메뉴 건너뛰기




Volumn 6, Issue 4, 2013, Pages 411-418

The regulation of iron metabolism in the mononuclear phagocyte system

Author keywords

divalent metal transporter 1; ferroportin 1; hepcidin; mononuclear phagocyte system; Transferrin receptor 1

Indexed keywords

ANIMALS; CATION TRANSPORT PROTEINS; HUMANS; IRON; MONONUCLEAR PHAGOCYTE SYSTEM; RECEPTORS, TRANSFERRIN;

EID: 84894184816     PISSN: 17474086     EISSN: 17474094     Source Type: Journal    
DOI: 10.1586/17474086.2013.814840     Document Type: Review
Times cited : (9)

References (82)
  • 2
    • 54549092697 scopus 로고    scopus 로고
    • Iron metabolism in the mononuclear phagocyte system
    • Kong WN. Iron metabolism in the mononuclear phagocyte system. Prog. Nat. Sci. 18, 1197-1202 (2008).
    • (2008) Prog. Nat. Sci. , vol.18 , pp. 1197-1202
    • Kong, W.N.1
  • 3
    • 84873338198 scopus 로고    scopus 로고
    • HRG1 Is essential for heme transport from the phagolysosome of macrophages during erythrophagocytosis
    • White C, Yuan X, Schmidt PJ et al. HRG1 Is essential for heme transport from the phagolysosome of macrophages during erythrophagocytosis. Cell Metab. 17(2), 261-270 (2013).
    • (2013) Cell Metab. , vol.17 , Issue.2 , pp. 261-270
    • White, C.1    Yuan, X.2    Schmidt, P.J.3
  • 4
    • 0035843134 scopus 로고    scopus 로고
    • Identification of the haemoglobin scavenger receptor
    • Kristiansen M, Graversen JH, Jacobsen C et al. Identification of the haemoglobin scavenger receptor. Nature 409(6817), 198-201 (2001).
    • (2001) Nature , vol.409 , Issue.6817 , pp. 198-201
    • Kristiansen, M.1    Graversen, J.H.2    Jacobsen, C.3
  • 5
    • 0030923630 scopus 로고    scopus 로고
    • The heme oxygenase system: A regulator of second messenger gases
    • Maines MD. The heme oxygenase system: a regulator of second messenger gases. Ann. Rev. Pharmacol. Toxicol. 37, 517-554 (1997).
    • (1997) Ann. Rev. Pharmacol. Toxicol. , vol.37 , pp. 517-554
    • Maines, M.D.1
  • 6
    • 78650676293 scopus 로고    scopus 로고
    • Dysfunction of the heme recycling system in heme oxygenase 1-deficient mice: Effects on macrophage viability and tissue iron distribution
    • Kovtunovych G, Eckhaus MA, Ghosh MC, Ollivierre-Wilson H, Rouault TA. Dysfunction of the heme recycling system in heme oxygenase 1-deficient mice: effects on macrophage viability and tissue iron distribution. Blood 116(26), 6054-6062 (2010).
    • (2010) Blood , vol.116 , Issue.26 , pp. 6054-6062
    • Kovtunovych, G.1    Eckhaus, M.A.2    Ghosh, M.C.3    Ollivierre-Wilson, H.4    Rouault, T.A.5
  • 7
    • 37549050907 scopus 로고    scopus 로고
    • Heme oxygenase-1 induction by NRF2 requires inactivation of the transcriptional repressor BACH1
    • Reichard JF, Motz GT, Puga A. Heme oxygenase-1 induction by NRF2 requires inactivation of the transcriptional repressor BACH1. Nucleic Acids Res. 35(21), 7074-7086 (2007).
    • (2007) Nucleic Acids Res. , vol.35 , Issue.21 , pp. 7074-7086
    • Reichard, J.F.1    Motz, G.T.2    Puga, A.3
  • 8
    • 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 et al. Heme controls ferroportin1 (FPN1) transcription involving Bach1, Nrf2 and a MARE/ARE sequence motif at position-7007 of the FPN1 promoter. Haematologica 95(8), 1261-1268 (2010).
    • (2010) Haematologica , vol.95 , Issue.8 , pp. 1261-1268
    • Marro, S.1    Chiabrando, D.2    Messana, E.3
  • 9
    • 25444449505 scopus 로고    scopus 로고
    • Lipopolysaccharide-induced heme oxygenase-1 expression in human monocytic cells is mediated via Nrf2 and protein kinase C
    • Rushworth SA, Chen XL, Mackman N, Ogborne RM, O'connell MA. Lipopolysaccharide-induced heme oxygenase-1 expression in human monocytic cells is mediated via Nrf2 and protein kinase C. J. Immunol. 175(7), 4408-4415 (2005).
    • (2005) J. Immunol. , vol.175 , Issue.7 , pp. 4408-4415
    • Rushworth, S.A.1    Chen, X.L.2    MacKman, N.3    Ogborne, R.M.4    O'Connell, M.A.5
  • 10
    • 77952752215 scopus 로고    scopus 로고
    • Regulation of heme oxygenase-1 gene by peptidoglycan involves the interaction of Elk-1 and C/EBPalpha to increase expression
    • Hung CC, Liu X, Kwon MY, Kang YH, Chung SW, Perrella MA. Regulation of heme oxygenase-1 gene by peptidoglycan involves the interaction of Elk-1 and C/EBPalpha to increase expression. Am. J. Physiol. Lung Cell Mol. Physiol. 298(6), L870-L879 (2010).
    • (2010) Am. J. Physiol. Lung Cell Mol. Physiol. , vol.298 , Issue.6
    • Hung, C.C.1    Liu, X.2    Kwon, M.Y.3    Kang, Y.H.4    Chung, S.W.5    Perrella, M.A.6
  • 11
    • 46249121630 scopus 로고    scopus 로고
    • Integrative survival response evoked by heme oxygenase-1 and heme metabolites
    • Pae HO, Kim EC, Chung HT. Integrative survival response evoked by heme oxygenase-1 and heme metabolites. J. Clin. Biochem. Nutr. 42(3), 197-203 (2008).
    • (2008) J. Clin. Biochem. Nutr. , vol.42 , Issue.3 , pp. 197-203
    • Pae, H.O.1    Kim, E.C.2    Chung, H.T.3
  • 12
    • 14244251815 scopus 로고    scopus 로고
    • Role of Ets-2 in the regulation of heme oxygenase-1 by endotoxin
    • Chung SW, Chen YH, Perrella MA. Role of Ets-2 in the regulation of heme oxygenase-1 by endotoxin. J. Biol. Chem.280(6), 4578-4584 (2005).
    • (2005) J. Biol. Chem. , vol.280 , Issue.6 , pp. 4578-4584
    • Chung, S.W.1    Chen, Y.H.2    Perrella, M.A.3
  • 13
    • 32044456746 scopus 로고    scopus 로고
    • Endotoxin-induced downregulation of Elk-3 facilitates heme oxygenase-1 induction in macrophages
    • Chung SW, Chen YH, Yet SF, Layne MD, Perrella MA. Endotoxin-induced downregulation of Elk-3 facilitates heme oxygenase-1 induction in macrophages. J. Immunol. 176(4), 2414-2420 (2006).
    • (2006) J. Immunol. , vol.176 , Issue.4 , pp. 2414-2420
    • Chung, S.W.1    Chen, Y.H.2    Yet, S.F.3    Layne, M.D.4    Perrella, M.A.5
  • 14
    • 79952162002 scopus 로고    scopus 로고
    • Regulation of cellular iron metabolism
    • Wang J, Pantopoulos K. Regulation of cellular iron metabolism. Biochem. J. 434(3), 365-381 (2011).
    • (2011) Biochem. J. , vol.434 , Issue.3 , pp. 365-381
    • Wang, J.1    Pantopoulos, K.2
  • 15
    • 0033769626 scopus 로고    scopus 로고
    • Interferongamma and lipopolysaccharide regulate the expression of Nramp2 and increase the uptake of iron from low relative molecular mass complexes by macrophages
    • Wardrop SL, Richardson DR. Interferongamma and lipopolysaccharide regulate the expression of Nramp2 and increase the uptake of iron from low relative molecular mass complexes by macrophages. Eur. J. Biochem. 267(22), 6586-6593 (2000).
    • (2000) Eur. J. Biochem. , vol.267 , Issue.22 , pp. 6586-6593
    • Wardrop, S.L.1    Richardson, D.R.2
  • 16
    • 0027184412 scopus 로고
    • Translational regulation via iron-responsive elements by the nitric oxide/NO-synthase pathway
    • Weiss G, Goossen B, Doppler W et al. Translational regulation via iron-responsive elements by the nitric oxide/NO-synthase pathway. EMBO J. 12(9), 3651-3657 (1993).
    • (1993) EMBO J. , vol.12 , Issue.9 , pp. 3651-3657
    • Weiss, G.1    Goossen, B.2    Doppler, W.3
  • 17
    • 0027301897 scopus 로고
    • Biosynthesis of nitric oxide activates iron regulatory factor in macrophages
    • Drapier JC, Hirling H, Wietzerbin J, Kaldy P, Kuhn LC. Biosynthesis of nitric oxide activates iron regulatory factor in macrophages. EMBO J. 12(9), 3643-3649 (1993).
    • (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
  • 18
    • 0032746973 scopus 로고    scopus 로고
    • Control of transferrin receptor expression via nitric oxide-mediated modulation of iron-regulatory protein 2
    • Kim S, Ponka P. Control of transferrin receptor expression via nitric oxide-mediated modulation of iron-regulatory protein 2. J. Biol. Chem. 274(46), 33035-33042 (1999).
    • (1999) J. Biol. Chem. , vol.274 , Issue.46 , pp. 33035-33042
    • Kim, S.1    Ponka, P.2
  • 19
    • 13444252613 scopus 로고    scopus 로고
    • Nitric oxide inhibits the degradation of IRP2
    • Wang J, Chen G, Pantopoulos K. Nitric oxide inhibits the degradation of IRP2. Mol. Cell. Biol. 25(4), 1347-1353 (2005).
    • (2005) Mol. Cell. Biol. , vol.25 , Issue.4 , pp. 1347-1353
    • Wang, J.1    Chen, G.2    Pantopoulos, K.3
  • 20
    • 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 DR, 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), 3211-3219 (1995).
    • (1995) Blood , vol.86 , Issue.8 , pp. 3211-3219
    • Richardson, D.R.1    Neumannova, V.2    Nagy, E.3    Ponka, P.4
  • 21
    • 33645830507 scopus 로고    scopus 로고
    • No nitric oxide for HO-1 from sodium nitroprusside
    • Schroder H. No nitric oxide for HO-1 from sodium nitroprusside. Mol. Pharmacol. 69(5), 1507-1509 (2006).
    • (2006) Mol. Pharmacol. , vol.69 , Issue.5 , pp. 1507-1509
    • Schroder, H.1
  • 22
    • 33644526911 scopus 로고    scopus 로고
    • Sodium nitroprusside promotes IRP2 degradation via an increase in intracellular iron and in the absence of S nitrosylation at C178
    • Wang J, Fillebeen C, Chen G, Andriopoulos B, Pantopoulos K. Sodium nitroprusside promotes IRP2 degradation via an increase in intracellular iron and in the absence of S nitrosylation at C178. Mol. Cell. Biol. 26(5), 1948-1954 (2006).
    • (2006) Mol. Cell. Biol. , vol.26 , Issue.5 , pp. 1948-1954
    • Wang, J.1    Fillebeen, C.2    Chen, G.3    Andriopoulos, B.4    Pantopoulos, K.5
  • 23
    • 0034089867 scopus 로고    scopus 로고
    • Effects of interferongamma and lipopolysaccharide on macrophage iron metabolism are mediated by nitric oxide-induced degradation of iron regulatory protein 2
    • Kim S, Ponka P. Effects of interferongamma and lipopolysaccharide on macrophage iron metabolism are mediated by nitric oxide-induced degradation of iron regulatory protein 2. J. Biol. Chem. 275(9), 6220-6226 (2000).
    • (2000) J. Biol. Chem. , vol.275 , Issue.9 , pp. 6220-6226
    • Kim, S.1    Ponka, P.2
  • 24
    • 0032006692 scopus 로고    scopus 로고
    • Nitric oxide-mediated induction of ferritin synthesis in J774 macrophages by inflammatory cytokines: Role of selective iron regulatory protein-2 downregulation
    • Recalcati S, Taramelli D, Conte D, Cairo G. Nitric oxide-mediated induction of ferritin synthesis in J774 macrophages by inflammatory cytokines: role of selective iron regulatory protein-2 downregulation. Blood 91(3), 1059-1066 (1998).
    • (1998) Blood , vol.91 , Issue.3 , pp. 1059-1066
    • Recalcati, S.1    Taramelli, D.2    Conte, D.3    Cairo, G.4
  • 25
    • 0028929741 scopus 로고
    • Nitric oxide signaling to iron-regulatory protein: Direct control of ferritin mRNA translation and transferrin receptor mRNA stability in transfected fibroblasts
    • Pantopoulos K, Hentze MW. Nitric oxide signaling to iron-regulatory protein: direct control of ferritin mRNA translation and transferrin receptor mRNA stability in transfected fibroblasts. Proc. Natl Acad. Sci. USA 92(5), 1267-1271 (1995).
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , Issue.5 , pp. 1267-1271
    • Pantopoulos, K.1    Hentze, M.W.2
  • 26
    • 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), 4148-4154 (2003).
    • (2003) Blood , vol.101 , Issue.10 , pp. 4148-4154
    • Ludwiczek, S.1    Aigner, E.2    Theurl, I.3    Weiss, G.4
  • 27
    • 33645512980 scopus 로고    scopus 로고
    • Function and mechanism of action of Dictyostelium Nramp1 (Slc11a1) in bacterial infection
    • Peracino B, Wagner C, Balest A et al. Function and mechanism of action of Dictyostelium Nramp1 (Slc11a1) in bacterial infection. Traffic 7(1), 22-38 (2006).
    • (2006) Traffic , vol.7 , Issue.1 , pp. 22-38
    • Peracino, B.1    Wagner, C.2    Balest, A.3
  • 28
    • 0035868324 scopus 로고    scopus 로고
    • Natural-resistance-associated macrophage protein 1 is an H+/bivalent cation antiporter
    • Goswami T, Bhattacharjee A, Babal P et al. Natural-resistance-associated macrophage protein 1 is an H+/bivalent cation antiporter. Biochem. J. 354(Pt 3), 511-519 (2001).
    • (2001) Biochem. J. , vol.354 , Issue.3 , pp. 511-519
    • Goswami, T.1    Bhattacharjee, A.2    Babal, P.3
  • 29
    • 65249166994 scopus 로고    scopus 로고
    • Nramp1 promotes efficient macrophage recycling of iron following erythrophagocytosis in vivo
    • Soe-Lin S, Apte SS, Andriopoulos B Jr et al. Nramp1 promotes efficient macrophage recycling of iron following erythrophagocytosis in vivo. Proc. Natl Acad. Sci. USA 106(14), 5960-5965 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , Issue.14 , pp. 5960-5965
    • Soe-Lin, S.1    Apte, S.S.2    Andriopoulos Jr., B.3
  • 30
    • 0036788722 scopus 로고    scopus 로고
    • Iron transporter Nramp2/DMT-1 is associated with the membrane of phagosomes in macrophages and Sertoli cells
    • Jabado N, Canonne-Hergaux F, Gruenheid S, Picard V, Gros P. Iron transporter Nramp2/DMT-1 is associated with the membrane of phagosomes in macrophages and Sertoli cells. Blood 100(7), 2617-2622 (2002).
    • (2002) Blood , vol.100 , Issue.7 , pp. 2617-2622
    • Jabado, N.1    Canonne-Hergaux, F.2    Gruenheid, S.3    Picard, V.4    Gros, P.5
  • 31
    • 77954541370 scopus 로고    scopus 로고
    • Both Nramp1. and DMT1 are necessary for efficient macrophage iron recycling
    • Soe-Lin S, Apte SS, Mikhael MR, Kayembe LK, Nie G, Ponka P. Both Nramp1 and DMT1 are necessary for efficient macrophage iron recycling. Exp. Hematol. 38(8), 609-617 (2010).
    • (2010) Exp. Hematol. , vol.38 , Issue.8 , pp. 609-617
    • Soe-Lin, S.1    Apte, S.S.2    Mikhael, M.R.3    Kayembe, L.K.4    Nie, G.5    Ponka, P.6
  • 32
    • 43449120402 scopus 로고    scopus 로고
    • Decreased DMT1. and increased ferroportin 1 expression is the mechanisms of reduced iron retention in macrophages by erythropoietin in rats
    • Kong WN, Zhao SE, Duan XL, Yang Z, Qian ZM, Chang YZ. Decreased DMT1 and increased ferroportin 1 expression is the mechanisms of reduced iron retention in macrophages by erythropoietin in rats. J. Cell. Biochem. 104(2), 629-641 (2008).
    • (2008) J. Cell. Biochem. , vol.104 , Issue.2 , pp. 629-641
    • Kong, W.N.1    Zhao, S.E.2    Duan, X.L.3    Yang, Z.4    Qian, Z.M.5    Chang, Y.Z.6
  • 33
    • 0037126002 scopus 로고    scopus 로고
    • Previously uncharacterized isoforms of divalent metal transporter (DMT)-1: Implications for regulation and cellular function
    • Hubert N, Hentze MW. Previously uncharacterized isoforms of divalent metal transporter (DMT)-1: implications for regulation and cellular function. Proc. Natl Acad. Sci. USA 99(19), 12345-12350 (2002).
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , Issue.19 , pp. 12345-12350
    • Hubert, N.1    Hentze, M.W.2
  • 34
    • 0036218170 scopus 로고    scopus 로고
    • Iron treatment downregulates DMT1 and IREG1 mRNA expression in Caco-2 cells
    • Martini LA, Tchack L, Wood RJ. Iron treatment downregulates DMT1 and IREG1 mRNA expression in Caco-2 cells. J. Nutr. 132(4), 693-696 (2002).
    • (2002) J. Nutr. , vol.132 , Issue.4 , pp. 693-696
    • Martini, L.A.1    Tchack, L.2    Wood, R.J.3
  • 35
    • 0035049419 scopus 로고    scopus 로고
    • Expression of the duodenal iron transporters divalent-metal transporter 1 and ferroportin 1 in iron deficiency and iron overload
    • Zoller H, Koch RO, Theurl I et al. Expression of the duodenal iron transporters divalent-metal transporter 1 and ferroportin 1 in iron deficiency and iron overload. Gastroenterology 120(6), 1412-1419 (2001).
    • (2001) Gastroenterology , vol.120 , Issue.6 , pp. 1412-1419
    • Zoller, H.1    Koch, R.O.2    Theurl, I.3
  • 36
    • 0036141414 scopus 로고    scopus 로고
    • Induction of Nramp2 in activated mouse macrophages is dissociated from regulation of the Nramp1, classical inflammatory genes, and genes involved in iron metabolism
    • Wardrop SL, Wells C, Ravasi T, Hume DA, Richardson DR. Induction of Nramp2 in activated mouse macrophages is dissociated from regulation of the Nramp1, classical inflammatory genes, and genes involved in iron metabolism. J. Leukoc. Biol. 71(1), 99-106 (2002).
    • (2002) J. Leukoc. Biol. , vol.71 , Issue.1 , pp. 99-106
    • Wardrop, S.L.1    Wells, C.2    Ravasi, T.3    Hume, D.A.4    Richardson, D.R.5
  • 38
    • 0035104119 scopus 로고    scopus 로고
    • LPS induction of gene expression in human monocytes
    • Guha M, Mackman N. LPS induction of gene expression in human monocytes. Cell Signal 13(2), 85-94 (2001).
    • (2001) Cell Signal , vol.13 , Issue.2 , pp. 85-94
    • Guha, M.1    MacKman, N.2
  • 39
    • 43249124764 scopus 로고    scopus 로고
    • Suppressive effects of Lithospermum erythrorhizon extracts on lipopolysaccharide-induced activation of AP-1 and NF-kappaB via mitogen-activated protein kinase pathways in mouse macrophage cells
    • Han KY, Kwon TH, Lee TH, Lee SJ, Kim SH, Kim J. Suppressive effects of Lithospermum erythrorhizon extracts on lipopolysaccharide-induced activation of AP-1 and NF-kappaB via mitogen-activated protein kinase pathways in mouse macrophage cells. BMB Rep. 41(4), 328-333 (2008).
    • (2008) BMB Rep. , vol.41 , Issue.4 , pp. 328-333
    • Han, K.Y.1    Kwon, T.H.2    Lee, T.H.3    Lee, S.J.4    Kim, S.H.5    Kim, J.6
  • 40
    • 0032104739 scopus 로고    scopus 로고
    • The human Nramp2 gene: Characterization of the gene structure, alternative splicing, promoter region and polymorphisms
    • Lee PL, Gelbart T, West C, Halloran C, Beutler E. The human Nramp2 gene: characterization of the gene structure, alternative splicing, promoter region and polymorphisms. Blood Cell. Mol. Dis. 24(2), 199-215 (1998).
    • (1998) Blood Cell. Mol. Dis. , vol.24 , Issue.2 , pp. 199-215
    • Lee, P.L.1    Gelbart, T.2    West, C.3    Halloran, C.4    Beutler, E.5
  • 41
    • 0035158459 scopus 로고    scopus 로고
    • The intracellular location of iron regulatory proteins is altered as a function of iron status in cell cultures and rat brain
    • Pinero DJ, Li N, Hu J, Beard JL, Connor JR. The intracellular location of iron regulatory proteins is altered as a function of iron status in cell cultures and rat brain. J. Nutr. 131(11), 2831-2836 (2001).
    • (2001) J. Nutr. , vol.131 , Issue.11 , pp. 2831-2836
    • Pinero, D.J.1    Li, N.2    Hu, J.3    Beard, J.L.4    Connor, J.R.5
  • 42
    • 25844499787 scopus 로고    scopus 로고
    • A physiological model to study iron recycling in macrophages
    • Delaby C, Pilard N, Hetet G et al. A physiological model to study iron recycling in macrophages. Exp. Cell Res. 310(1), 43-53 (2005).
    • (2005) Exp. Cell Res. , vol.310 , Issue.1 , pp. 43-53
    • Delaby, C.1    Pilard, N.2    Hetet, G.3
  • 43
    • 0034612245 scopus 로고    scopus 로고
    • Down-regulation of iron regulatory protein 1 gene expression by nitric oxide
    • Oliveira L, Drapier JC. Down-regulation of iron regulatory protein 1 gene expression by nitric oxide. Proc. Natl Acad. Sci. USA 97(12), 6550-6555 (2000).
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , Issue.12 , pp. 6550-6555
    • Oliveira, L.1    Drapier, J.C.2
  • 44
    • 0345688910 scopus 로고    scopus 로고
    • Iron loading and erythrophagocytosis increase ferroportin 1 (FPN1) expression in J774 macrophages
    • Knutson MD, Vafa MR, Haile DJ, Wessling-Resnick M. Iron loading and erythrophagocytosis increase ferroportin 1 (FPN1) expression in J774 macrophages. Blood 102(12), 4191-4197 (2003).
    • (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
  • 45
    • 13444252281 scopus 로고    scopus 로고
    • Iron release from macrophages after erythrophagocytosis is up-regulated by ferroportin 1 overexpression and downregulated by hepcidin
    • Knutson MD, Oukka M, Koss LM, Aydemir F, Wessling-Resnick M. Iron release from macrophages after erythrophagocytosis is up-regulated by ferroportin 1 overexpression and downregulated by hepcidin. Proc. Natl Acad. Sci. USA 102(5), 1324-1328 (2005).
    • (2005) Proc. Natl Acad. Sci. USA , 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
  • 46
    • 80051895753 scopus 로고    scopus 로고
    • Ferroportin1 deficiency in mouse macrophages impairs iron homeostasis and inflammatory responses
    • Zhang Z, Zhang F, An P et al. Ferroportin1 deficiency in mouse macrophages impairs iron homeostasis and inflammatory responses. Blood 118(7), 1912-1922 (2011).
    • (2011) Blood , vol.118 , Issue.7 , pp. 1912-1922
    • Zhang, Z.1    Zhang, F.2    An, P.3
  • 47
    • 28444488323 scopus 로고    scopus 로고
    • Presence of the iron exporter ferroportin at the plasma membrane of macrophages is enhanced by iron loading and down-regulated by hepcidin
    • Delaby C, Pilard N, Goncalves AS, Beaumont C, Canonne-Hergaux F. Presence of the iron exporter ferroportin at the plasma membrane of macrophages is enhanced by iron loading and down-regulated by hepcidin. Blood 106(12), 3979-3984 (2005).
    • (2005) Blood , vol.106 , Issue.12 , pp. 3979-3984
    • Delaby, C.1    Pilard, N.2    Goncalves, A.S.3    Beaumont, C.4    Canonne-Hergaux, F.5
  • 48
    • 65349126484 scopus 로고    scopus 로고
    • A ferroportin transcript that lacks an iron-responsive element enables duodenal and erythroid precursor cells to evade translational repression
    • Zhang DL, Hughes RM, Ollivierre-Wilson H, Ghosh MC, Rouault TA. A ferroportin transcript that lacks an iron-responsive element enables duodenal and erythroid precursor cells to evade translational repression. Cell Metab. 9(5), 461-473 (2009).
    • (2009) Cell Metab. , vol.9 , Issue.5 , pp. 461-473
    • Zhang, D.L.1    Hughes, R.M.2    Ollivierre-Wilson, H.3    Ghosh, M.C.4    Rouault, T.A.5
  • 50
    • 0034733635 scopus 로고    scopus 로고
    • A novel mammalian iron-regulated protein involved in intracellular iron metabolism
    • Abboud S, Haile DJ. A novel mammalian iron-regulated protein involved in intracellular iron metabolism. J. Biol. Chem. 275(26), 19906-19912 (2000).
    • (2000) J. Biol. Chem. , vol.275 , Issue.26 , pp. 19906-19912
    • Abboud, S.1    Haile, D.J.2
  • 51
    • 29644440335 scopus 로고    scopus 로고
    • Molecular analysis of increased iron status in moderately exercised rats
    • Liu YQ, Duan XL, Chang YZ, Wang HT, Qian ZM. Molecular analysis of increased iron status in moderately exercised rats. Mol. Cell Biochem. 282(1-2), 117-123 (2006).
    • (2006) Mol. Cell Biochem. , vol.282 , Issue.1-2 , pp. 117-123
    • Liu, Y.Q.1    Duan, X.L.2    Chang, Y.Z.3    Wang, H.T.4    Qian, Z.M.5
  • 52
    • 73749085208 scopus 로고    scopus 로고
    • Role of hepcidin in murine brain iron metabolism
    • Wang SM, Fu LJ, Duan XL et al. Role of hepcidin in murine brain iron metabolism. Cell. Mol. Life Sci. 67(1), 123-133 (2010).
    • (2010) Cell. Mol. Life Sci. , vol.67 , Issue.1 , pp. 123-133
    • Wang, S.M.1    Fu, L.J.2    Duan, X.L.3
  • 53
    • 58149483731 scopus 로고    scopus 로고
    • Hepcidin, an antimicrobial peptide is downregulated in ceruloplasmin-deficient mice
    • Guo P, Cui R, Chang YZ et al. Hepcidin, an antimicrobial peptide is downregulated in ceruloplasmin-deficient mice. Peptides 30(2), 262-266 (2009).
    • (2009) Peptides , vol.30 , Issue.2 , pp. 262-266
    • Guo, P.1    Cui, R.2    Chang, Y.Z.3
  • 54
    • 20444413054 scopus 로고    scopus 로고
    • Deregulation of proteins involved in iron metabolism in hepcidin-deficient mice
    • Viatte L, Lesbordes-Brion JC, Lou DQ et al. Deregulation of proteins involved in iron metabolism in hepcidin-deficient mice. Blood 105(12), 4861-4864 (2005).
    • (2005) Blood , vol.105 , Issue.12 , pp. 4861-4864
    • Viatte, L.1    Lesbordes-Brion, J.C.2    Lou, D.Q.3
  • 55
    • 10844258104 scopus 로고    scopus 로고
    • Hepcidin regulates cellular iron efflux by binding to ferroportin and inducing its internalization
    • Nemeth E, Tuttle MS, Powelson J et al. Hepcidin regulates cellular iron efflux by binding to ferroportin and inducing its internalization. Science 306(5704), 2090-2093 (2004).
    • (2004) Science , vol.306 , Issue.5704 , pp. 2090-2093
    • Nemeth, E.1    Tuttle, M.S.2    Powelson, J.3
  • 56
    • 34250865977 scopus 로고    scopus 로고
    • The molecular mechanism of hepcidin-mediated ferroportin down-regulation
    • De Domenico I, Ward DM, Langelier C et al. The molecular mechanism of hepcidin-mediated ferroportin down-regulation. Mol. Biol. Cell 18(7), 2569-2578 (2007).
    • (2007) Mol. Biol. Cell , vol.18 , Issue.7 , pp. 2569-2578
    • De Domenico, I.1    Ward, D.M.2    Langelier, C.3
  • 57
    • 62649135982 scopus 로고    scopus 로고
    • Hepcidin-induced internalization of ferroportin requires binding and cooperative interaction with Jak2
    • De Domenico I, Lo E, Ward DM, Kaplan J. Hepcidin-induced internalization of ferroportin requires binding and cooperative interaction with Jak2. Proc. Natl Acad. Sci. USA. 106(10), 3800-3805 (2009).
    • (2009) Proc. Natl Acad. Sci. USA. , vol.106 , Issue.10 , pp. 3800-3805
    • De Domenico, I.1    Lo, E.2    Ward, D.M.3    Kaplan, J.4
  • 58
    • 84862007363 scopus 로고    scopus 로고
    • Molecular mechanism of hepcidin-mediated ferroportin internalization requires ferroportin lysines, not tyrosines or JAK-STAT
    • Ross SL, Tran L, Winters A et al. Molecular mechanism of hepcidin-mediated ferroportin internalization requires ferroportin lysines, not tyrosines or JAK-STAT. Cell Metab. 15(6), 905-917 (2012).
    • (2012) Cell Metab. , vol.15 , Issue.6 , pp. 905-917
    • Ross, S.L.1    Tran, L.2    Winters, A.3
  • 59
    • 84862002810 scopus 로고    scopus 로고
    • Hepcidininduced endocytosis of ferroportin is dependent on ferroportin ubiquitination
    • Qiao B, Sugianto P, Fung E et al. Hepcidininduced endocytosis of ferroportin is dependent on ferroportin ubiquitination. Cell Metab. 15(6), 918-924 (2012).
    • (2012) Cell Metab. , vol.15 , Issue.6 , pp. 918-924
    • Qiao, B.1    Sugianto, P.2    Fung, E.3
  • 60
    • 0037131264 scopus 로고    scopus 로고
    • Regulation of reticuloendothelial iron transporter MTP1 (Slc11a3) by inflammation
    • Yang F, Liu XB, Quinones M, Melby PC, Ghio A, Haile DJ. Regulation of reticuloendothelial iron transporter MTP1 (Slc11a3) by inflammation. J. Biol. Chem. 277(42), 39786-39791 (2002).
    • (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
  • 61
    • 21544449756 scopus 로고    scopus 로고
    • Regulation of hepcidin and ferroportin expression by lipopolysaccharide in splenic macrophages
    • Liu XB, Nguyen NB, Marquess KD, Yang F, Haile DJ. Regulation of hepcidin and ferroportin expression by lipopolysaccharide in splenic macrophages. Blood Cells Mol. Dis. 35(1), 47-56 (2005).
    • (2005) Blood Cells Mol. Dis. , vol.35 , Issue.1 , pp. 47-56
    • Liu, X.B.1    Nguyen, N.B.2    Marquess, K.D.3    Yang, F.4    Haile, D.J.5
  • 62
    • 0038662619 scopus 로고    scopus 로고
    • Hepcidin, a putative mediator of anemia of inflammation, is a type II acute-phase protein
    • Nemeth E, Valore EV, 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), 2461-2463 (2003).
    • (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
  • 63
    • 41349106987 scopus 로고    scopus 로고
    • Autocrine formation of hepcidin induces iron retention in human monocytes
    • Theurl I, Theurl M, Seifert M et al. Autocrine formation of hepcidin induces iron retention in human monocytes. Blood 111(4), 2392-2399 (2008).
    • (2008) Blood , vol.111 , Issue.4 , pp. 2392-2399
    • Theurl, I.1    Theurl, M.2    Seifert, M.3
  • 64
    • 33646427702 scopus 로고    scopus 로고
    • TLR4-dependent hepcidin expression by myeloid cells in response to bacterial pathogens
    • Peyssonnaux C, Zinkernagel AS, Datta V, Lauth X, Johnson RS, Nizet V. TLR4-dependent hepcidin expression by myeloid cells in response to bacterial pathogens. Blood 107(9), 3727-3732 (2006).
    • (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
  • 66
    • 80052655782 scopus 로고    scopus 로고
    • The molecular pathogenesis of hereditary hemochromatosis
    • Babitt JL, Lin HY. The molecular pathogenesis of hereditary hemochromatosis. Semin. Liver. Dis. 31(3), 280-292 (2011).
    • (2011) Semin. Liver. Dis. , vol.31 , Issue.3 , pp. 280-292
    • Babitt, J.L.1    Lin, H.Y.2
  • 68
    • 0037100517 scopus 로고    scopus 로고
    • Novel mutation in ferroportin1 is associated with autosomal dominant hemochromatosis
    • Wallace DF, Pedersen P, Dixon JL et al. Novel mutation in ferroportin1 is associated with autosomal dominant hemochromatosis. Blood 100(2), 692-694 (2002).
    • (2002) Blood , vol.100 , Issue.2 , pp. 692-694
    • Wallace, D.F.1    Pedersen, P.2    Dixon, J.L.3
  • 69
    • 20844462571 scopus 로고    scopus 로고
    • In vitro functional analysis of human ferroportin (FPN) and hemochromatosis-associated FPN mutations
    • Schimanski LM, Drakesmith H, Merryweather-Clarke AT et al. In vitro functional analysis of human ferroportin (FPN) and hemochromatosis-associated FPN mutations. Blood 105(10), 4096-4102 (2005).
    • (2005) Blood , vol.105 , Issue.10 , pp. 4096-4102
    • Schimanski, L.M.1    Drakesmith, H.2    Merryweather-Clarke, A.T.3
  • 70
    • 21144435281 scopus 로고    scopus 로고
    • The molecular basis of ferroportinlinked hemochromatosis
    • De Domenico I, Ward DM, Nemeth E et al. The molecular basis of ferroportinlinked hemochromatosis. Proc. Natl Acad. Sci. USA 102(25), 8955-8960 (2005).
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , Issue.25 , pp. 8955-8960
    • De Domenico, I.1    Ward, D.M.2    Nemeth, E.3
  • 71
    • 77957340866 scopus 로고    scopus 로고
    • Ferroportin disease: A systematic metaanalysis of clinical and molecular findings
    • Mayr R, Janecke AR, Schranz M et al. Ferroportin disease: a systematic metaanalysis of clinical and molecular findings. J. Hepatol. 53(5), 941-949 (2010).
    • (2010) J. Hepatol. , vol.53 , Issue.5 , pp. 941-949
    • Mayr, R.1    Janecke, A.R.2    Schranz, M.3
  • 72
    • 67651087324 scopus 로고    scopus 로고
    • The molecular basis of hepcidin-resistant hereditary hemochromatosis
    • Fernandes A, Preza GC, Phung Y et al. The molecular basis of hepcidin-resistant hereditary hemochromatosis. Blood 114(2), 437-443 (2009).
    • (2009) Blood , vol.114 , Issue.2 , pp. 437-443
    • Fernandes, A.1    Preza, G.C.2    Phung, Y.3
  • 73
    • 13844270538 scopus 로고    scopus 로고
    • Autosomal dominant hereditary hemochromatosis associated with a novel ferroportin mutation and unique clinical features
    • Sham RL, Phatak PD, West C, Lee P, Andrews C, Beutler E. Autosomal dominant hereditary hemochromatosis associated with a novel ferroportin mutation and unique clinical features. Blood Cells Mol. Dis. 34(2), 157-161 (2005).
    • (2005) Blood Cells Mol. Dis. , vol.34 , Issue.2 , pp. 157-161
    • Sham, R.L.1    Phatak, P.D.2    West, C.3    Lee, P.4    Andrews, C.5    Beutler, E.6
  • 74
    • 20244388240 scopus 로고    scopus 로고
    • Mutant antimicrobial peptide hepcidin is associated with severe juvenile hemochromatosis
    • Roetto A, Papanikolaou G, Politou M et al. Mutant antimicrobial peptide hepcidin is associated with severe juvenile hemochromatosis. Nat. Genet. 33(1), 21-22 (2003).
    • (2003) Nat. Genet. , vol.33 , Issue.1 , pp. 21-22
    • Roetto, A.1    Papanikolaou, G.2    Politou, M.3
  • 75
    • 27144459908 scopus 로고    scopus 로고
    • Competitive regulation of hepcidin mRNA by soluble and cell-associated hemojuvelin
    • Lin L, Goldberg YP, Ganz T. Competitive regulation of hepcidin mRNA by soluble and cell-associated hemojuvelin. Blood 106(8), 2884-2889 (2005).
    • (2005) Blood , vol.106 , Issue.8 , pp. 2884-2889
    • Lin, L.1    Goldberg, Y.P.2    Ganz, T.3
  • 76
    • 0036728509 scopus 로고    scopus 로고
    • Iron and the anemia of chronic disease
    • Spivak JL. Iron and the anemia of chronic disease. Oncology (Williston Park) 16(9 Suppl. 10), 25-33 (2002).
    • (2002) Oncology (Williston Park) , vol.16 , Issue.9 SUPPL.10 , pp. 25-33
    • Spivak, J.L.1
  • 77
    • 0037111732 scopus 로고    scopus 로고
    • Inappropriate expression of hepcidin is associated with iron refractory anemia: Implications for the anemia of chronic disease
    • Weinstein DA, Roy CN, Fleming MD, Loda MF, Wolfsdorf JI, Andrews NC. Inappropriate expression of hepcidin is associated with iron refractory anemia: implications for the anemia of chronic disease. Blood 100(10), 3776-3781 (2002).
    • (2002) Blood , vol.100 , Issue.10 , pp. 3776-3781
    • Weinstein, D.A.1    Roy, C.N.2    Fleming, M.D.3    Loda, M.F.4    Wolfsdorf, J.I.5    Andrews, N.C.6
  • 79
    • 60249084746 scopus 로고    scopus 로고
    • Cell-autonomous and systemic contextdependent functions of iron regulatory protein 2 in mammalian iron metabolism
    • Ferring-Appel D, Hentze MW, Galy B. Cell-autonomous and systemic contextdependent functions of iron regulatory protein 2 in mammalian iron metabolism. Blood 113(3), 679-687 (2009).
    • (2009) Blood , vol.113 , Issue.3 , pp. 679-687
    • Ferring-Appel, D.1    Hentze, M.W.2    Galy, B.3
  • 81
    • 0021357863 scopus 로고
    • Monocyte transferrin-iron uptake in hereditary hemochromatosis
    • Sizemore DJ, Bassett ML. Monocyte transferrin-iron uptake in hereditary hemochromatosis. Am. J. Hematol. 16(4), 347-354 (1984).
    • (1984) Am. J. Hematol. , vol.16 , Issue.4 , pp. 347-354
    • Sizemore, D.J.1    Bassett, M.L.2
  • 82
    • 77749260592 scopus 로고    scopus 로고
    • Differential regulation of iron homeostasis during human macrophage polarized activation
    • Recalcati S, Locati M, Marini A et al. Differential regulation of iron homeostasis during human macrophage polarized activation. Eur. J. Immunol. 40(3), 824-835 (2010).
    • (2010) Eur. J. Immunol. , vol.40 , Issue.3 , pp. 824-835
    • Recalcati, S.1    Locati, M.2    Marini, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.