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Volumn 69, Issue 6, 2017, Pages 399-413

Systemic iron homeostasis and erythropoiesis

Author keywords

erythroferrone; erythropoietin; ferroportin; hepcidin; hypoxia; iron; IRP1; IRP2; transferrin receptor

Indexed keywords

CYTOKINE; HEPCIDIN; IRON; JANUS KINASE; CATION TRANSPORT PROTEIN; HAMP PROTEIN, HUMAN; IRON REGULATORY PROTEIN 1; IRON REGULATORY PROTEIN 2; IRP1 PROTEIN, HUMAN; IRP2 PROTEIN, HUMAN; METAL TRANSPORTING PROTEIN 1;

EID: 85017392997     PISSN: 15216543     EISSN: 15216551     Source Type: Journal    
DOI: 10.1002/iub.1629     Document Type: Review
Times cited : (83)

References (131)
  • 3
    • 84885768132 scopus 로고    scopus 로고
    • Systemic iron homeostasis
    • Ganz, T. (2013) Systemic iron homeostasis. Physiol. Rev. 93, 1721–1741.
    • (2013) Physiol. Rev. , vol.93 , pp. 1721-1741
    • Ganz, T.1
  • 4
    • 0026470429 scopus 로고
    • Contributions of heme and nonheme iron to human nutrition
    • Carpenter, C. E., and Mahoney, A. W. (1992) Contributions of heme and nonheme iron to human nutrition. Crit. Rev. Food Sci. Nutr. 31, 333–367.
    • (1992) Crit. Rev. Food Sci. Nutr. , vol.31 , pp. 333-367
    • Carpenter, C.E.1    Mahoney, A.W.2
  • 6
    • 84879585295 scopus 로고    scopus 로고
    • Multi-copper oxidases and human iron metabolism
    • Vashchenko, G., and MacGillivray, R. T. (2013) Multi-copper oxidases and human iron metabolism. Nutrients 5, 2289–2313.
    • (2013) Nutrients , vol.5 , pp. 2289-2313
    • Vashchenko, G.1    MacGillivray, R.T.2
  • 7
    • 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, M. A., Ghosh, M. C., Ollivierre-Wilson, H., and Rouault, T. A. (2010) Dysfunction of the heme recycling system in heme oxygenase 1-deficient mice: effects on macrophage viability and tissue iron distribution. Blood 116, 6054–6062.
    • (2010) Blood , vol.116 , pp. 6054-6062
    • Kovtunovych, G.1    Eckhaus, M.A.2    Ghosh, M.C.3    Ollivierre-Wilson, H.4    Rouault, T.A.5
  • 8
    • 84899746695 scopus 로고    scopus 로고
    • Quantitative proteomics identifies NCOA4 as the cargo receptor mediating ferritinophagy
    • Mancias, J. D., Wang, X., Gygi, S. P., Harper, J. W., and Kimmelman, A. C. (2014) Quantitative proteomics identifies NCOA4 as the cargo receptor mediating ferritinophagy. Nature 509, 105–109.
    • (2014) Nature , vol.509 , pp. 105-109
    • Mancias, J.D.1    Wang, X.2    Gygi, S.P.3    Harper, J.W.4    Kimmelman, A.C.5
  • 9
    • 84865565820 scopus 로고    scopus 로고
    • Ferroportin1 in hepatocytes and macrophages is required for the efficient mobilization of body iron stores in mice
    • Sep
    • Zhang, Z., Zhang, F., Guo, X., An, P., Tao, Y., and Wang, F. (2012) Ferroportin1 in hepatocytes and macrophages is required for the efficient mobilization of body iron stores in mice. Hepatology 56, 961–971. Sep
    • (2012) Hepatology , vol.56 , pp. 961-971
    • Zhang, Z.1    Zhang, F.2    Guo, X.3    An, P.4    Tao, Y.5    Wang, F.6
  • 10
    • 0028049495 scopus 로고
    • Regulators of iron balance in humans
    • Finch, C. (1994) Regulators of iron balance in humans. Blood 84, 1697–1702.
    • (1994) Blood , vol.84 , pp. 1697-1702
    • Finch, C.1
  • 11
    • 84893457195 scopus 로고    scopus 로고
    • Primitive and definitive erythropoiesis in mammals
    • Palis, J. (2014) Primitive and definitive erythropoiesis in mammals. Front. Physiol. 5, 3.
    • (2014) Front. Physiol. , vol.5 , pp. 3
    • Palis, J.1
  • 12
    • 0031028178 scopus 로고    scopus 로고
    • Tissue-specific regulation of iron metabolism and heme synthesis: distinct control mechanisms in erythroid cells
    • Ponka, P. (1997) Tissue-specific regulation of iron metabolism and heme synthesis: distinct control mechanisms in erythroid cells. Blood 89, 1–25.
    • (1997) Blood , vol.89 , pp. 1-25
    • Ponka, P.1
  • 13
    • 33644748145 scopus 로고    scopus 로고
    • Mitoferrin is essential for erythroid iron assimilation
    • Shaw, G. C., Cope, J. J., Li, L., Corson, K., Hersey, C., et al. (2006) Mitoferrin is essential for erythroid iron assimilation. Nature 440, 96–100.
    • (2006) Nature , vol.440 , pp. 96-100
    • Shaw, G.C.1    Cope, J.J.2    Li, L.3    Corson, K.4    Hersey, C.5
  • 14
    • 34347375300 scopus 로고    scopus 로고
    • Direct interorganellar transfer of iron from endosome to mitochondrion
    • Sheftel, A. D., Zhang, A. S., Brown, C., Shirihai, O. S., and Ponka, P. (2007) Direct interorganellar transfer of iron from endosome to mitochondrion. Blood 1, 125–132.
    • (2007) Blood , vol.1 , pp. 125-132
    • Sheftel, A.D.1    Zhang, A.S.2    Brown, C.3    Shirihai, O.S.4    Ponka, P.5
  • 15
    • 0032959574 scopus 로고    scopus 로고
    • Transferrin receptor is necessary for development of erythrocytes and the nervous system
    • Levy, J. E., Jin, O., Fujiwara, Y., Kuo, F., and Andrews, N. C. (1999) Transferrin receptor is necessary for development of erythrocytes and the nervous system. Nat. Genet. 21, 396–399.
    • (1999) Nat. Genet. , vol.21 , pp. 396-399
    • Levy, J.E.1    Jin, O.2    Fujiwara, Y.3    Kuo, F.4    Andrews, N.C.5
  • 16
    • 84901705651 scopus 로고    scopus 로고
    • Global transcriptome analyses of human and murine terminal erythroid differentiation
    • An, X., Schulz, V. P., Li, J., Wu, K., Liu, J., et al. (2014) Global transcriptome analyses of human and murine terminal erythroid differentiation. Blood 123, 3466–3477.
    • (2014) Blood , vol.123 , pp. 3466-3477
    • An, X.1    Schulz, V.P.2    Li, J.3    Wu, K.4    Liu, J.5
  • 17
    • 84945945809 scopus 로고    scopus 로고
    • Beyond soluble transferrin receptor: old challenges and new horizons
    • Harms, K., and Kaiser, T. (2015) Beyond soluble transferrin receptor: old challenges and new horizons. Best Pract. Res. Clin. Endocrinol. Metab. 29, 799–810.
    • (2015) Best Pract. Res. Clin. Endocrinol. Metab. , vol.29 , pp. 799-810
    • Harms, K.1    Kaiser, T.2
  • 19
    • 84946615455 scopus 로고    scopus 로고
    • Ferritinophagy via NCOA4 is required for erythropoiesis and is regulated by iron dependent HERC2-mediated proteolysis
    • Mancias, J. D., Pontano Vaites, L., Nissim, S., Biancur, D. E., Kim, A. J., et al. (2015) Ferritinophagy via NCOA4 is required for erythropoiesis and is regulated by iron dependent HERC2-mediated proteolysis. Elife 4, 05.
    • (2015) Elife , vol.4 , pp. 05
    • Mancias, J.D.1    Pontano Vaites, L.2    Nissim, S.3    Biancur, D.E.4    Kim, A.J.5
  • 20
    • 79952162002 scopus 로고    scopus 로고
    • Regulation of cellular iron metabolism
    • Wang, J., and Pantopoulos, K. (2011) Regulation of cellular iron metabolism. Biochem. J. 434, 365–381.
    • (2011) Biochem. J. , vol.434 , pp. 365-381
    • Wang, J.1    Pantopoulos, K.2
  • 21
    • 10844282789 scopus 로고    scopus 로고
    • Mammalian tissue oxygen levels modulate iron-regulatory protein activities in vivo
    • Meyron-Holtz, E. G., Ghosh, M. C., and Rouault, T. A. (2004) Mammalian tissue oxygen levels modulate iron-regulatory protein activities in vivo. Science 306, 2087–2090.
    • (2004) Science , vol.306 , pp. 2087-2090
    • Meyron-Holtz, E.G.1    Ghosh, M.C.2    Rouault, T.A.3
  • 22
    • 34247628002 scopus 로고    scopus 로고
    • Iron-regulatory proteins limit hypoxia-inducible factor-2alpha expression in iron deficiency
    • Sanchez, M., Galy, B., Muckenthaler, M. U., and Hentze, M. W. (2007) Iron-regulatory proteins limit hypoxia-inducible factor-2alpha expression in iron deficiency. Nat. Struct. Mol. Biol. 14, 420–426.
    • (2007) Nat. Struct. Mol. Biol. , vol.14 , pp. 420-426
    • Sanchez, M.1    Galy, B.2    Muckenthaler, M.U.3    Hentze, M.W.4
  • 23
    • 84904764584 scopus 로고    scopus 로고
    • The IRP/IRE system in vivo: insights from mouse models
    • Wilkinson, N., and Pantopoulos, K. (2014) The IRP/IRE system in vivo: insights from mouse models. Front. Pharmacol. 5, 176.
    • (2014) Front. Pharmacol. , vol.5 , pp. 176
    • Wilkinson, N.1    Pantopoulos, K.2
  • 24
    • 84894387582 scopus 로고    scopus 로고
    • Hypoxia-inducible factors link iron homeostasis and erythropoiesis
    • Shah, Y. M., and Xie, L. (2014) Hypoxia-inducible factors link iron homeostasis and erythropoiesis. Gastroenterology 146, 630–642.
    • (2014) Gastroenterology , vol.146 , pp. 630-642
    • Shah, Y.M.1    Xie, L.2
  • 26
    • 58749094789 scopus 로고    scopus 로고
    • Intestinal hypoxia-inducible transcription factors are essential for iron absorption following iron deficiency
    • Shah, Y. M., Matsubara, T., Ito, S., Yim, S. H., and Gonzalez, F. J. (2009) Intestinal hypoxia-inducible transcription factors are essential for iron absorption following iron deficiency. Cell Metab. 9, 152–164.
    • (2009) Cell Metab. , vol.9 , pp. 152-164
    • Shah, Y.M.1    Matsubara, T.2    Ito, S.3    Yim, S.H.4    Gonzalez, F.J.5
  • 27
    • 79958146087 scopus 로고    scopus 로고
    • Hypoxia-inducible factor-2alpha mediates the adaptive increase of intestinal ferroportin during iron deficiency in mice
    • Taylor, M., Qu, A., Anderson, E. R., Matsubara, T., Martin, A., et al. (2011) Hypoxia-inducible factor-2alpha mediates the adaptive increase of intestinal ferroportin during iron deficiency in mice. Gastroenterology 140, 2044–2055.
    • (2011) Gastroenterology , vol.140 , pp. 2044-2055
    • Taylor, M.1    Qu, A.2    Anderson, E.R.3    Matsubara, T.4    Martin, A.5
  • 28
    • 77956327702 scopus 로고    scopus 로고
    • Intestinal ferritin h is required for an accurate control of iron absorption
    • Vanoaica, L., Darshan, D., Richman, L., Schumann, K., and Kuhn, L. C. (2010) Intestinal ferritin h is required for an accurate control of iron absorption. Cell Metab. 12, 273–282.
    • (2010) Cell Metab. , vol.12 , pp. 273-282
    • Vanoaica, L.1    Darshan, D.2    Richman, L.3    Schumann, K.4    Kuhn, L.C.5
  • 29
    • 84875805891 scopus 로고    scopus 로고
    • Iron regulatory proteins control a mucosal block to intestinal iron absorption
    • Galy, B., Ferring-Appel, D., Becker, C., Gretz, N., Grone, H. J., et al. (2013) Iron regulatory proteins control a mucosal block to intestinal iron absorption. Cell Rep. 3, 844–857.
    • (2013) Cell Rep. , vol.3 , pp. 844-857
    • Galy, B.1    Ferring-Appel, D.2    Becker, C.3    Gretz, N.4    Grone, H.J.5
  • 30
    • 23044503950 scopus 로고    scopus 로고
    • Microcytic anemia, erythropoietic protoporphyria and neurodegeneration in mice with targeted deletion of iron regulatory protein 2
    • Cooperman, S. S., Meyron-Holtz, E. G., Olivierre-Wilson, H., Ghosh, M. C., McConnell, J. P., and Rouault, T. A., et al. (2005) Microcytic anemia, erythropoietic protoporphyria and neurodegeneration in mice with targeted deletion of iron regulatory protein 2. Blood 106, 1084–1091.
    • (2005) Blood , vol.106 , pp. 1084-1091
    • Cooperman, S.S.1    Meyron-Holtz, E.G.2    Olivierre-Wilson, H.3    Ghosh, M.C.4    McConnell, J.P.5    Rouault, T.A.6
  • 31
    • 27144467097 scopus 로고    scopus 로고
    • Altered body iron distribution and microcytosis in mice deficient for iron regulatory protein 2 (IRP2)
    • Galy, B., Ferring, D., Minana, B., Bell, O., Janser, H. G., et al. (2005) Altered body iron distribution and microcytosis in mice deficient for iron regulatory protein 2 (IRP2). Blood 106, 2580–2589.
    • (2005) Blood , vol.106 , pp. 2580-2589
    • Galy, B.1    Ferring, D.2    Minana, B.3    Bell, O.4    Janser, H.G.5
  • 32
    • 33947584856 scopus 로고    scopus 로고
    • Regulation of protein synthesis by the heme-regulated eIF2alpha kinase: relevance to anemias
    • Chen, J. J. (2007) Regulation of protein synthesis by the heme-regulated eIF2alpha kinase: relevance to anemias. Blood 109, 2693–2699.
    • (2007) Blood , vol.109 , pp. 2693-2699
    • Chen, J.J.1
  • 33
    • 33646548593 scopus 로고    scopus 로고
    • Remodeling the regulation of iron metabolism during erythroid differentiation to ensure efficient heme biosynthesis
    • Schranzhofer, M., Schifrer, M., Cabrera, J. A., Kopp, S., Chiba, P., et al. (2006) Remodeling the regulation of iron metabolism during erythroid differentiation to ensure efficient heme biosynthesis. Blood 107, 4159–4167.
    • (2006) Blood , vol.107 , pp. 4159-4167
    • Schranzhofer, M.1    Schifrer, M.2    Cabrera, J.A.3    Kopp, S.4    Chiba, P.5
  • 34
    • 52649091181 scopus 로고    scopus 로고
    • Hematopoietic-specific Stat5-null mice display microcytic hypochromic anemia associated with reduced transferrin receptor gene expression
    • Zhu, B. M., McLaughlin, S. K., Na, R., Liu, J., Cui, Y., et al. (2008) Hematopoietic-specific Stat5-null mice display microcytic hypochromic anemia associated with reduced transferrin receptor gene expression. Blood 112, 2071–2080.
    • (2008) Blood , vol.112 , pp. 2071-2080
    • Zhu, B.M.1    McLaughlin, S.K.2    Na, R.3    Liu, J.4    Cui, Y.5
  • 35
    • 84862291307 scopus 로고    scopus 로고
    • N- and C-terminal transactivation domains of GATA1 protein coordinate hematopoietic program
    • Kaneko, H., Kobayashi, E., Yamamoto, M., and Shimizu, R. (2012) N- and C-terminal transactivation domains of GATA1 protein coordinate hematopoietic program. J. Biol. Chem. 287, 21439–21449.
    • (2012) J. Biol. Chem. , vol.287 , pp. 21439-21449
    • Kaneko, H.1    Kobayashi, E.2    Yamamoto, M.3    Shimizu, R.4
  • 36
    • 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., et al. (2004) Hepcidin regulates cellular iron efflux by binding to ferroportin and inducing its internalization. Science 306, 2090–2093.
    • (2004) Science , vol.306 , pp. 2090-2093
    • Nemeth, E.1    Tuttle, M.S.2    Powelson, J.3    Vaughn, M.B.4    Donovan, A.5
  • 37
    • 0035896642 scopus 로고    scopus 로고
    • Hepcidin, a urinary antimicrobial peptide synthesized in the liver
    • Park, C. H., Valore, E. V., Waring, A. J., and Ganz, T. (2001) Hepcidin, a urinary antimicrobial peptide synthesized in the liver. J. Biol. Chem. 276, 7806–7810.
    • (2001) J. Biol. Chem. , vol.276 , pp. 7806-7810
    • Park, C.H.1    Valore, E.V.2    Waring, A.J.3    Ganz, T.4
  • 38
    • 0035896581 scopus 로고    scopus 로고
    • A new mouse liver-specific gene, encoding a protein homologous to human antimicrobial peptide hepcidin, is overexpressed during iron overload
    • Pigeon, C., Ilyin, G., Courselaud, B., Leroyer, P., Turlin, B., et al. (2001) A new mouse liver-specific gene, encoding a protein homologous to human antimicrobial peptide hepcidin, is overexpressed during iron overload. J. Biol. Chem. 276, 7811–7819.
    • (2001) J. Biol. Chem. , vol.276 , pp. 7811-7819
    • Pigeon, C.1    Ilyin, G.2    Courselaud, B.3    Leroyer, P.4    Turlin, B.5
  • 39
    • 84055190801 scopus 로고    scopus 로고
    • Minihepcidins are rationally designed small peptides that mimic hepcidin activity in mice and may be useful for the treatment of iron overload
    • Preza, G. C., Ruchala, P., Pinon, R., Ramos, E., Qiao, B., et al. (2011) Minihepcidins are rationally designed small peptides that mimic hepcidin activity in mice and may be useful for the treatment of iron overload. J. Clin. Invest. 121, 4880–4888.
    • (2011) J. Clin. Invest. , vol.121 , pp. 4880-4888
    • Preza, G.C.1    Ruchala, P.2    Pinon, R.3    Ramos, E.4    Qiao, B.5
  • 40
    • 84902194073 scopus 로고    scopus 로고
    • Targeted disruption of hepcidin in the liver recapitulates the hemochromatotic phenotype
    • Zumerle, S., Mathieu, J. R., Delga, S., Heinis, M., Viatte, L., et al. (2014) Targeted disruption of hepcidin in the liver recapitulates the hemochromatotic phenotype. Blood 123, 3646–3650.
    • (2014) Blood , vol.123 , pp. 3646-3650
    • Zumerle, S.1    Mathieu, J.R.2    Delga, S.3    Heinis, M.4    Viatte, L.5
  • 41
    • 84929575005 scopus 로고    scopus 로고
    • Hepcidin: regulation of the master iron regulator
    • Rishi, G., Wallace, D. F., and Subramaniam, V. N. (2015) Hepcidin: regulation of the master iron regulator. Biosci. Rep. 35, e00192.
    • (2015) Biosci. Rep. , vol.35
    • Rishi, G.1    Wallace, D.F.2    Subramaniam, V.N.3
  • 42
    • 84937979159 scopus 로고    scopus 로고
    • Iron homeostasis in host defence and inflammation
    • Ganz, T., and Nemeth, E. (2015) Iron homeostasis in host defence and inflammation. Nat. Rev. Immunol. 15, 500–510.
    • (2015) Nat. Rev. Immunol. , vol.15 , pp. 500-510
    • Ganz, T.1    Nemeth, E.2
  • 43
    • 77955005442 scopus 로고    scopus 로고
    • Hepcidin mediates transcriptional changes that modulate acute cytokine-induced inflammatory responses in mice
    • De Domenico, I., Zhang, T. Y., Koening, C. L., Branch, R. W., London, N., et al. (2010) Hepcidin mediates transcriptional changes that modulate acute cytokine-induced inflammatory responses in mice. J. Clin. Invest. 120, 2395–2405.
    • (2010) J. Clin. Invest. , vol.120 , pp. 2395-2405
    • De Domenico, I.1    Zhang, T.Y.2    Koening, C.L.3    Branch, R.W.4    London, N.5
  • 44
    • 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., et al. (2011) Low hepcidin accounts for the proinflammatory status associated with iron deficiency. Blood 118, 736–746.
    • (2011) Blood , vol.118 , pp. 736-746
    • Pagani, A.1    Nai, A.2    Corna, G.3    Bosurgi, L.4    Rovere-Querini, P.5
  • 45
    • 84952802841 scopus 로고    scopus 로고
    • Iron and the liver
    • Pietrangelo, A. (2016) Iron and the liver. Liver Int. 36, 116–123.
    • (2016) Liver Int. , vol.36 , pp. 116-123
    • Pietrangelo, A.1
  • 46
    • 0035902605 scopus 로고    scopus 로고
    • Lack of hepcidin gene expression and severe tissue iron overload in upstream stimulatory factor 2 (USF2) knockout mice
    • Nicolas, G., Bennoun, M., Devaux, I., Beaumont, C., Grandchamp, B., et al. (2001) Lack of hepcidin gene expression and severe tissue iron overload in upstream stimulatory factor 2 (USF2) knockout mice. Proc. Natl. Acad. Sci. USA 98, 8780–8785.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 8780-8785
    • Nicolas, G.1    Bennoun, M.2    Devaux, I.3    Beaumont, C.4    Grandchamp, B.5
  • 48
    • 20244388240 scopus 로고    scopus 로고
    • Mutant antimicrobial peptide hepcidin is associated with severe juvenile hemochromatosis
    • Roetto, A., Papanikolaou, G., Politou, M., Alberti, F., Girelli, D., et al. (2003) Mutant antimicrobial peptide hepcidin is associated with severe juvenile hemochromatosis. Nat. Genet. 33, 21–22.
    • (2003) Nat. Genet. , vol.33 , pp. 21-22
    • Roetto, A.1    Papanikolaou, G.2    Politou, M.3    Alberti, F.4    Girelli, D.5
  • 49
    • 9144252017 scopus 로고    scopus 로고
    • Mutations in HFE2 cause iron overload in chromosome 1q-linked juvenile hemochromatosis
    • Papanikolaou, G., Samuels, M. E., Ludwig, E. H., MacDonald, M. L., Franchini, P. L., et al. (2004) Mutations in HFE2 cause iron overload in chromosome 1q-linked juvenile hemochromatosis. Nat. Genet. 36, 77–82.
    • (2004) Nat. Genet. , vol.36 , pp. 77-82
    • Papanikolaou, G.1    Samuels, M.E.2    Ludwig, E.H.3    MacDonald, M.L.4    Franchini, P.L.5
  • 50
    • 0037460697 scopus 로고    scopus 로고
    • Disrupted hepcidin regulation in HFE-associated haemochromatosis and the liver as a regulator of body iron homoeostasis
    • Bridle, K. R., Frazer, D. M., Wilkins, S. J., Dixon, J. L., Purdie, D. M., et al. (2003) Disrupted hepcidin regulation in HFE-associated haemochromatosis and the liver as a regulator of body iron homoeostasis. Lancet 361, 669–673.
    • (2003) Lancet , vol.361 , pp. 669-673
    • Bridle, K.R.1    Frazer, D.M.2    Wilkins, S.J.3    Dixon, J.L.4    Purdie, D.M.5
  • 51
    • 13544250486 scopus 로고    scopus 로고
    • Hepcidin is decreased in TFR2 hemochromatosis
    • Nemeth, E., Roetto, A., Garozzo, G., Ganz, T., and Camaschella, C. (2005) Hepcidin is decreased in TFR2 hemochromatosis. Blood 105, 1803–1806.
    • (2005) Blood , vol.105 , pp. 1803-1806
    • Nemeth, E.1    Roetto, A.2    Garozzo, G.3    Ganz, T.4    Camaschella, C.5
  • 52
    • 79960504861 scopus 로고    scopus 로고
    • Knockout mouse models of iron homeostasis
    • Fleming, R. E., Feng, Q., and Britton, R. S. (2011) Knockout mouse models of iron homeostasis. Annu. Rev. Nutr. 31, 117–137.
    • (2011) Annu. Rev. Nutr. , vol.31 , pp. 117-137
    • Fleming, R.E.1    Feng, Q.2    Britton, R.S.3
  • 53
    • 84937525787 scopus 로고    scopus 로고
    • SLC39A14 is required for the development of hepatocellular iron overload in murine models of hereditary hemochromatosis
    • Jenkitkasemwong, S., Wang, C. Y., Coffey, R., Zhang, W., Chan, A., et al. (2015) SLC39A14 is required for the development of hepatocellular iron overload in murine models of hereditary hemochromatosis. Cell Metab. 22, 138–150.
    • (2015) Cell Metab. , vol.22 , pp. 138-150
    • Jenkitkasemwong, S.1    Wang, C.Y.2    Coffey, R.3    Zhang, W.4    Chan, A.5
  • 54
    • 42649118442 scopus 로고    scopus 로고
    • Mutations in TMPRSS6 cause iron-refractory iron deficiency anemia (IRIDA)
    • May
    • Finberg, K. E., Heeney, M. M., Campagna, D. R., Aydinok, Y., Pearson, H. A., et al. (2008) Mutations in TMPRSS6 cause iron-refractory iron deficiency anemia (IRIDA). Nat. Genet. 40, 569–571. May
    • (2008) Nat. Genet. , vol.40 , pp. 569-571
    • Finberg, K.E.1    Heeney, M.M.2    Campagna, D.R.3    Aydinok, Y.4    Pearson, H.A.5
  • 55
    • 84958780878 scopus 로고    scopus 로고
    • Hepcidin regulation in the anemia of inflammation
    • Wang, C. Y., and Babitt, J. L. (2016) Hepcidin regulation in the anemia of inflammation. Curr. Opin. Hematol. 23, 189–197.
    • (2016) Curr. Opin. Hematol. , vol.23 , pp. 189-197
    • Wang, C.Y.1    Babitt, J.L.2
  • 56
    • 14744278436 scopus 로고    scopus 로고
    • Anemia of chronic disease
    • Weiss, G., and Goodnough, L. T. (2005) Anemia of chronic disease. N. Engl. J. Med. 352, 1011–1023.
    • (2005) N. Engl. J. Med. , vol.352 , pp. 1011-1023
    • Weiss, G.1    Goodnough, L.T.2
  • 57
    • 0037093202 scopus 로고    scopus 로고
    • Regulation of ferritin genes and protein
    • Torti, F. M., and Torti, S. V. (2002) Regulation of ferritin genes and protein. Blood 99, 3505–3516.
    • (2002) Blood , vol.99 , pp. 3505-3516
    • Torti, F.M.1    Torti, S.V.2
  • 58
    • 84926660351 scopus 로고    scopus 로고
    • A novel inflammatory pathway mediating rapid hepcidin-independent hypoferremia
    • Guida, C., Altamura, S., Klein, F. A., Galy, B., Boutros, M., et al. (2015) A novel inflammatory pathway mediating rapid hepcidin-independent hypoferremia. Blood 2, 2265–2275.
    • (2015) Blood , vol.2 , pp. 2265-2275
    • Guida, C.1    Altamura, S.2    Klein, F.A.3    Galy, B.4    Boutros, M.5
  • 59
    • 84977633506 scopus 로고    scopus 로고
    • Pharmacological targeting of the hepcidin/ferroportin axis
    • Sebastiani, G., Wilkinson, N., and Pantopoulos, K. (2016) Pharmacological targeting of the hepcidin/ferroportin axis. Front. Pharmacol. 7, 160.
    • (2016) Front. Pharmacol. , vol.7 , pp. 160
    • Sebastiani, G.1    Wilkinson, N.2    Pantopoulos, K.3
  • 60
    • 33646370235 scopus 로고    scopus 로고
    • Bone morphogenetic protein signaling by hemojuvelin regulates hepcidin expression
    • May
    • Babitt, J. L., Huang, F. W., Wrighting, D. M., Xia, Y., Sidis, Y., et al. (2006) Bone morphogenetic protein signaling by hemojuvelin regulates hepcidin expression. Nat. Genet. 38, 531–539. May
    • (2006) Nat. Genet. , vol.38 , pp. 531-539
    • Babitt, J.L.1    Huang, F.W.2    Wrighting, D.M.3    Xia, Y.4    Sidis, Y.5
  • 61
  • 62
    • 63449103712 scopus 로고    scopus 로고
    • BMP6 is a key endogenous regulator of hepcidin expression and iron metabolism
    • Andriopoulos, B., Jr., Corradini, E., Xia, Y., Faasse, S. A., Chen, S., et al. (2009) BMP6 is a key endogenous regulator of hepcidin expression and iron metabolism. Nat. Genet. 1, 482–487.
    • (2009) Nat. Genet. , vol.1 , pp. 482-487
    • Andriopoulos, B.1    Corradini, E.2    Xia, Y.3    Faasse, S.A.4    Chen, S.5
  • 64
    • 85014966092 scopus 로고    scopus 로고
    • Endothelial cells produce bone morphogenetic protein 6 required for iron homeostasis in mice
    • Canali, S., Zumbrennen-Bullough, K. B., Core, A. B., Wang, C. Y., Nairz, M., et al. (2017) Endothelial cells produce bone morphogenetic protein 6 required for iron homeostasis in mice. Blood 129, 405–414.
    • (2017) Blood , vol.129 , pp. 405-414
    • Canali, S.1    Zumbrennen-Bullough, K.B.2    Core, A.B.3    Wang, C.Y.4    Nairz, M.5
  • 65
    • 79960674973 scopus 로고    scopus 로고
    • Regulation of TMPRSS6 by BMP6 and iron in human cells and mice
    • Meynard, D., Vaja, V., Sun, C. C., Corradini, E., Chen, S., et al. (2011) Regulation of TMPRSS6 by BMP6 and iron in human cells and mice. Blood 118, 747–756.
    • (2011) Blood , vol.118 , pp. 747-756
    • Meynard, D.1    Vaja, V.2    Sun, C.C.3    Corradini, E.4    Chen, S.5
  • 66
    • 56449096622 scopus 로고    scopus 로고
    • The serine protease matriptase-2 (TMPRSS6) inhibits hepcidin activation by cleaving membrane hemojuvelin
    • Silvestri, L., Pagani, A., Nai, A., De Domenico, I., Kaplan, J., and Camaschella, C. (2008) The serine protease matriptase-2 (TMPRSS6) inhibits hepcidin activation by cleaving membrane hemojuvelin. Cell Metab. 8, 502–511.
    • (2008) Cell Metab. , vol.8 , pp. 502-511
    • Silvestri, L.1    Pagani, A.2    Nai, A.3    De Domenico, I.4    Kaplan, J.5    Camaschella, C.6
  • 67
    • 79551629285 scopus 로고    scopus 로고
    • Suppression of hepatic hepcidin expression in response to acute iron deprivation is associated with an increase of matriptase-2 protein
    • Zhang, A. S., Anderson, S. A., Wang, J., Yang, F., DeMaster, K., et al. (2011) Suppression of hepatic hepcidin expression in response to acute iron deprivation is associated with an increase of matriptase-2 protein. Blood 117, 1687–1699.
    • (2011) Blood , vol.117 , pp. 1687-1699
    • Zhang, A.S.1    Anderson, S.A.2    Wang, J.3    Yang, F.4    DeMaster, K.5
  • 68
    • 84952639186 scopus 로고    scopus 로고
    • Differing impact of the deletion of hemochromatosis-associated molecules HFE and transferrin receptor-2 on the iron phenotype of mice lacking bone morphogenetic protein 6 or hemojuvelin
    • Latour, C., Besson-Fournier, C., Meynard, D., Silvestri, L., Gourbeyre, O., et al. (2016) Differing impact of the deletion of hemochromatosis-associated molecules HFE and transferrin receptor-2 on the iron phenotype of mice lacking bone morphogenetic protein 6 or hemojuvelin. Hepatology 63, 126–137.
    • (2016) Hepatology , vol.63 , pp. 126-137
    • Latour, C.1    Besson-Fournier, C.2    Meynard, D.3    Silvestri, L.4    Gourbeyre, O.5
  • 69
    • 85014911721 scopus 로고    scopus 로고
    • Angiocrine Bmp2 signaling in murine liver controls normal iron homeostasis
    • Koch, P. S., Olsavszky, V., Ulbrich, F., Sticht, C., Demory, A., et al. (2017) Angiocrine Bmp2 signaling in murine liver controls normal iron homeostasis. Blood 129, 415–419.
    • (2017) Blood , vol.129 , pp. 415-419
    • Koch, P.S.1    Olsavszky, V.2    Ulbrich, F.3    Sticht, C.4    Demory, A.5
  • 71
    • 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., and Subramaniam, V. N. (2007) Targeted disruption of the hepatic transferrin receptor 2 gene in mice leads to iron overload. Gastroenterology 132, 301–310.
    • (2007) Gastroenterology , vol.132 , pp. 301-310
    • Wallace, D.F.1    Summerville, L.2    Subramaniam, V.N.3
  • 72
    • 80055055193 scopus 로고    scopus 로고
    • Conditional disruption of mouse Hfe2 gene: maintenance of systemic iron homeostasis requires hepatic but not skeletal muscle hemojuvelin
    • Gkouvatsos, K., Wagner, J., Papanikolaou, G., Sebastiani, G., and Pantopoulos, K. (2011) Conditional disruption of mouse Hfe2 gene: maintenance of systemic iron homeostasis requires hepatic but not skeletal muscle hemojuvelin. Hepatology 54, 1800–1807.
    • (2011) Hepatology , vol.54 , pp. 1800-1807
    • Gkouvatsos, K.1    Wagner, J.2    Papanikolaou, G.3    Sebastiani, G.4    Pantopoulos, K.5
  • 74
    • 84907321174 scopus 로고    scopus 로고
    • HFE interacts with the BMP type I receptor ALK3 to regulate hepcidin expression
    • Wu, X. G., Wang, Y., Wu, Q., Cheng, W. H., Liu, W., et al. (2014) HFE interacts with the BMP type I receptor ALK3 to regulate hepcidin expression. Blood 124, 1335–1343.
    • (2014) Blood , vol.124 , pp. 1335-1343
    • Wu, X.G.1    Wang, Y.2    Wu, Q.3    Cheng, W.H.4    Liu, W.5
  • 75
    • 9344224529 scopus 로고    scopus 로고
    • A novel MHC class I-like gene is mutated in patients with hereditary haemochromatosis
    • Feder, J. N., Gnirke, A., Thomas, W., Tsuchihashi, Z., Ruddy, D. A., et al. (1996) A novel MHC class I-like gene is mutated in patients with hereditary haemochromatosis. Nat. Genet. 13, 399–408.
    • (1996) Nat. Genet. , vol.13 , pp. 399-408
    • Feder, J.N.1    Gnirke, A.2    Thomas, W.3    Tsuchihashi, Z.4    Ruddy, D.A.5
  • 76
    • 13144282684 scopus 로고    scopus 로고
    • The hemochromatosis gene product complexes with the transferrin receptor and lowers its affinity for ligand binding
    • Feder, J. N., Penny, D. M., Irrinki, A., Lee, V. K., Lebron, J. A., et al. (1998) The hemochromatosis gene product complexes with the transferrin receptor and lowers its affinity for ligand binding. Proc. Natl. Acad. Sci. USA 95, 1472–1477.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 1472-1477
    • Feder, J.N.1    Penny, D.M.2    Irrinki, A.3    Lee, V.K.4    Lebron, J.A.5
  • 77
    • 0032478524 scopus 로고    scopus 로고
    • Crystal structure of the hemochromatosis protein HFE and characterization of its interaction with transferrin receptor
    • Lebrón, J. A., Bennet, M. J., Vaughn, D. E., Chirino, A. J., Snow, P. M., et al. (1998) Crystal structure of the hemochromatosis protein HFE and characterization of its interaction with transferrin receptor. Cell 93, 111–123.
    • (1998) Cell , vol.93 , pp. 111-123
    • Lebrón, J.A.1    Bennet, M.J.2    Vaughn, D.E.3    Chirino, A.J.4    Snow, P.M.5
  • 78
    • 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., and Andrews, N. C. (2008) The transferrin receptor modulates hfe-dependent regulation of hepcidin expression. Cell Metab. 7, 205–214.
    • (2008) Cell Metab. , vol.7 , pp. 205-214
    • Schmidt, P.J.1    Toran, P.T.2    Giannetti, A.M.3    Bjorkman, P.J.4    Andrews, N.C.5
  • 79
    • 10244255021 scopus 로고    scopus 로고
    • Regulation of transferrin receptor 2 protein levels by transferrin
    • Robb, A., and Wessling-Resnick, M. (2004) Regulation of transferrin receptor 2 protein levels by transferrin. Blood 104, 4294–4299.
    • (2004) Blood , vol.104 , pp. 4294-4299
    • Robb, A.1    Wessling-Resnick, M.2
  • 80
    • 10244265904 scopus 로고    scopus 로고
    • Diferric transferrin regulates transferrin receptor 2 protein stability
    • Johnson, M. B., and Enns, C. A. (2004) Diferric transferrin regulates transferrin receptor 2 protein stability. Blood 104, 4287–4293.
    • (2004) Blood , vol.104 , pp. 4287-4293
    • Johnson, M.B.1    Enns, C.A.2
  • 81
    • 60649103774 scopus 로고    scopus 로고
    • Interaction of the hereditary hemochromatosis protein HFE with transferrin receptor 2 is required for transferrin-induced hepcidin expression
    • Gao, J., Chen, J., Kramer, M., Tsukamoto, H., Zhang, A. S., and Enns, C. A., et al. (2009) Interaction of the hereditary hemochromatosis protein HFE with transferrin receptor 2 is required for transferrin-induced hepcidin expression. Cell Metab. 9, 217–227.
    • (2009) Cell Metab. , vol.9 , pp. 217-227
    • Gao, J.1    Chen, J.2    Kramer, M.3    Tsukamoto, H.4    Zhang, A.S.5    Enns, C.A.6
  • 82
    • 84885400359 scopus 로고    scopus 로고
    • In situ proximity ligation assays indicate that hemochromatosis proteins Hfe and transferrin receptor 2 (Tfr2) do not interact
    • Rishi, G., Crampton, E. M., Wallace, D. F., and Subramaniam, V. N. (2013) In situ proximity ligation assays indicate that hemochromatosis proteins Hfe and transferrin receptor 2 (Tfr2) do not interact. PLoS One 8, e77267.
    • (2013) PLoS One , vol.8
    • Rishi, G.1    Crampton, E.M.2    Wallace, D.F.3    Subramaniam, V.N.4
  • 83
    • 84861344055 scopus 로고    scopus 로고
    • Transgenic HFE-dependent induction of hepcidin in mice does not require transferrin receptor-2
    • Jun
    • Schmidt, P. J., and Fleming, M. D. (2012) Transgenic HFE-dependent induction of hepcidin in mice does not require transferrin receptor-2. Am. J. Hematol. 87, 588–595. Jun
    • (2012) Am. J. Hematol. , vol.87 , pp. 588-595
    • Schmidt, P.J.1    Fleming, M.D.2
  • 84
    • 14944345916 scopus 로고    scopus 로고
    • Juvenile hemochromatosis associated with pathogenic mutations of adult hemochromatosis genes
    • Feb
    • Pietrangelo, A., Caleffi, A., Henrion, J., Ferrara, F., Corradini, E., et al. (2005) Juvenile hemochromatosis associated with pathogenic mutations of adult hemochromatosis genes. Gastroenterology 128, 470–479. Feb
    • (2005) Gastroenterology , vol.128 , pp. 470-479
    • Pietrangelo, A.1    Caleffi, A.2    Henrion, J.3    Ferrara, F.4    Corradini, E.5
  • 85
    • 73149083742 scopus 로고    scopus 로고
    • Combined deletion of Hfe and transferrin receptor 2 in mice leads to marked dysregulation of hepcidin and iron overload
    • Wallace, D. F., Summerville, L., Crampton, E. M., Frazer, D. M., Anderson, G. J., and Subramaniam, V. N., et al. (2009) Combined deletion of Hfe and transferrin receptor 2 in mice leads to marked dysregulation of hepcidin and iron overload. Hepatology 50, 1992–2000.
    • (2009) Hepatology , vol.50 , pp. 1992-2000
    • Wallace, D.F.1    Summerville, L.2    Crampton, E.M.3    Frazer, D.M.4    Anderson, G.J.5    Subramaniam, V.N.6
  • 86
    • 79953757053 scopus 로고    scopus 로고
    • Evidence for distinct pathways of hepcidin regulation by acute and chronic iron loading in mice
    • Apr
    • Ramos, E., Kautz, L., Rodriguez, R., Hansen, M., Gabayan, V., et al. (2011) Evidence for distinct pathways of hepcidin regulation by acute and chronic iron loading in mice. Hepatology 53, 1333–1341. Apr
    • (2011) Hepatology , vol.53 , pp. 1333-1341
    • Ramos, E.1    Kautz, L.2    Rodriguez, R.3    Hansen, M.4    Gabayan, V.5
  • 87
    • 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., et al. (2011) Serum and liver iron differently regulate the bone morphogenetic protein 6 (BMP6)-SMAD signaling pathway in mice. Hepatology 54, 273–284.
    • (2011) Hepatology , vol.54 , pp. 273-284
    • Corradini, E.1    Meynard, D.2    Wu, Q.3    Chen, S.4    Ventura, P.5
  • 88
    • 66749183353 scopus 로고    scopus 로고
    • Cross-talk between the mitogen activated protein kinase and bone morphogenetic protein/hemojuvelin pathways is required for the induction of hepcidin by holotransferrin in primary mouse hepatocytes
    • Ramey, G., Deschemin, J. C., and Vaulont, S. (2009) Cross-talk between the mitogen activated protein kinase and bone morphogenetic protein/hemojuvelin pathways is required for the induction of hepcidin by holotransferrin in primary mouse hepatocytes. Haematologica 94, 765–772.
    • (2009) Haematologica , vol.94 , pp. 765-772
    • Ramey, G.1    Deschemin, J.C.2    Vaulont, S.3
  • 89
    • 33846212344 scopus 로고    scopus 로고
    • STAT3 is required for IL-6-gp130-dependent activation of hepcidin in vivo
    • Jan
    • Pietrangelo, A., Dierssen, U., Valli, L., Garuti, C., Rump, A., et al. (2007) STAT3 is required for IL-6-gp130-dependent activation of hepcidin in vivo. Gastroenterology 132, 294–300. Jan
    • (2007) Gastroenterology , vol.132 , pp. 294-300
    • Pietrangelo, A.1    Dierssen, U.2    Valli, L.3    Garuti, C.4    Rump, A.5
  • 91
    • 33751175421 scopus 로고    scopus 로고
    • Interleukin-6 induces hepcidin expression through STAT3
    • Wrighting, D. M., and Andrews, N. C. (2006) Interleukin-6 induces hepcidin expression through STAT3. Blood 108, 3204–3209.
    • (2006) Blood , vol.108 , pp. 3204-3209
    • Wrighting, D.M.1    Andrews, N.C.2
  • 92
    • 84940525503 scopus 로고    scopus 로고
    • Regulation of iron metabolism by hepcidin under conditions of inflammation
    • Schmidt, P. J. (2015) Regulation of iron metabolism by hepcidin under conditions of inflammation. J. Biol. Chem. 290, 18975–18983.
    • (2015) J. Biol. Chem. , vol.290 , pp. 18975-18983
    • Schmidt, P.J.1
  • 93
    • 84902105343 scopus 로고    scopus 로고
    • The type I BMP receptor Alk3 is required for the induction of hepatic hepcidin gene expression by interleukin-6
    • Mayeur, C., Lohmeyer, L. K., Leyton, P., Kao, S. M., Pappas, A. E., et al. (2014) The type I BMP receptor Alk3 is required for the induction of hepatic hepcidin gene expression by interleukin-6. Blood 123, 2261–2268.
    • (2014) Blood , vol.123 , pp. 2261-2268
    • Mayeur, C.1    Lohmeyer, L.K.2    Leyton, P.3    Kao, S.M.4    Pappas, A.E.5
  • 94
    • 84864053080 scopus 로고    scopus 로고
    • Induction of activin B by inflammatory stimuli up-regulates expression of the iron-regulatory peptide hepcidin through Smad1/5/8 signaling
    • Besson-Fournier, C., Latour, C., Kautz, L., Bertrand, J., Ganz, T., et al. (2012) Induction of activin B by inflammatory stimuli up-regulates expression of the iron-regulatory peptide hepcidin through Smad1/5/8 signaling. Blood 12;120, 431–439.
    • (2012) Blood , vol.12 , Issue.120 , pp. 431-439
    • Besson-Fournier, C.1    Latour, C.2    Kautz, L.3    Bertrand, J.4    Ganz, T.5
  • 96
    • 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., et al. (2016) 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, 1146–1162.
    • (2016) Endocrinology , vol.157 , pp. 1146-1162
    • Canali, S.1    Core, A.B.2    Zumbrennen-Bullough, K.B.3    Merkulova, M.4    Wang, C.Y.5
  • 97
    • 85014936657 scopus 로고    scopus 로고
    • Hepcidin upregulation by inflammation is independent of Smad1/5/8 signaling by activin B
    • Besson-Fournier, C., Gineste, A., Latour, C., Gourbeyre, O., Meynard, D., et al. (2017) Hepcidin upregulation by inflammation is independent of Smad1/5/8 signaling by activin B. Blood 129, 533–536.
    • (2017) Blood , vol.129 , pp. 533-536
    • Besson-Fournier, C.1    Gineste, A.2    Latour, C.3    Gourbeyre, O.4    Meynard, D.5
  • 98
    • 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., and Cherayil, B. J. (2015) 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, 30637–30647.
    • (2015) J. Biol. Chem. , vol.290 , pp. 30637-30647
    • Shanmugam, N.K.1    Chen, K.2    Cherayil, B.J.3
  • 99
    • 84974534303 scopus 로고    scopus 로고
    • Hepcidin in the diagnosis of iron disorders
    • Girelli, D., Nemeth, E., and Swinkels, D. W. (2016) Hepcidin in the diagnosis of iron disorders. Blood 127, 2809–2813.
    • (2016) Blood , vol.127 , pp. 2809-2813
    • Girelli, D.1    Nemeth, E.2    Swinkels, D.W.3
  • 100
    • 77949707023 scopus 로고    scopus 로고
    • Erythropoietin administration in humans causes a marked and prolonged reduction in circulating hepcidin
    • Ashby, D. R., Gale, D. P., Busbridge, M., Murphy, K. G., Duncan, N. D., et al. (2010) Erythropoietin administration in humans causes a marked and prolonged reduction in circulating hepcidin. Haematologica 95, 505–508.
    • (2010) Haematologica , vol.95 , pp. 505-508
    • Ashby, D.R.1    Gale, D.P.2    Busbridge, M.3    Murphy, K.G.4    Duncan, N.D.5
  • 101
    • 0036791486 scopus 로고    scopus 로고
    • The gene encoding the iron regulatory peptide hepcidin is regulated by anemia, hypoxia, and inflammation
    • Nicolas, G., Chauvet, C., Viatte, L., Danan, J. L., Bigard, X., et al. (2002) The gene encoding the iron regulatory peptide hepcidin is regulated by anemia, hypoxia, and inflammation. J. Clin. Invest. 110, 1037–1044.
    • (2002) J. Clin. Invest. , vol.110 , pp. 1037-1044
    • Nicolas, G.1    Chauvet, C.2    Viatte, L.3    Danan, J.L.4    Bigard, X.5
  • 103
    • 33745755350 scopus 로고    scopus 로고
    • The effects of erythropoetic activity and iron burden on hepcidin expression in patients with thalassemia major
    • Kattamis, A., Papassotiriou, I., Palaiologou, D., Apostolakou, F., Galani, A., et al. (2006) The effects of erythropoetic activity and iron burden on hepcidin expression in patients with thalassemia major. Haematologica 91, 809–812.
    • (2006) Haematologica , vol.91 , pp. 809-812
    • Kattamis, A.1    Papassotiriou, I.2    Palaiologou, D.3    Apostolakou, F.4    Galani, A.5
  • 104
    • 33845245942 scopus 로고    scopus 로고
    • Suppression of hepcidin during anemia requires erythropoietic activity
    • Pak, M., Lopez, M. A., Gabayan, V., Ganz, T., and Rivera, S. (2006) Suppression of hepcidin during anemia requires erythropoietic activity. Blood 108, 3730–3735.
    • (2006) Blood , vol.108 , pp. 3730-3735
    • Pak, M.1    Lopez, M.A.2    Gabayan, V.3    Ganz, T.4    Rivera, S.5
  • 105
    • 33745742487 scopus 로고    scopus 로고
    • Hepcidin mRNA levels in mouse liver respond to inhibition of erythropoiesis
    • Vokurka, M., Krijt, J., Sulc, K., and Necas, E. (2006) Hepcidin mRNA levels in mouse liver respond to inhibition of erythropoiesis. Physiol. Res. 55, 667–674.
    • (2006) Physiol. Res. , vol.55 , pp. 667-674
    • Vokurka, M.1    Krijt, J.2    Sulc, K.3    Necas, E.4
  • 106
    • 34948904750 scopus 로고    scopus 로고
    • High levels of GDF15 in thalassemia suppress expression of the iron regulatory protein hepcidin
    • Sep
    • Tanno, T., Bhanu, N. V., Oneal, P. A., Goh, S. H., Staker, P., et al. (2007) High levels of GDF15 in thalassemia suppress expression of the iron regulatory protein hepcidin. Nat. Med. 13, 1096–1101. Sep
    • (2007) Nat. Med. , vol.13 , pp. 1096-1101
    • Tanno, T.1    Bhanu, N.V.2    Oneal, P.A.3    Goh, S.H.4    Staker, P.5
  • 107
    • 80052430244 scopus 로고    scopus 로고
    • Growth differentiation factor 15 in patients with congenital dyserythropoietic anaemia (CDA) type II
    • Casanovas, G., Swinkels, D. W., Altamura, S., Schwarz, K., Laarakkers, C. M., et al. (2011) Growth differentiation factor 15 in patients with congenital dyserythropoietic anaemia (CDA) type II. J. Mol. Med. (Berl.) 89, 811–816.
    • (2011) J. Mol. Med. (Berl.) , vol.89 , pp. 811-816
    • Casanovas, G.1    Swinkels, D.W.2    Altamura, S.3    Schwarz, K.4    Laarakkers, C.M.5
  • 108
    • 58149399349 scopus 로고    scopus 로고
    • Elevated growth differentiation factor 15 expression in patients with congenital dyserythropoietic anemia type I
    • Tamary, H., Shalev, H., Perez-Avraham, G., Zoldan, M., Levi, I., et al. (2008) Elevated growth differentiation factor 15 expression in patients with congenital dyserythropoietic anemia type I. Blood 112, 5241–5244.
    • (2008) Blood , vol.112 , pp. 5241-5244
    • Tamary, H.1    Shalev, H.2    Perez-Avraham, G.3    Zoldan, M.4    Levi, I.5
  • 109
    • 67651043722 scopus 로고    scopus 로고
    • Identification of TWSG1 as a second novel erythroid regulator of hepcidin expression in murine and human cells
    • Tanno, T., Porayette, P., Sripichai, O., Noh, S. J., Byrnes, C., et al. (2009) Identification of TWSG1 as a second novel erythroid regulator of hepcidin expression in murine and human cells. Blood 114, 181–186.
    • (2009) Blood , vol.114 , pp. 181-186
    • Tanno, T.1    Porayette, P.2    Sripichai, O.3    Noh, S.J.4    Byrnes, C.5
  • 110
    • 84871223663 scopus 로고    scopus 로고
    • The murine growth differentiation factor 15 is not essential for systemic iron homeostasis in phlebotomized mice
    • Casanovas, G., Vujic Spasic, M., Casu, C., Rivella, S., Strelau, J., et al. (2013) The murine growth differentiation factor 15 is not essential for systemic iron homeostasis in phlebotomized mice. Haematologica 98, 444–447.
    • (2013) Haematologica , vol.98 , pp. 444-447
    • Casanovas, G.1    Vujic Spasic, M.2    Casu, C.3    Rivella, S.4    Strelau, J.5
  • 111
    • 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., and Ganz, T. (2014) Identification of erythroferrone as an erythroid regulator of iron metabolism. Nat. Genet. 46, 678–684.
    • (2014) Nat. Genet. , vol.46 , pp. 678-684
    • Kautz, L.1    Jung, G.2    Valore, E.V.3    Rivella, S.4    Nemeth, E.5    Ganz, T.6
  • 112
    • 84969201260 scopus 로고    scopus 로고
    • Limiting hepatic Bmp-Smad signaling by matriptase-2 is required for erythropoietin-mediated hepcidin suppression in mice
    • Nai, A., Rubio, A., Campanella, A., Gourbeyre, O., Artuso, I., et al. (2016) Limiting hepatic Bmp-Smad signaling by matriptase-2 is required for erythropoietin-mediated hepcidin suppression in mice. Blood 127, 2327–2336.
    • (2016) Blood , vol.127 , pp. 2327-2336
    • Nai, A.1    Rubio, A.2    Campanella, A.3    Gourbeyre, O.4    Artuso, I.5
  • 113
    • 84859488137 scopus 로고    scopus 로고
    • Myonectin (CTRP15), a novel myokine that links skeletal muscle to systemic lipid homeostasis
    • Seldin, M. M., Peterson, J. M., Byerly, M. S., Wei, Z., and Wong, G. W. (2012) Myonectin (CTRP15), a novel myokine that links skeletal muscle to systemic lipid homeostasis. J. Biol. Chem. 287, 11968–11980.
    • (2012) J. Biol. Chem. , vol.287 , pp. 11968-11980
    • Seldin, M.M.1    Peterson, J.M.2    Byerly, M.S.3    Wei, Z.4    Wong, G.W.5
  • 114
    • 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., et al. (2015) Erythroferrone contributes to hepcidin suppression and iron overload in a mouse model of beta-thalassemia. Blood 126, 2031–2037.
    • (2015) Blood , vol.126 , pp. 2031-2037
    • Kautz, L.1    Jung, G.2    Du, X.3    Gabayan, V.4    Chapman, J.5
  • 115
    • 85011310533 scopus 로고    scopus 로고
    • Characterization of putative erythroid regulators of hepcidin in mouse models of anemia
    • Mirciov, C. S., Wilkins, S. J., Dunn, L. A., Anderson, G. J., and Frazer, D. M. (2017) Characterization of putative erythroid regulators of hepcidin in mouse models of anemia. PLoS One 12, e0171054.
    • (2017) PLoS One , vol.12
    • Mirciov, C.S.1    Wilkins, S.J.2    Dunn, L.A.3    Anderson, G.J.4    Frazer, D.M.5
  • 116
    • 33947192111 scopus 로고    scopus 로고
    • Erythropoietin and iron-restricted erythropoiesis
    • Goodnough, L. T. (2007) Erythropoietin and iron-restricted erythropoiesis. Exp. Hematol. 35, 167–172.
    • (2007) Exp. Hematol. , vol.35 , pp. 167-172
    • Goodnough, L.T.1
  • 117
    • 0022645743 scopus 로고
    • Hematopoiesis in the rat: quantitation of hematopoietic progenitors and the response to iron deficiency anemia
    • Kimura, H., Finch, C. A., and Adamson, J. W. (1986) Hematopoiesis in the rat: quantitation of hematopoietic progenitors and the response to iron deficiency anemia. J. Cell Physiol. 126, 298–306.
    • (1986) J. Cell Physiol. , vol.126 , pp. 298-306
    • Kimura, H.1    Finch, C.A.2    Adamson, J.W.3
  • 118
    • 34548168278 scopus 로고    scopus 로고
    • Serum transferrin receptor concentration and its ratio to bone marrow erythroblasts in iron deficiency anemia and anemia of chronic diseases
    • Choi, J. W. (2007) Serum transferrin receptor concentration and its ratio to bone marrow erythroblasts in iron deficiency anemia and anemia of chronic diseases. Ann. Clin. Lab. Sci. 37, 288–290.
    • (2007) Ann. Clin. Lab. Sci. , vol.37 , pp. 288-290
    • Choi, J.W.1
  • 119
    • 84888037689 scopus 로고    scopus 로고
    • IRP1 regulates erythropoiesis and systemic iron homeostasis by controlling HIF2alpha mRNA translation
    • Wilkinson, N., and Pantopoulos, K. (2013) IRP1 regulates erythropoiesis and systemic iron homeostasis by controlling HIF2alpha mRNA translation. Blood 122, 1658–1668.
    • (2013) Blood , vol.122 , pp. 1658-1668
    • Wilkinson, N.1    Pantopoulos, K.2
  • 120
    • 84873338684 scopus 로고    scopus 로고
    • Deletion of iron regulatory protein 1 causes polycythemia and pulmonary hypertension in mice through translational derepression of HIF2alpha
    • Ghosh, M. C., Zhang, D. L., Jeong, S. Y., Kovtunovych, G., Ollivierre-Wilson, H., et al. (2013) Deletion of iron regulatory protein 1 causes polycythemia and pulmonary hypertension in mice through translational derepression of HIF2alpha. Cell Metab. 17, 271–281.
    • (2013) Cell Metab. , vol.17 , pp. 271-281
    • Ghosh, M.C.1    Zhang, D.L.2    Jeong, S.Y.3    Kovtunovych, G.4    Ollivierre-Wilson, H.5
  • 121
    • 84873361483 scopus 로고    scopus 로고
    • The IRP1-HIF-2alpha axis coordinates iron and oxygen sensing with erythropoiesis and iron absorption
    • Anderson, S. A., Nizzi, C. P., Chang, Y. I., Deck, K. M., Schmidt, P. J., et al. (2013) The IRP1-HIF-2alpha axis coordinates iron and oxygen sensing with erythropoiesis and iron absorption. Cell Metab. 17, 282–290.
    • (2013) Cell Metab. , vol.17 , pp. 282-290
    • Anderson, S.A.1    Nizzi, C.P.2    Chang, Y.I.3    Deck, K.M.4    Schmidt, P.J.5
  • 122
    • 80052510705 scopus 로고    scopus 로고
    • Chronic IFN-gamma production in mice induces anemia by reducing erythrocyte life span and inhibiting erythropoiesis through an IRF-1/PU.1 axis
    • Libregts, S. F., Gutierrez, L., de Bruin, A. M., Wensveen, F. M., Papadopoulos, P., et al. (2011) Chronic IFN-gamma production in mice induces anemia by reducing erythrocyte life span and inhibiting erythropoiesis through an IRF-1/PU.1 axis. Blood 118, 2578–2588.
    • (2011) Blood , vol.118 , pp. 2578-2588
    • Libregts, S.F.1    Gutierrez, L.2    de Bruin, A.M.3    Wensveen, F.M.4    Papadopoulos, P.5
  • 123
    • 84881239640 scopus 로고    scopus 로고
    • Isocitrate ameliorates anemia by suppressing the erythroid iron restriction response
    • Richardson, C. L., Delehanty, L. L., Bullock, G. C., Rival, C. M., Tung, K. S., et al. (2013) Isocitrate ameliorates anemia by suppressing the erythroid iron restriction response. J. Clin. Invest. 123, 3614–3623.
    • (2013) J. Clin. Invest. , vol.123 , pp. 3614-3623
    • Richardson, C.L.1    Delehanty, L.L.2    Bullock, G.C.3    Rival, C.M.4    Tung, K.S.5
  • 124
    • 77955909228 scopus 로고    scopus 로고
    • Iron control of erythroid development by a novel aconitase-associated regulatory pathway
    • Bullock, G. C., Delehanty, L. L., Talbot, A. L., Gonias, S. L., Tong, W. H., et al. (2010) Iron control of erythroid development by a novel aconitase-associated regulatory pathway. Blood 116, 97–108.
    • (2010) Blood , vol.116 , pp. 97-108
    • Bullock, G.C.1    Delehanty, L.L.2    Talbot, A.L.3    Gonias, S.L.4    Tong, W.H.5
  • 125
    • 84963691751 scopus 로고    scopus 로고
    • Isocitrate treatment of acute anemia of inflammation in a mouse model
    • Jan
    • Kim, A., Fung, E., Parikh, S. G., Gabayan, V., Nemeth, E., and Ganz, T. (2016) Isocitrate treatment of acute anemia of inflammation in a mouse model. Blood Cells Mol. Dis. 56, 31–36. Jan
    • (2016) Blood Cells Mol. Dis. , vol.56 , pp. 31-36
    • Kim, A.1    Fung, E.2    Parikh, S.G.3    Gabayan, V.4    Nemeth, E.5    Ganz, T.6
  • 126
    • 78650037490 scopus 로고    scopus 로고
    • Transferrin receptor 2 is a component of the erythropoietin receptor complex and is required for efficient erythropoiesis
    • Forejtnikova, H., Vieillevoye, M., Zermati, Y., Lambert, M., Pellegrino, R. M., et al. (2010) Transferrin receptor 2 is a component of the erythropoietin receptor complex and is required for efficient erythropoiesis. Blood 116, 5357–5367.
    • (2010) Blood , vol.116 , pp. 5357-5367
    • Forejtnikova, H.1    Vieillevoye, M.2    Zermati, Y.3    Lambert, M.4    Pellegrino, R.M.5
  • 127
    • 84926337889 scopus 로고    scopus 로고
    • Regulation of cell surface transferrin receptor-2 by iron-dependent cleavage and release of a soluble form
    • Pagani, A., Vieillevoye, M., Nai, A., Rausa, M., Ladli, M., et al. (2015) Regulation of cell surface transferrin receptor-2 by iron-dependent cleavage and release of a soluble form. Haematologica 100, 458–465.
    • (2015) Haematologica , vol.100 , pp. 458-465
    • Pagani, A.1    Vieillevoye, M.2    Nai, A.3    Rausa, M.4    Ladli, M.5
  • 128
    • 84978200043 scopus 로고    scopus 로고
    • Hematopoietic deletion of transferrin receptor 2 in mice leads to a block in erythroid differentiation during iron-deficient anemia
    • Rishi, G., Secondes, E. S., Wallace, D. F., and Subramaniam, V. N. (2016) Hematopoietic deletion of transferrin receptor 2 in mice leads to a block in erythroid differentiation during iron-deficient anemia. Am. J. Hematol. 91, 812–818.
    • (2016) Am. J. Hematol. , vol.91 , pp. 812-818
    • Rishi, G.1    Secondes, E.S.2    Wallace, D.F.3    Subramaniam, V.N.4
  • 129
    • 84923293373 scopus 로고    scopus 로고
    • The second transferrin receptor regulates red blood cell production in mice
    • Nai, A., Lidonnici, M. R., Rausa, M., Mandelli, G., Pagani, A., et al. (2015) The second transferrin receptor regulates red blood cell production in mice. Blood 125, 1170–1179.
    • (2015) Blood , vol.125 , pp. 1170-1179
    • Nai, A.1    Lidonnici, M.R.2    Rausa, M.3    Mandelli, G.4    Pagani, A.5
  • 130
    • 84923291109 scopus 로고    scopus 로고
    • TfR2 links iron metabolism and erythropoiesis
    • Pantopoulos, K. (2015) TfR2 links iron metabolism and erythropoiesis. Blood 12, 1055–1056.
    • (2015) Blood , vol.12 , pp. 1055-1056
    • Pantopoulos, K.1


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