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Volumn 82, Issue , 2008, Pages 141-167

Iron Homeostasis and Erythropoiesis

Author keywords

[No Author keywords available]

Indexed keywords

ANTIMICROBIAL CATIONIC PEPTIDE; HEPCIDIN; IRON;

EID: 39049085307     PISSN: 00702153     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0070-2153(07)00006-3     Document Type: Review
Times cited : (53)

References (148)
  • 1
    • 0034733635 scopus 로고    scopus 로고
    • A novel mammalian iron-regulated protein involved in intracellular iron metabolism
    • Abboud S., and Haile D.J. A novel mammalian iron-regulated protein involved in intracellular iron metabolism. J. Biol. Chem. 275 (2000) 19906-19912
    • (2000) J. Biol. Chem. , vol.275 , pp. 19906-19912
    • Abboud, S.1    Haile, D.J.2
  • 3
    • 0034575478 scopus 로고    scopus 로고
    • Iron metabolism: Iron deficiency and iron overload
    • Andrews N.C. Iron metabolism: Iron deficiency and iron overload. Annu. Rev. Genomics Hum. Genet. 1 (2000) 75-98
    • (2000) Annu. Rev. Genomics Hum. Genet. , vol.1 , pp. 75-98
    • Andrews, N.C.1
  • 5
    • 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., and Lin H.Y. Modulation of bone morphogenetic protein signaling in vivo regulates systemic iron balance. J. Clin. Invest. 117 (2007) 1933-1939
    • (2007) J. Clin. Invest. , vol.117 , 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
  • 6
    • 0034610781 scopus 로고    scopus 로고
    • Crystal structure of the hereditary haemochromatosis protein HFE complexed with transferrin receptor
    • Bennett M.J., Lebron J.A., and Bjorkman P.J. Crystal structure of the hereditary haemochromatosis protein HFE complexed with transferrin receptor. Nature 403 (2000) 46-53
    • (2000) Nature , vol.403 , pp. 46-53
    • Bennett, M.J.1    Lebron, J.A.2    Bjorkman, P.J.3
  • 8
    • 33646947821 scopus 로고    scopus 로고
    • Neutrophil gelatinase-associated lipocalin, a siderophore-binding eukaryotic protein
    • Borregaard N., and Cowland J.B. Neutrophil gelatinase-associated lipocalin, a siderophore-binding eukaryotic protein. Biometals 19 (2006) 211-215
    • (2006) Biometals , vol.19 , pp. 211-215
    • Borregaard, N.1    Cowland, J.B.2
  • 16
    • 0035895096 scopus 로고    scopus 로고
    • Characterization of the iron transporter DMT1 (NRAMP2/DCT1) in red blood cells of normal and anemic mk/mk mice
    • Canonne-Hergaux F., Zhang A.S., Ponka P., and Gros P. Characterization of the iron transporter DMT1 (NRAMP2/DCT1) in red blood cells of normal and anemic mk/mk mice. Blood 98 (2001) 3823-3830
    • (2001) Blood , vol.98 , pp. 3823-3830
    • Canonne-Hergaux, F.1    Zhang, A.S.2    Ponka, P.3    Gros, P.4
  • 18
    • 0026646606 scopus 로고
    • Transferrin receptor gene is hyperexpressed and transcriptionally regulated in differentiating erythroid cells
    • Chan L.-N.L., and Gerhardt E.M. Transferrin receptor gene is hyperexpressed and transcriptionally regulated in differentiating erythroid cells. J. Biol. Chem. 267 (1992) 8254-8259
    • (1992) J. Biol. Chem. , vol.267 , pp. 8254-8259
    • Chan, L.-N.L.1    Gerhardt, E.M.2
  • 19
    • 33947095427 scopus 로고    scopus 로고
    • ROS mediate the hypoxic repression of the hepcidin gene by inhibiting C/EBPalpha and STAT-3
    • Choi S.O., Cho Y.S., Kim H.L., and Park J.W. ROS mediate the hypoxic repression of the hepcidin gene by inhibiting C/EBPalpha and STAT-3. Biochem. Biophys. Res. Commun. 356 (2007) 312-317
    • (2007) Biochem. Biophys. Res. Commun. , vol.356 , pp. 312-317
    • Choi, S.O.1    Cho, Y.S.2    Kim, H.L.3    Park, J.W.4
  • 21
    • 0000241799 scopus 로고
    • pH and the recycling of transferrin during receptor-mediated endocytosis
    • Dautry-Varsat A., Ciechanover A., and Lodish H.F. pH and the recycling of transferrin during receptor-mediated endocytosis. Proc. Natl. Acad. Sci. USA 80 (1983) 2258-2262
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 2258-2262
    • Dautry-Varsat, A.1    Ciechanover, A.2    Lodish, H.F.3
  • 24
    • 34250800318 scopus 로고    scopus 로고
    • Ferroxidase activity is required for the stability of cell surface ferroportin in cells expressing GPI-ceruloplasmin
    • De Domenico I., Ward D.M., di Patti M.C., Jeong S.Y., David S., Musci G., and Kaplan J. Ferroxidase activity is required for the stability of cell surface ferroportin in cells expressing GPI-ceruloplasmin. EMBO J. 26 (2007) 2823-2831
    • (2007) EMBO J. , vol.26 , pp. 2823-2831
    • De Domenico, I.1    Ward, D.M.2    di Patti, M.C.3    Jeong, S.Y.4    David, S.5    Musci, G.6    Kaplan, J.7
  • 26
    • 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 A.S., Beaumont C., and 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 (2005) 3979-3984
    • (2005) Blood , vol.106 , pp. 3979-3984
    • Delaby, C.1    Pilard, N.2    Goncalves, A.S.3    Beaumont, C.4    Canonne-Hergaux, F.5
  • 33
    • 0028049495 scopus 로고
    • Regulators of iron balance in humans
    • Finch C. Regulators of iron balance in humans. Blood 84 (1994) 1697-1702
    • (1994) Blood , vol.84 , pp. 1697-1702
    • Finch, C.1
  • 35
    • 34047235103 scopus 로고    scopus 로고
    • In vivo imaging of hepcidin promoter stimulation by iron and inflammation
    • Flanagan J.M., Truksa J., Peng H., Lee P., and Beutler E. In vivo imaging of hepcidin promoter stimulation by iron and inflammation. Blood Cells Mol. Dis. 38 (2007) 253-257
    • (2007) Blood Cells Mol. Dis. , vol.38 , pp. 253-257
    • Flanagan, J.M.1    Truksa, J.2    Peng, H.3    Lee, P.4    Beutler, E.5
  • 37
    • 0032477866 scopus 로고    scopus 로고
    • Nramp2 is mutated in the anemic Belgrade (b) rat: Evidence of a role for Nramp2 in endosomal iron transport
    • Fleming M.D., Romano M.A., Su M.A., Garrick L.M., Garrick M.D., and Andrews N.C. Nramp2 is mutated in the anemic Belgrade (b) rat: Evidence of a role for Nramp2 in endosomal iron transport. Proc. Natl. Acad. Sci. USA 95 (1998) 1148-1153
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 1148-1153
    • Fleming, M.D.1    Romano, M.A.2    Su, M.A.3    Garrick, L.M.4    Garrick, M.D.5    Andrews, N.C.6
  • 38
    • 34249658982 scopus 로고    scopus 로고
    • Ineffective erythropoiesis in {beta}-thalassemia is characterized by increased iron absorption mediated by down-regulation of hepcidin and up-regulation of ferroportin
    • Gardenghi S., Marongiu M.F., Ramos P., Guy E., Breda L., Chadburn A., Liu Y., Amariglio N., Rechavi G., Rachmilewitz E.A., Breur W., Cabantchik Z.I., et al. Ineffective erythropoiesis in {beta}-thalassemia is characterized by increased iron absorption mediated by down-regulation of hepcidin and up-regulation of ferroportin. Blood 109 11 (2007) 5027-5035
    • (2007) Blood , vol.109 , Issue.11 , pp. 5027-5035
    • Gardenghi, S.1    Marongiu, M.F.2    Ramos, P.3    Guy, E.4    Breda, L.5    Chadburn, A.6    Liu, Y.7    Amariglio, N.8    Rechavi, G.9    Rachmilewitz, E.A.10    Breur, W.11    Cabantchik, Z.I.12
  • 39
    • 0025972125 scopus 로고
    • Erythropoietin mRNA levels are governed by both the rate of gene transcription and posttranscriptional events
    • Goldberg M.A., Gaut C.C., and Bunn H.F. Erythropoietin mRNA levels are governed by both the rate of gene transcription and posttranscriptional events. Blood 77 (1991) 271-277
    • (1991) Blood , vol.77 , pp. 271-277
    • Goldberg, M.A.1    Gaut, C.C.2    Bunn, H.F.3
  • 40
    • 33749393565 scopus 로고    scopus 로고
    • Hereditary hemochromatosis protein, HFE, interaction with transferrin receptor 2 suggests a molecular mechanism for mammalian iron sensing
    • Goswami T., and Andrews N.C. Hereditary hemochromatosis protein, HFE, interaction with transferrin receptor 2 suggests a molecular mechanism for mammalian iron sensing. J. Biol. Chem. 281 (2006) 28494-28498
    • (2006) J. Biol. Chem. , vol.281 , pp. 28494-28498
    • Goswami, T.1    Andrews, N.C.2
  • 42
    • 18244399587 scopus 로고    scopus 로고
    • Slc11a2 is required for intestinal iron absorption and erythropoiesis but dispensable in placenta and liver
    • Gunshin H., Fujiwara Y., Custodio A.O., Direnzo C., Robine S., and Andrews N.C. Slc11a2 is required for intestinal iron absorption and erythropoiesis but dispensable in placenta and liver. J. Clin. Invest. 115 (2005) 1258-1266
    • (2005) J. Clin. Invest. , vol.115 , pp. 1258-1266
    • Gunshin, H.1    Fujiwara, Y.2    Custodio, A.O.3    Direnzo, C.4    Robine, S.5    Andrews, N.C.6
  • 44
    • 0019847498 scopus 로고
    • Superoxide-dependent formation of hydroxyl radicals in the presence of iron salts
    • Gutteridge J.M.C., Rowley D.A., and Halliwell B. Superoxide-dependent formation of hydroxyl radicals in the presence of iron salts. Biochem. J. 199 (1981) 263-265
    • (1981) Biochem. J. , vol.199 , pp. 263-265
    • Gutteridge, J.M.C.1    Rowley, D.A.2    Halliwell, B.3
  • 45
    • 0021910539 scopus 로고
    • Low-molecular-weight iron complexes and oxygen radical reactions in idiopathic haemochromatosis
    • Gutteridge J.M.C., Rowley D.A., Griffiths E., and Halliwell B. Low-molecular-weight iron complexes and oxygen radical reactions in idiopathic haemochromatosis. Clin. Sci. 68 (1985) 463-467
    • (1985) Clin. Sci. , vol.68 , pp. 463-467
    • Gutteridge, J.M.C.1    Rowley, D.A.2    Griffiths, E.3    Halliwell, B.4
  • 46
    • 0026355764 scopus 로고
    • Congenital atransferrinemia: A case report and review of the literature
    • Hamill R.L., Woods J.C., and Cook B.A. Congenital atransferrinemia: A case report and review of the literature. Am. J. Clin. Pathol. 96 (1991) 215-218
    • (1991) Am. J. Clin. Pathol. , vol.96 , pp. 215-218
    • Hamill, R.L.1    Woods, J.C.2    Cook, B.A.3
  • 48
    • 0032875387 scopus 로고    scopus 로고
    • Targeted gene disruption reveals an essential role for ceruloplasmin in cellular iron efflux
    • Harris Z.L., Durley A.P., Man T.K., and Gitlin J.D. Targeted gene disruption reveals an essential role for ceruloplasmin in cellular iron efflux. Proc. Natl. Acad. Sci. USA 96 (1999) 10812-10817
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 10812-10817
    • Harris, Z.L.1    Durley, A.P.2    Man, T.K.3    Gitlin, J.D.4
  • 50
    • 0037020241 scopus 로고    scopus 로고
    • The solution structure of human hepcidin, a peptide hormone with antimicrobial activity that is involved in iron uptake and hereditary hemochromatosis
    • Hunter H.N., Fulton D.B., Ganz T., and Vogel H.J. The solution structure of human hepcidin, a peptide hormone with antimicrobial activity that is involved in iron uptake and hereditary hemochromatosis. J. Biol. Chem. 277 (2002) 37597-37603
    • (2002) J. Biol. Chem. , vol.277 , pp. 37597-37603
    • Hunter, H.N.1    Fulton, D.B.2    Ganz, T.3    Vogel, H.J.4
  • 51
    • 30144443274 scopus 로고    scopus 로고
    • Microcytic anemia and hepatic iron overload in a child with compound heterozygous mutations in DMT1 (SCL11A2)
    • Iolascon A., d'Apolito M., Servedio V., Cimmino F., Piga A., and Camaschella C. Microcytic anemia and hepatic iron overload in a child with compound heterozygous mutations in DMT1 (SCL11A2). Blood 107 (2006) 349-354
    • (2006) Blood , vol.107 , pp. 349-354
    • Iolascon, A.1    d'Apolito, M.2    Servedio, V.3    Cimmino, F.4    Piga, A.5    Camaschella, C.6
  • 52
    • 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., and Gros P. Iron transporter Nramp2/DMT-1 is associated with the membrane of phagosomes in macrophages and Sertoli cells. Blood 100 (2002) 2617-2622
    • (2002) Blood , vol.100 , pp. 2617-2622
    • Jabado, N.1    Canonne-Hergaux, F.2    Gruenheid, S.3    Picard, V.4    Gros, P.5
  • 53
    • 34347389655 scopus 로고    scopus 로고
    • Iron homeostasis during transfusional iron overload in beta-thalassemia and sickle cell disease: Changes in iron regulatory protein, hepcidin, and ferritin expression
    • Jenkins Z.A., Hagar W., Bowlus C.L., Johansson H.E., Harmatz P., Vichinsky E.P., and Theil E.C. Iron homeostasis during transfusional iron overload in beta-thalassemia and sickle cell disease: Changes in iron regulatory protein, hepcidin, and ferritin expression. Pediatr. Hematol. Oncol. 24 (2007) 237-243
    • (2007) Pediatr. Hematol. Oncol. , vol.24 , pp. 237-243
    • Jenkins, Z.A.1    Hagar, W.2    Bowlus, C.L.3    Johansson, H.E.4    Harmatz, P.5    Vichinsky, E.P.6    Theil, E.C.7
  • 54
    • 10244265904 scopus 로고    scopus 로고
    • Regulation of transferrin receptor 2 by transferrin: Diferric transferrin regulates transferrin receptor 2 protein stability
    • Johnson M.B., and Enns C.A. Regulation of transferrin receptor 2 by transferrin: Diferric transferrin regulates transferrin receptor 2 protein stability. Blood 104 13 (2004) 4287-4293
    • (2004) Blood , vol.104 , Issue.13 , pp. 4287-4293
    • Johnson, M.B.1    Enns, C.A.2
  • 55
    • 33947111426 scopus 로고    scopus 로고
    • Transferrin receptor 2: Evidence for ligand-induced stabilization and redirection to a recycling pathway
    • Johnson M.B., Chen J., Murchison N., Green F.A., and Enns C.A. Transferrin receptor 2: Evidence for ligand-induced stabilization and redirection to a recycling pathway. Mol. Biol. Cell 18 (2007) 743-754
    • (2007) Mol. Biol. Cell , vol.18 , pp. 743-754
    • Johnson, M.B.1    Chen, J.2    Murchison, N.3    Green, F.A.4    Enns, C.A.5
  • 57
    • 0033597780 scopus 로고    scopus 로고
    • Molecular cloning of transferrin receptor 2. A new member of the transferrin receptor-like family
    • Kawabata H., Yang R., Hirama T., Vuong P.T., Kawano S., Gombart A.F., and Koeffler H.P. Molecular cloning of transferrin receptor 2. A new member of the transferrin receptor-like family. J. Biol. Chem. 274 (1999) 20826-20832
    • (1999) J. Biol. Chem. , vol.274 , pp. 20826-20832
    • Kawabata, H.1    Yang, R.2    Hirama, T.3    Vuong, P.T.4    Kawano, S.5    Gombart, A.F.6    Koeffler, H.P.7
  • 58
    • 0034595856 scopus 로고    scopus 로고
    • Transferrin receptor 2-{alpha} supports cell growth both in iron-chelated cultured cells and in vivo
    • Kawabata H., Germain R.S., Vuong P.T., Nakamaki T., Said J.W., and Koeffler H.P. Transferrin receptor 2-{alpha} supports cell growth both in iron-chelated cultured cells and in vivo. J. Biol. Chem. 275 (2000) 16618-16625
    • (2000) J. Biol. Chem. , vol.275 , pp. 16618-16625
    • Kawabata, H.1    Germain, R.S.2    Vuong, P.T.3    Nakamaki, T.4    Said, J.W.5    Koeffler, H.P.6
  • 60
    • 23944502314 scopus 로고    scopus 로고
    • Time-course analysis of hepcidin, serum iron, and plasma cytokine levels in humans injected with LPS
    • Kemna E., Pickkers P., Nemeth E., van der Hoeven H., and Swinkels D. Time-course analysis of hepcidin, serum iron, and plasma cytokine levels in humans injected with LPS. Blood 106 (2005) 1864-1866
    • (2005) Blood , vol.106 , pp. 1864-1866
    • Kemna, E.1    Pickkers, P.2    Nemeth, E.3    van der Hoeven, H.4    Swinkels, D.5
  • 61
    • 34147197662 scopus 로고    scopus 로고
    • Mass spectrometry-based hepcidin measurements in serum and urine: Analytical aspects and clinical implications
    • Kemna E.H., Tjalsma H., Podust V.N., and Swinkels D.W. Mass spectrometry-based hepcidin measurements in serum and urine: Analytical aspects and clinical implications. Clin. Chem. 53 (2007) 620-628
    • (2007) Clin. Chem. , vol.53 , pp. 620-628
    • Kemna, E.H.1    Tjalsma, H.2    Podust, V.N.3    Swinkels, D.W.4
  • 67
    • 33748797945 scopus 로고    scopus 로고
    • Complex biosynthesis of the muscle-enriched iron regulator RGMc
    • Kuninger D., Kuns-Hashimoto R., Kuzmickas R., and Rotwein P. Complex biosynthesis of the muscle-enriched iron regulator RGMc. J. Cell Sci. 119 (2006) 3273-3283
    • (2006) J. Cell Sci. , vol.119 , pp. 3273-3283
    • Kuninger, D.1    Kuns-Hashimoto, R.2    Kuzmickas, R.3    Rotwein, P.4
  • 68
    • 3042636759 scopus 로고    scopus 로고
    • The IL-6- and lipopolysaccharide-induced transcription of hepcidin in HFE-, transferrin receptor 2-, and beta 2-microglobulin-deficient hepatocytes
    • Lee P., Peng H., Gelbart T., and Beutler E. The IL-6- and lipopolysaccharide-induced transcription of hepcidin in HFE-, transferrin receptor 2-, and beta 2-microglobulin-deficient hepatocytes. Proc. Natl. Acad. Sci. USA 101 (2004) 9263-9265
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 9263-9265
    • Lee, P.1    Peng, H.2    Gelbart, T.3    Beutler, E.4
  • 69
    • 13844307889 scopus 로고    scopus 로고
    • Regulation of hepcidin transcription by interleukin-1 and interleukin-6
    • Lee P., Peng H., Gelbart T., Wang L., and Beutler E. Regulation of hepcidin transcription by interleukin-1 and interleukin-6. Proc. Natl. Acad. Sci. USA 102 (2005) 1906-1910
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 1906-1910
    • Lee, P.1    Peng, H.2    Gelbart, T.3    Wang, L.4    Beutler, E.5
  • 70
    • 0031041377 scopus 로고    scopus 로고
    • Hypoxia-inducible factor-1 mediates transcriptional activation of the heme oxygenase-1 gene in response to hypoxia
    • Lee P.J., Jiang B.H., Chin B.Y., Iyer N.V., Alam J., Semenza G.L., and Choi A.M. Hypoxia-inducible factor-1 mediates transcriptional activation of the heme oxygenase-1 gene in response to hypoxia. J. Biol. Chem. 272 (1997) 5375-5381
    • (1997) J. Biol. Chem. , vol.272 , pp. 5375-5381
    • Lee, P.J.1    Jiang, B.H.2    Chin, B.Y.3    Iyer, N.V.4    Alam, J.5    Semenza, G.L.6    Choi, A.M.7
  • 71
    • 25444435160 scopus 로고    scopus 로고
    • Increased duodenal iron uptake and transfer in a rat model of chronic hypoxia is accompanied by reduced hepcidin expression
    • Leung P.S., Srai S.K., Mascarenhas M., Churchill L.J., and Debnam E.S. Increased duodenal iron uptake and transfer in a rat model of chronic hypoxia is accompanied by reduced hepcidin expression. Gut 54 (2005) 1391-1395
    • (2005) Gut , vol.54 , pp. 1391-1395
    • Leung, P.S.1    Srai, S.K.2    Mascarenhas, M.3    Churchill, L.J.4    Debnam, E.S.5
  • 72
    • 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. Transferrin receptor is necessary for development of erythrocytes and the nervous system. Nat. Genet. 21 (1999) 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
  • 73
    • 27144459908 scopus 로고    scopus 로고
    • Competitive regulation of hepcidin mRNA by soluble and cell-associated hemojuvelin
    • Lin L., Goldberg Y.P., and Ganz T. Competitive regulation of hepcidin mRNA by soluble and cell-associated hemojuvelin. Blood 106 8 (2005) 2884-2889
    • (2005) Blood , vol.106 , Issue.8 , pp. 2884-2889
    • Lin, L.1    Goldberg, Y.P.2    Ganz, T.3
  • 74
    • 34548825938 scopus 로고    scopus 로고
    • Iron-transferrin regulates hepcidin synthesis in primary hepatocyte culture through hemojuvelin and BMP2/4
    • Lin L., Valore E.V., Nemeth E., Goodnough J.B., Gabayan V., and Ganz T. Iron-transferrin regulates hepcidin synthesis in primary hepatocyte culture through hemojuvelin and BMP2/4. Blood 110 6 (2007) 2182-2189
    • (2007) Blood , vol.110 , Issue.6 , pp. 2182-2189
    • Lin, L.1    Valore, E.V.2    Nemeth, E.3    Goodnough, J.B.4    Gabayan, V.5    Ganz, T.6
  • 75
    • 21544442328 scopus 로고    scopus 로고
    • Functional consequences of ferroportin 1 mutations
    • Liu X.B., Yang F., and Haile D.J. Functional consequences of ferroportin 1 mutations. Blood Cells Mol. Dis. 35 (2005) 33-46
    • (2005) Blood Cells Mol. Dis. , vol.35 , pp. 33-46
    • Liu, X.B.1    Yang, F.2    Haile, D.J.3
  • 78
    • 12844260664 scopus 로고    scopus 로고
    • Identification of a human mutation of DMT1 in a patient with microcytic anemia and iron overload
    • Mims M.P., Guan Y., Pospisilova D., Priwitzerova M., Indrak K., Ponka P., Divoky V., and Prchal J.T. Identification of a human mutation of DMT1 in a patient with microcytic anemia and iron overload. Blood 105 3 (2004) 1337-1342
    • (2004) Blood , vol.105 , Issue.3 , pp. 1337-1342
    • Mims, M.P.1    Guan, Y.2    Pospisilova, D.3    Priwitzerova, M.4    Indrak, K.5    Ponka, P.6    Divoky, V.7    Prchal, J.T.8
  • 81
    • 0022032020 scopus 로고
    • Regional specificity of iron uptake by small intestinal brush-border membranes from normal and iron-deficient mice
    • Muir A., and Hopfer U. Regional specificity of iron uptake by small intestinal brush-border membranes from normal and iron-deficient mice. Am. J. Physiol. 248 3Pt1 (1985) G376-G379
    • (1985) Am. J. Physiol. , vol.248 , Issue.3 Pt1
    • Muir, A.1    Hopfer, U.2
  • 82
    • 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., and Ganz T. Hepcidin, a putative mediator of anemia of inflammation, is a type II acute-phase protein. Blood 101 (2003) 2461-2463
    • (2003) Blood , vol.101 , pp. 2461-2463
    • Nemeth, E.1    Valore, E.V.2    Territo, M.3    Schiller, G.4    Lichtenstein, A.5    Ganz, T.6
  • 83
    • 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., and Ganz T. IL-6 mediates hypoferremia of inflammation by inducing the synthesis of the iron regulatory hormone hepcidin. J. Clin. Invest. 113 (2004) 1271-1276
    • (2004) J. Clin. Invest. , vol.113 , pp. 1271-1276
    • Nemeth, E.1    Rivera, S.2    Gabayan, V.3    Keller, C.4    Taudorf, S.5    Pedersen, B.K.6    Ganz, T.7
  • 84
    • 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., and Kaplan J. Hepcidin regulates cellular iron efflux by binding to ferroportin and inducing its internalization. Science 306 (2004) 2090-2093
    • (2004) Science , vol.306 , pp. 2090-2093
    • Nemeth, E.1    Tuttle, M.S.2    Powelson, J.3    Vaughn, M.B.4    Donovan, A.5    Ward, D.M.6    Ganz, T.7    Kaplan, J.8
  • 86
    • 30144432585 scopus 로고    scopus 로고
    • The N-terminus of hepcidin is essential for its interaction with ferroportin: Structure-function study
    • Nemeth E., Preza G.C., Jung C.L., Kaplan J., Waring A.J., and Ganz T. The N-terminus of hepcidin is essential for its interaction with ferroportin: Structure-function study. Blood 107 (2006) 328-333
    • (2006) Blood , vol.107 , pp. 328-333
    • Nemeth, E.1    Preza, G.C.2    Jung, C.L.3    Kaplan, J.4    Waring, A.J.5    Ganz, T.6
  • 87
    • 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., Kahn A., and Vaulont S. Lack of hepcidin gene expression and severe tissue iron overload in upstream stimulatory factor 2 (USF2) knockout mice. Proc. Natl. Acad. Sci. USA 98 (2001) 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    Kahn, A.6    Vaulont, S.7
  • 91
    • 23644444316 scopus 로고    scopus 로고
    • Hemojuvelin is essential for dietary iron sensing, and its mutation leads to severe iron overload
    • Niederkofler V., Salie R., and Arber S. Hemojuvelin is essential for dietary iron sensing, and its mutation leads to severe iron overload. J. Clin. Invest. 115 (2005) 2180-2186
    • (2005) J. Clin. Invest. , vol.115 , pp. 2180-2186
    • Niederkofler, V.1    Salie, R.2    Arber, S.3
  • 92
    • 1642395635 scopus 로고    scopus 로고
    • Expression pattern of the repulsive guidance molecules RGM A, B and C during mouse development
    • Oldekamp J., Kramer N., Alvarez-Bolado G., and Skutella T. Expression pattern of the repulsive guidance molecules RGM A, B and C during mouse development. Gene Expr. Patterns 4 (2004) 283-288
    • (2004) Gene Expr. Patterns , vol.4 , pp. 283-288
    • Oldekamp, J.1    Kramer, N.2    Alvarez-Bolado, G.3    Skutella, T.4
  • 95
    • 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. Hepcidin, a urinary antimicrobial peptide synthesized in the liver. J. Biol. Chem. 276 (2001) 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
  • 98
    • 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., Brissot P., and Loreal O. A new mouse liver-specific gene, encoding a protein homologous to human antimicrobial peptide hepcidin, is overexpressed during iron overload. J. Biol. Chem. 276 (2001) 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    Brissot, P.6    Loreal, O.7
  • 99
    • 0030886381 scopus 로고    scopus 로고
    • Heme oxygenase 1 is required for mammalian iron reutilization
    • Poss K.D., and Tonegawa S. Heme oxygenase 1 is required for mammalian iron reutilization. Proc. Natl. Acad. Sci. USA 94 (1997) 10919-10924
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 10919-10924
    • Poss, K.D.1    Tonegawa, S.2
  • 100
    • 33751244559 scopus 로고    scopus 로고
    • Identification of an intestinal folate transporter and the molecular basis for hereditary folate malabsorption
    • Qiu A., Jansen M., Sakaris A., Min S., Chattopadhyay S., Tsai E., Sandoval C., Zhao R., Akabas M., and Goldman I. Identification of an intestinal folate transporter and the molecular basis for hereditary folate malabsorption. Cell 127 5 (2007) 917-928
    • (2007) Cell , vol.127 , Issue.5 , pp. 917-928
    • Qiu, A.1    Jansen, M.2    Sakaris, A.3    Min, S.4    Chattopadhyay, S.5    Tsai, E.6    Sandoval, C.7    Zhao, R.8    Akabas, M.9    Goldman, I.10
  • 101
    • 0034986262 scopus 로고    scopus 로고
    • Serum soluble transferrin receptor concentration is an accurate estimate of the mass of tissue receptors
    • R'Zik S., and Beguin Y. Serum soluble transferrin receptor concentration is an accurate estimate of the mass of tissue receptors. Exp. Hematol. 29 (2001) 677-685
    • (2001) Exp. Hematol. , vol.29 , pp. 677-685
    • R'Zik, S.1    Beguin, Y.2
  • 102
    • 0023897841 scopus 로고
    • In vivo studies on the relationship between intestinal (Fe3+) absorption, hypoxia and erythropoiesis in the mouse
    • Raja K.B., Simpson R.J., Pippard M.J., and Peters T.J. In vivo studies on the relationship between intestinal (Fe3+) absorption, hypoxia and erythropoiesis in the mouse. Br. J. Haematol. 68 (1988) 373-378
    • (1988) Br. J. Haematol. , vol.68 , pp. 373-378
    • Raja, K.B.1    Simpson, R.J.2    Pippard, M.J.3    Peters, T.J.4
  • 103
    • 13544252463 scopus 로고    scopus 로고
    • Hepcidin excess induces the sequestration of iron and exacerbates tumor-associated anemia
    • Rivera S., Liu L., Nemeth E., Gabayan V., Sorensen O.E., and Ganz T. Hepcidin excess induces the sequestration of iron and exacerbates tumor-associated anemia. Blood 105 (2005) 1797-1802
    • (2005) Blood , vol.105 , pp. 1797-1802
    • Rivera, S.1    Liu, L.2    Nemeth, E.3    Gabayan, V.4    Sorensen, O.E.5    Ganz, T.6
  • 104
    • 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., and Ganz T. Synthetic hepcidin causes rapid dose-dependent hypoferremia and is concentrated in ferroportin-containing organs. Blood 106 (2005) 2196-2199
    • (2005) Blood , vol.106 , pp. 2196-2199
    • Rivera, S.1    Nemeth, E.2    Gabayan, V.3    Lopez, M.A.4    Farshidi, D.5    Ganz, T.6
  • 105
    • 10244255021 scopus 로고    scopus 로고
    • Regulation of transferrin receptor 2 protein levels by transferrin
    • Robb A., and Wessling-Resnick M. Regulation of transferrin receptor 2 protein levels by transferrin. Blood 104 (2004) 4294-4299
    • (2004) Blood , vol.104 , pp. 4294-4299
    • Robb, A.1    Wessling-Resnick, M.2
  • 106
    • 33845946773 scopus 로고    scopus 로고
    • Expression studies of neogenin and its ligand hemojuvelin in mouse tissues
    • Rodriguez A., Pan P., and Parkkila S. Expression studies of neogenin and its ligand hemojuvelin in mouse tissues. J. Histochem. Cytochem. 55 (2007) 85-96
    • (2007) J. Histochem. Cytochem. , vol.55 , pp. 85-96
    • Rodriguez, A.1    Pan, P.2    Parkkila, S.3
  • 108
    • 0030792094 scopus 로고    scopus 로고
    • Oxygen-regulated transferring expression is mediated by hypoxia-inducible factor-1
    • Rolfs A., Kvietikova I., Gassmann M., and Wenger R.H. Oxygen-regulated transferring expression is mediated by hypoxia-inducible factor-1. J. Biol. Chem. 272 (1997) 20055-20062
    • (1997) J. Biol. Chem. , vol.272 , pp. 20055-20062
    • Rolfs, A.1    Kvietikova, I.2    Gassmann, M.3    Wenger, R.H.4
  • 109
    • 0037369165 scopus 로고    scopus 로고
    • 2002 E. Mead Johnson Award for Research in Pediatrics Lecture: The molecular biology of the anemia of chronic disease: A hypothesis
    • Roy C.N., Weinstein D.A., and Andrews N.C. 2002 E. Mead Johnson Award for Research in Pediatrics Lecture: The molecular biology of the anemia of chronic disease: A hypothesis. Pediatr. Res. 53 (2003) 507-512
    • (2003) Pediatr. Res. , vol.53 , pp. 507-512
    • Roy, C.N.1    Weinstein, D.A.2    Andrews, N.C.3
  • 111
    • 34247366783 scopus 로고    scopus 로고
    • Hepcidin antimicrobial peptide transgenic mice exhibit features of the anemia of inflammation
    • Roy C.N., Mak H.H., Akpan I., Losyev G., Zurakowski D., and Andrews N.C. Hepcidin antimicrobial peptide transgenic mice exhibit features of the anemia of inflammation. Blood 109 (2007) 4038-4044
    • (2007) Blood , vol.109 , pp. 4038-4044
    • Roy, C.N.1    Mak, H.H.2    Akpan, I.3    Losyev, G.4    Zurakowski, D.5    Andrews, N.C.6
  • 112
    • 0035744950 scopus 로고    scopus 로고
    • Properties of the mammalian and yeast metal-ion transporters DCT1 and Smf1p expressed in Xenopus laevis oocytes
    • Sacher A., Cohen A., and Nelson N. Properties of the mammalian and yeast metal-ion transporters DCT1 and Smf1p expressed in Xenopus laevis oocytes. J. Exp. Biol. 204 (2001) 1053-1061
    • (2001) J. Exp. Biol. , vol.204 , pp. 1053-1061
    • Sacher, A.1    Cohen, A.2    Nelson, N.3
  • 116
    • 13844270538 scopus 로고    scopus 로고
    • Autosomal dominant hereditary hemochromatosis associated with a novel ferroportin mutation and unique clinical features
    • Sham R.L., Phatak P.D., West C., Lee P., Andrews C., and Beutler E. Autosomal dominant hereditary hemochromatosis associated with a novel ferroportin mutation and unique clinical features. Blood Cells Mol. Dis. 34 (2005) 157-161
    • (2005) Blood Cells Mol. Dis. , vol.34 , pp. 157-161
    • Sham, R.L.1    Phatak, P.D.2    West, C.3    Lee, P.4    Andrews, C.5    Beutler, E.6
  • 119
    • 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. Direct interorganellar transfer of iron from endosome to mitochondrion. Blood 110 (2007) 125-132
    • (2007) Blood , vol.110 , pp. 125-132
    • Sheftel, A.D.1    Zhang, A.S.2    Brown, C.3    Shirihai, O.S.4    Ponka, P.5
  • 121
    • 34248371666 scopus 로고    scopus 로고
    • Defective targeting of hemojuvelin to plasma membrane is a common pathogenetic mechanism in juvenile hemochromatosis
    • Silvestri L., Pagani A., Fazi C., Gerardi G., Levi S., Arosio P., and Camaschella C. Defective targeting of hemojuvelin to plasma membrane is a common pathogenetic mechanism in juvenile hemochromatosis. Blood 109 (2007) 4503-4510
    • (2007) Blood , vol.109 , pp. 4503-4510
    • Silvestri, L.1    Pagani, A.2    Fazi, C.3    Gerardi, G.4    Levi, S.5    Arosio, P.6    Camaschella, C.7
  • 122
    • 0032530922 scopus 로고    scopus 로고
    • The G185R mutation disrupts function of the iron transporter Nramp2
    • Su M.A., Trenor C.C., Fleming J.C., Fleming M.D., and Andrews N.C. The G185R mutation disrupts function of the iron transporter Nramp2. Blood 92 (1998) 2157-2163
    • (1998) Blood , vol.92 , pp. 2157-2163
    • Su, M.A.1    Trenor, C.C.2    Fleming, J.C.3    Fleming, M.D.4    Andrews, N.C.5
  • 123
    • 0037006654 scopus 로고    scopus 로고
    • Role of HFE in iron metabolism, hereditary haemochromatosis, anaemia of chronic disease, and secondary iron overload
    • Townsend A., and Drakesmith H. Role of HFE in iron metabolism, hereditary haemochromatosis, anaemia of chronic disease, and secondary iron overload. Lancet 359 (2002) 786-790
    • (2002) Lancet , vol.359 , pp. 786-790
    • Townsend, A.1    Drakesmith, H.2
  • 125
    • 33745898241 scopus 로고    scopus 로고
    • Bone morphogenetic proteins 2, 4, and 9 stimulate murine hepcidin 1 expression independently of Hfe, transferrin receptor 2 (Tfr2), and IL-6
    • Truksa J., Peng H., Lee P., and Beutler E. Bone morphogenetic proteins 2, 4, and 9 stimulate murine hepcidin 1 expression independently of Hfe, transferrin receptor 2 (Tfr2), and IL-6. Proc. Natl. Acad. Sci. USA 103 (2006) 10289-10293
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 10289-10293
    • Truksa, J.1    Peng, H.2    Lee, P.3    Beutler, E.4
  • 128
  • 131
    • 0035230599 scopus 로고    scopus 로고
    • Stat transcription factors in mammary gland development and tumorigenesis
    • Watson C.J. Stat transcription factors in mammary gland development and tumorigenesis. J. Mammary Gland Biol. Neoplasia 6 (2001) 115-127
    • (2001) J. Mammary Gland Biol. Neoplasia , vol.6 , pp. 115-127
    • Watson, C.J.1
  • 132
    • 0018102319 scopus 로고
    • Iron and infection
    • Weinberg E.D. Iron and infection. Microbiol. Rev. 45 1 (1978) 45-66
    • (1978) Microbiol. Rev. , vol.45 , Issue.1 , pp. 45-66
    • Weinberg, E.D.1
  • 133
    • 0036390056 scopus 로고    scopus 로고
    • Effect of continuous glucose therapy with uncooked cornstarch on the long-term clinical course of type 1a glycogen storage disease
    • Weinstein D.A., and Wolfsdorf J.I. Effect of continuous glucose therapy with uncooked cornstarch on the long-term clinical course of type 1a glycogen storage disease. Eur. J. Pediatr. 161 (2002) S35-S39
    • (2002) Eur. J. Pediatr. , vol.161
    • Weinstein, D.A.1    Wolfsdorf, J.I.2
  • 134
    • 0037111732 scopus 로고    scopus 로고
    • Inappropriate expression of hepcidin is associated with iron refractory anemia: Implications for the anemia of chronic disease
    • Weinstein D.A., Roy C.N., Fleming M.D., Loda M.F., Wolfsdorf J.I., and Andrews N.C. Inappropriate expression of hepcidin is associated with iron refractory anemia: Implications for the anemia of chronic disease. Blood 100 (2002) 3776-3781
    • (2002) Blood , vol.100 , 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
  • 135
    • 14744278436 scopus 로고    scopus 로고
    • Anemia of chronic disease
    • Weiss G., and Goodnough L.T. Anemia of chronic disease. N. Engl. J. Med. 352 (2005) 1011-1023
    • (2005) N. Engl. J. Med. , vol.352 , pp. 1011-1023
    • Weiss, G.1    Goodnough, L.T.2
  • 137
  • 138
    • 0034623930 scopus 로고    scopus 로고
    • Comparison of the interactions of transferrin receptor and transferrin receptor 2 with transferrin and the hereditary hemochromatosis protein HFE
    • West Jr. A.P., Bennett M.J., Sellers V.M., Andrews N.C., Enns C.A., and Bjorkman P.J. Comparison of the interactions of transferrin receptor and transferrin receptor 2 with transferrin and the hereditary hemochromatosis protein HFE. J. Biol. Chem. 275 (2000) 38135-38138
    • (2000) J. Biol. Chem. , vol.275 , pp. 38135-38138
    • West Jr., A.P.1    Bennett, M.J.2    Sellers, V.M.3    Andrews, N.C.4    Enns, C.A.5    Bjorkman, P.J.6
  • 139
    • 0033508544 scopus 로고    scopus 로고
    • Effect of continuous glucose therapy begun in infancy on the long-term clinical course of patients with type I glycogen storage disease
    • Wolfsdorf J.I., and Crigler J.F. Effect of continuous glucose therapy begun in infancy on the long-term clinical course of patients with type I glycogen storage disease. J. Pediatr. Gastroenterol. Nutr. 29 (1999) 136-143
    • (1999) J. Pediatr. Gastroenterol. Nutr. , vol.29 , pp. 136-143
    • Wolfsdorf, J.I.1    Crigler, J.F.2
  • 140
    • 33751175421 scopus 로고    scopus 로고
    • Interleukin-6 induces hepcidin expression through STAT3
    • Wrighting D.M., and Andrews N.C. Interleukin-6 induces hepcidin expression through STAT3. Blood 108 (2006) 3204-3209
    • (2006) Blood , vol.108 , pp. 3204-3209
    • Wrighting, D.M.1    Andrews, N.C.2
  • 141
    • 19344369930 scopus 로고    scopus 로고
    • A spontaneous, recurrent mutation in divalent metal transporter-1 exposes a calcium entry pathway
    • Xu H., Jin J., DeFelice L.J., Andrews N.C., and Clapham D.E. A spontaneous, recurrent mutation in divalent metal transporter-1 exposes a calcium entry pathway. PLoS Biol. 2 (2004) E50
    • (2004) PLoS Biol. , vol.2
    • Xu, H.1    Jin, J.2    DeFelice, L.J.3    Andrews, N.C.4    Clapham, D.E.5
  • 144
    • 26644471267 scopus 로고    scopus 로고
    • Interaction of hemojuvelin with neogenin results in iron accumulation in human embryonic kidney 293 cells
    • Zhang A.S., West Jr. A.P., Wyman A.E., Bjorkman P.J., and Enns C.A. Interaction of hemojuvelin with neogenin results in iron accumulation in human embryonic kidney 293 cells. J. Biol. Chem. 280 (2005) 33885-33894
    • (2005) J. Biol. Chem. , vol.280 , pp. 33885-33894
    • Zhang, A.S.1    West Jr., A.P.2    Wyman, A.E.3    Bjorkman, P.J.4    Enns, C.A.5
  • 145
    • 34250308049 scopus 로고    scopus 로고
    • Evidence that inhibition of hemojuvelin shedding in response to iron is mediated through neogenin
    • Zhang A.S., Anderson S.A., Meyers K.R., Hernandez C., Eisenstein R.S., and Enns C.A. Evidence that inhibition of hemojuvelin shedding in response to iron is mediated through neogenin. J. Biol. Chem. 282 (2007) 12547-12556
    • (2007) J. Biol. Chem. , vol.282 , pp. 12547-12556
    • Zhang, A.S.1    Anderson, S.A.2    Meyers, K.R.3    Hernandez, C.4    Eisenstein, R.S.5    Enns, C.A.6
  • 147
    • 26244467650 scopus 로고    scopus 로고
    • Hemochromatosis: Genetic testing and clinical practice
    • Zoller H., and Cox T.M. Hemochromatosis: Genetic testing and clinical practice. Clin. Gastroenterol. Hepatol. 3 (2005) 945-958
    • (2005) Clin. Gastroenterol. Hepatol. , vol.3 , pp. 945-958
    • Zoller, H.1    Cox, T.M.2


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