    McAdam, K.P.4    Whittle, H.C.5    Hill, A.V.6
  • 280
    • 84930479967 scopus 로고    scopus 로고
    • Genetic variants of SLC11A1 are associated with both autoimmune and infectious diseases: systematic review and meta-analysis
    • Archer, N.S., Nassif, N.T., O'Brien, B.A., Genetic variants of SLC11A1 are associated with both autoimmune and infectious diseases: systematic review and meta-analysis. Genes Immun. 16:4 (2015), 275–283.
    • (2015) Genes Immun. , vol.16 , Issue.4 , pp. 275-283
    • Archer, N.S.1    Nassif, N.T.2    O'Brien, B.A.3
  • 282
    • 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. 203:10 (2006), 2363–2375.
    • (2006) J. Exp. Med. , vol.203 , Issue.10 , pp. 2363-2375
    • Huynh, C.1    Sacks, D.L.2    Andrews, N.W.3
  • 284
    • 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. 11:1 (2009), 83–94.
    • (2009) Cell. Microbiol. , vol.11 , Issue.1 , pp. 83-94
    • Das, N.K.1    Biswas, S.2    Solanki, S.3    Mukhopadhyay, C.K.4
  • 286
    • 84901049327 scopus 로고    scopus 로고
    • Iron ERRs with Salmonella
    • Fang, F.C., Weiss, G., Iron ERRs with Salmonella. Cell Host Microbe 15:5 (2014), 515–516.
    • (2014) Cell Host Microbe , vol.15 , Issue.5 , pp. 515-516
    • Fang, F.C.1    Weiss, G.2
  • 287
    • 0029013807 scopus 로고
    • The plasmodium digestive vacuole: metabolic headquarters and choice drug target
    • Olliaro, P.L., Goldberg, D.E., The plasmodium digestive vacuole: metabolic headquarters and choice drug target. Parasitol. Today 11:8 (1995), 294–297.
    • (1995) Parasitol. Today , vol.11 , Issue.8 , pp. 294-297
    • Olliaro, P.L.1    Goldberg, D.E.2
  • 288
    • 84875814268 scopus 로고    scopus 로고
    • Parasite maturation and host serum iron influence the labile iron pool of erythrocyte stage Plasmodium falciparum
    • Clark, M., Fisher, N.C., Kasthuri, R., Cerami Hand, C., Parasite maturation and host serum iron influence the labile iron pool of erythrocyte stage Plasmodium falciparum. Br. J. Haematol. 161:2 (2013), 262–269.
    • (2013) Br. J. Haematol. , vol.161 , Issue.2 , pp. 262-269
    • Clark, M.1    Fisher, N.C.2    Kasthuri, R.3    Cerami Hand, C.4
  • 289
    • 82555176482 scopus 로고    scopus 로고
    • Superinfection in malaria: Plasmodium shows its iron will
    • Portugal, S., Drakesmith, H., Mota, M.M., Superinfection in malaria: Plasmodium shows its iron will. EMBO Rep. 12:12 (2011), 1233–1242.
    • (2011) EMBO Rep. , vol.12 , Issue.12 , pp. 1233-1242
    • Portugal, S.1    Drakesmith, H.2    Mota, M.M.3
  • 293
    • 77954503396 scopus 로고    scopus 로고
    • Increased serum hepcidin and alterations in blood iron parameters associated with asymptomatic P. falciparum and P. vivax malaria
    • de Mast, Q., Syafruddin, D., Keijmel, S., Riekerink, T.O., Deky, O., Asih, P.B., Swinkels, D.W., van der Ven, A.J., Increased serum hepcidin and alterations in blood iron parameters associated with asymptomatic P. falciparum and P. vivax malaria. Haematologica 95:7 (2010), 1068–1074.
    • (2010) Haematologica , vol.95 , Issue.7 , pp. 1068-1074
    • de Mast, Q.1    Syafruddin, D.2    Keijmel, S.3    Riekerink, T.O.4    Deky, O.5    Asih, P.B.6    Swinkels, D.W.7    van der Ven, A.J.8
  • 295
    • 83755183844 scopus 로고    scopus 로고
    • Hepcidin is regulated during blood-stage malaria and plays a protective role in malaria infection
    • Wang, H.Z., He, Y.X., Yang, C.J., Zhou, W., Zou, C.G., Hepcidin is regulated during blood-stage malaria and plays a protective role in malaria infection. J. Immunol. 187:12 (2011), 6410–6416.
    • (2011) J. Immunol. , vol.187 , Issue.12 , pp. 6410-6416
    • Wang, H.Z.1    He, Y.X.2    Yang, C.J.3    Zhou, W.4    Zou, C.G.5
  • 296
    • 4844227764 scopus 로고    scopus 로고
    • Antimicrobial reactive oxygen and nitrogen species: concepts and controversies
    • Fang, F.C., Antimicrobial reactive oxygen and nitrogen species: concepts and controversies. Nat. Rev. Microbiol. 2:10 (2004), 820–832.
    • (2004) Nat. Rev. Microbiol. , vol.2 , Issue.10 , pp. 820-832
    • Fang, F.C.1
  • 297
    • 31144432757 scopus 로고    scopus 로고
    • Modulation of the activation of Stat1 by the interferon-gamma receptor complex
    • Krause, C.D., He, W., Kotenko, S., Pestka, S., Modulation of the activation of Stat1 by the interferon-gamma receptor complex. Cell Res. 16:1 (2006), 113–123.
    • (2006) Cell Res. , vol.16 , Issue.1 , pp. 113-123
    • Krause, C.D.1    He, W.2    Kotenko, S.3    Pestka, S.4
  • 298
    • 84924228289 scopus 로고    scopus 로고
    • Nitric oxide synthase in innate and adaptive immunity: an update
    • Bogdan, C., Nitric oxide synthase in innate and adaptive immunity: an update. Trends Immunol. 36:3 (2015), 161–178.
    • (2015) Trends Immunol. , vol.36 , Issue.3 , pp. 161-178
    • Bogdan, C.1
  • 299
    • 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. 38:7 (2008), 1923–1936.
    • (2008) Eur. J. Immunol. , vol.38 , Issue.7 , pp. 1923-1936
    • Nairz, M.1    Fritsche, G.2    Brunner, P.3    Talasz, H.4    Hantke, K.5    Weiss, G.6
  • 300
    • 85060969033 scopus 로고    scopus 로고
    • Hemojuvelin regulates the innate immune response to peritoneal bacterial infection in mice
    • Wu, Q., Shen, Y., Tao, Y., Wei, J., Wang, H., An, P., Zhang, Z., Gao, H., Zhou, T., Wang, F., Min, J., Hemojuvelin regulates the innate immune response to peritoneal bacterial infection in mice. Cell Discov 3 (2017), 17028–17041.
    • (2017) Cell Discov , vol.3 , pp. 17028-17041
    • Wu, Q.1    Shen, Y.2    Tao, Y.3    Wei, J.4    Wang, H.5    An, P.6    Zhang, Z.7    Gao, H.8    Zhou, T.9    Wang, F.10    Min, J.11
  • 301
    • 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. 83:5 (1989), 1457–1465.
    • (1989) J. Clin. Invest. , vol.83 , Issue.5 , pp. 1457-1465
    • Byrd, T.F.1    Horwitz, M.A.2
  • 302
    • 0034783452 scopus 로고    scopus 로고
    • Infection with Mycobacterium avium differentially regulates the expression of iron transport protein mRNA in murine peritoneal macrophages
    • Zhong, W., Lafuse, W.P., Zwilling, B.S., Infection with Mycobacterium avium differentially regulates the expression of iron transport protein mRNA in murine peritoneal macrophages. Infect. Immun. 69:11 (2001), 6618–6624.
    • (2001) Infect. Immun. , vol.69 , Issue.11 , pp. 6618-6624
    • Zhong, W.1    Lafuse, W.P.2    Zwilling, B.S.3
  • 305
    • 33744958258 scopus 로고    scopus 로고
    • Autophagy controls Salmonella infection in response to damage to the Salmonella-containing vacuole
    • Birmingham, C.L., Smith, A.C., Bakowski, M.A., Yoshimori, T., Brumell, J.H., Autophagy controls Salmonella infection in response to damage to the Salmonella-containing vacuole. J. Biol. Chem. 281:16 (2006), 11374–11383.
    • (2006) J. Biol. Chem. , vol.281 , Issue.16 , pp. 11374-11383
    • Birmingham, C.L.1    Smith, A.C.2    Bakowski, M.A.3    Yoshimori, T.4    Brumell, J.H.5
  • 307
    • 84983455413 scopus 로고    scopus 로고
    • Iron deficiency or anemia of inflammation? Differential diagnosis and mechanisms of anemia of inflammation
    • Nairz, M., Theurl, I., Wolf, D., Weiss, G., Iron deficiency or anemia of inflammation? Differential diagnosis and mechanisms of anemia of inflammation. Wien. Med. Wochenschr. 166:13–14 (2016), 411–423.
    • (2016) Wien. Med. Wochenschr. , vol.166 , Issue.13-14 , pp. 411-423
    • Nairz, M.1    Theurl, I.2    Wolf, D.3    Weiss, G.4
  • 311
    • 77951745552 scopus 로고    scopus 로고
    • Antihepcidin antibody treatment modulates iron metabolism and is effective in a mouse model of inflammation-induced anemia
    • Sasu, B.J., Cooke, K.S., Arvedson, T.L., Plewa, C., Ellison, A.R., Sheng, J., Winters, A., Juan, T., Li, H., Begley, C.G., Molineux, G., Antihepcidin antibody treatment modulates iron metabolism and is effective in a mouse model of inflammation-induced anemia. Blood 115:17 (2010), 3616–3624.
    • (2010) Blood , vol.115 , Issue.17 , pp. 3616-3624
    • Sasu, B.J.1    Cooke, K.S.2    Arvedson, T.L.3    Plewa, C.4    Ellison, A.R.5    Sheng, J.6    Winters, A.7    Juan, T.8    Li, H.9    Begley, C.G.10    Molineux, G.11
  • 312
    • 85041303346 scopus 로고    scopus 로고
    • Anemia at older age: etiologies, clinical implications and management
    • Stauder, R., Valent, P., Theurl, I., Anemia at older age: etiologies, clinical implications and management. Blood 131:5 (2018), 505–514.
    • (2018) Blood , vol.131 , Issue.5 , pp. 505-514
    • Stauder, R.1    Valent, P.2    Theurl, I.3
  • 313
    • 33750577945 scopus 로고    scopus 로고
    • Deferiprone iron chelation as a novel therapy for experimental mucormycosis
    • Ibrahim, A.S., Edwards, J.E. Jr., Fu, Y., Spellberg, B., Deferiprone iron chelation as a novel therapy for experimental mucormycosis. J. Antimicrob. Chemother. 58:5 (2006), 1070–1073.
    • (2006) J. Antimicrob. Chemother. , vol.58 , Issue.5 , pp. 1070-1073
    • Ibrahim, A.S.1    Edwards, J.E.2    Fu, Y.3    Spellberg, B.4
  • 317
    • 84950335447 scopus 로고    scopus 로고
    • Commensal bacteria-induced interleukin 1beta (IL-1beta) secreted by macrophages up-regulates hepcidin expression in hepatocytes by activating the bone morphogenetic protein signaling pathway
    • Shanmugam, N.K., Chen, K., Cherayil, B.J., Commensal bacteria-induced interleukin 1beta (IL-1beta) secreted by macrophages up-regulates hepcidin expression in hepatocytes by activating the bone morphogenetic protein signaling pathway. J. Biol. Chem. 290:51 (2015), 30637–30647.
    • (2015) J. Biol. Chem. , vol.290 , Issue.51 , pp. 30637-30647
    • Shanmugam, N.K.1    Chen, K.2    Cherayil, B.J.3
  • 318
    • 85040353411 scopus 로고    scopus 로고
    • Dopamine promotes cellular iron accumulation and oxidative stress responses in macrophages
    • Dichtl, S., Haschka, D., Nairz, M., Seifert, M., Volani, C., Lutz, O., Weiss, G., Dopamine promotes cellular iron accumulation and oxidative stress responses in macrophages. Biochem. Pharmacol. 148 (2018), 193–201.
    • (2018) Biochem. Pharmacol. , vol.148 , pp. 193-201
    • Dichtl, S.1    Haschka, D.2    Nairz, M.3    Seifert, M.4    Volani, C.5    Lutz, O.6    Weiss, G.7


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