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Volumn 17, Issue 2, 2007, Pages 93-100

Iron uptake and metabolism in the new millennium

Author keywords

[No Author keywords available]

Indexed keywords

CD71 ANTIGEN; FERROPORTIN 1; HEME; HEMOJUVELIN; HEPCIDIN; IRON; MELANOTRANSFERRIN; NATURAL RESISTANCE ASSOCIATED MACROPHAGE PROTEIN 2; REGULATOR PROTEIN; TRANSFERRIN; UNCLASSIFIED DRUG;

EID: 33846691564     PISSN: 09628924     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tcb.2006.12.003     Document Type: Review
Times cited : (342)

References (70)
  • 1
    • 2042546096 scopus 로고    scopus 로고
    • Balancing acts: molecular control of mammalian iron metabolism
    • Hentze M.W., et al. Balancing acts: molecular control of mammalian iron metabolism. Cell 117 (2004) 285-297
    • (2004) Cell , vol.117 , pp. 285-297
    • Hentze, M.W.1
  • 2
    • 10744223491 scopus 로고    scopus 로고
    • Genetic ablations of iron regulatory proteins 1 and 2 reveal why iron regulatory protein 2 dominates iron homeostasis
    • Meyron-Holtz E.G., et al. Genetic ablations of iron regulatory proteins 1 and 2 reveal why iron regulatory protein 2 dominates iron homeostasis. EMBO J. 23 (2004) 386-395
    • (2004) EMBO J. , vol.23 , pp. 386-395
    • Meyron-Holtz, E.G.1
  • 3
    • 33645307993 scopus 로고    scopus 로고
    • Complete loss of iron regulatory proteins 1 and 2 prevents viability of murine zygotes beyond the blastocyst stage of embryonic development
    • Smith S.R., et al. Complete loss of iron regulatory proteins 1 and 2 prevents viability of murine zygotes beyond the blastocyst stage of embryonic development. Blood Cells Mol. Dis. 36 (2006) 283-287
    • (2006) Blood Cells Mol. Dis. , vol.36 , pp. 283-287
    • Smith, S.R.1
  • 4
    • 20444416123 scopus 로고    scopus 로고
    • The iron exporter ferroportin/Slc40a1 is essential for iron homeostasis
    • Donovan A., et al. The iron exporter ferroportin/Slc40a1 is essential for iron homeostasis. Cell Metab. 1 (2005) 191-200
    • (2005) Cell Metab. , vol.1 , pp. 191-200
    • Donovan, A.1
  • 5
    • 33745752870 scopus 로고    scopus 로고
    • Targeted disruption of the hepcidin1 gene results in severe hemochromatosis
    • Lesbordes-Brion J.C., et al. Targeted disruption of the hepcidin1 gene results in severe hemochromatosis. Blood 108 (2006) 1402-1405
    • (2006) Blood , vol.108 , pp. 1402-1405
    • Lesbordes-Brion, J.C.1
  • 6
    • 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., et al. Lack of hepcidin gene expression and severe tissue iron overload in upstream stimulatory factor 2 (USF2) knockout mice. Proc. Natl. Acad. Sci. U. S. A. 98 (2001) 8780-8785
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 8780-8785
    • Nicolas, G.1
  • 7
    • 0037007064 scopus 로고    scopus 로고
    • Severe iron deficiency anemia in transgenic mice expressing liver hepcidin
    • Nicolas G., et al. Severe iron deficiency anemia in transgenic mice expressing liver hepcidin. Proc. Natl. Acad. Sci. U. S. A. 99 (2002) 4596-4601
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 4596-4601
    • Nicolas, G.1
  • 8
    • 23644460325 scopus 로고    scopus 로고
    • A mouse model of juvenile hemochromatosis
    • Huang F.W., et al. A mouse model of juvenile hemochromatosis. J. Clin. Invest. 115 (2005) 2187-2191
    • (2005) J. Clin. Invest. , vol.115 , pp. 2187-2191
    • Huang, F.W.1
  • 9
    • 23644444316 scopus 로고    scopus 로고
    • Hemojuvelin is essential for dietary iron sensing, and its mutation leads to severe iron overload
    • Niederkofler V., et al. 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
  • 10
    • 21044434748 scopus 로고    scopus 로고
    • First phenotypic description of transferrin receptor 2 knockout mouse, and the role of hepcidin
    • Wallace D.F., et al. First phenotypic description of transferrin receptor 2 knockout mouse, and the role of hepcidin. Gut 54 (2005) 980-986
    • (2005) Gut , vol.54 , pp. 980-986
    • Wallace, D.F.1
  • 11
    • 0001376313 scopus 로고    scopus 로고
    • HFE gene knockout produces mouse model of hereditary hemochromatosis
    • Zhou X.Y., et al. HFE gene knockout produces mouse model of hereditary hemochromatosis. Proc. Natl. Acad. Sci. U. S. A. 95 (1998) 2492-2497
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 2492-2497
    • Zhou, X.Y.1
  • 12
    • 0037214319 scopus 로고    scopus 로고
    • Iron status in mice carrying a targeted disruption of lactoferrin
    • Ward P.P., et al. Iron status in mice carrying a targeted disruption of lactoferrin. Mol. Cell. Biol. 23 (2003) 178-185
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 178-185
    • Ward, P.P.1
  • 13
    • 33645528381 scopus 로고    scopus 로고
    • Role of melanotransferrin in iron metabolism: studies using targeted gene disruption in vivo
    • Sekyere E.O., et al. Role of melanotransferrin in iron metabolism: studies using targeted gene disruption in vivo. Blood 107 (2006) 2599-2601
    • (2006) Blood , vol.107 , pp. 2599-2601
    • Sekyere, E.O.1
  • 14
    • 33750429650 scopus 로고    scopus 로고
    • The function of melanotransferrin: a role in melanoma cell proliferation and tumorigenesis
    • Dunn L.L., et al. The function of melanotransferrin: a role in melanoma cell proliferation and tumorigenesis. Carcinogenesis 7 (2006) 2157-2169
    • (2006) Carcinogenesis , vol.7 , pp. 2157-2169
    • Dunn, L.L.1
  • 15
    • 13444252281 scopus 로고    scopus 로고
    • Iron release from macrophages after erythrophagocytosis is up-regulated by ferroportin 1 overexpression and down-regulated by hepcidin
    • Knutson M.D., et al. Iron release from macrophages after erythrophagocytosis is up-regulated by ferroportin 1 overexpression and down-regulated by hepcidin. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 1324-1328
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 1324-1328
    • Knutson, M.D.1
  • 16
    • 27144507493 scopus 로고    scopus 로고
    • Cybrd1 (duodenal Cytochrome b) is not necessary for dietary iron absorption in mice
    • Gunshin H., et al. Cybrd1 (duodenal Cytochrome b) is not necessary for dietary iron absorption in mice. Blood 106 (2005) 2879-2883
    • (2005) Blood , vol.106 , pp. 2879-2883
    • Gunshin, H.1
  • 17
    • 0030763856 scopus 로고    scopus 로고
    • Microcytic anaemia mice have a mutation in Nramp2, a candidate iron transporter gene
    • Fleming M.D., et al. Microcytic anaemia mice have a mutation in Nramp2, a candidate iron transporter gene. Nat. Genet. 16 (1997) 383-386
    • (1997) Nat. Genet. , vol.16 , pp. 383-386
    • Fleming, M.D.1
  • 18
    • 18244399587 scopus 로고    scopus 로고
    • Slc11a2 is required for intestinal iron absorption and erythropoiesis but dispensable in placenta and liver
    • Gunshin H., et al. 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
  • 19
    • 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., et al. Nramp2 is mutated in the anemic Belgrade (b) rat: evidence of a role for Nramp2 in endosomal iron transport. Proc. Natl. Acad. Sci. U. S. A. 95 (1998) 1148-1153
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 1148-1153
    • Fleming, M.D.1
  • 20
    • 24144459870 scopus 로고    scopus 로고
    • Identification of an intestinal heme transporter
    • Shayeghi M., et al. Identification of an intestinal heme transporter. Cell 122 (2005) 789-801
    • (2005) Cell , vol.122 , pp. 789-801
    • Shayeghi, M.1
  • 21
    • 0029865751 scopus 로고    scopus 로고
    • Distribution of iron in reticulocytes after inhibition of heme synthesis with succinylacetone: examination of the intermediates involved in iron metabolism
    • Richardson D.R., et al. Distribution of iron in reticulocytes after inhibition of heme synthesis with succinylacetone: examination of the intermediates involved in iron metabolism. Blood 87 (1996) 3477-3488
    • (1996) Blood , vol.87 , pp. 3477-3488
    • Richardson, D.R.1
  • 22
    • 2342508341 scopus 로고    scopus 로고
    • Hephaestin is a ferroxidase that maintains partial activity in sex-linked anemia mice
    • Chen H., et al. Hephaestin is a ferroxidase that maintains partial activity in sex-linked anemia mice. Blood 103 (2004) 3933-3939
    • (2004) Blood , vol.103 , pp. 3933-3939
    • Chen, H.1
  • 23
    • 0032909207 scopus 로고    scopus 로고
    • Hephaestin, a ceruloplasmin homologue implicated in intestinal iron transport, is defective in the sla mouse
    • Vulpe C.D., et al. Hephaestin, a ceruloplasmin homologue implicated in intestinal iron transport, is defective in the sla mouse. Nat. Genet. 21 (1999) 195-199
    • (1999) Nat. Genet. , vol.21 , pp. 195-199
    • Vulpe, C.D.1
  • 24
    • 10844258104 scopus 로고    scopus 로고
    • Hepcidin regulates cellular iron efflux by binding to ferroportin and inducing its internalization
    • Nemeth E., et al. 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
  • 25
    • 27644455133 scopus 로고    scopus 로고
    • Identification of a ferrireductase required for efficient transferrin-dependent iron uptake in erythroid cells
    • Ohgami R.S., et al. Identification of a ferrireductase required for efficient transferrin-dependent iron uptake in erythroid cells. Nat. Genet. 37 (2005) 1264-1269
    • (2005) Nat. Genet. , vol.37 , pp. 1264-1269
    • Ohgami, R.S.1
  • 26
    • 27644526967 scopus 로고    scopus 로고
    • A mutation in Sec15l1 causes anemia in hemoglobin deficit (hbd) mice
    • Lim J.E., et al. A mutation in Sec15l1 causes anemia in hemoglobin deficit (hbd) mice. Nat. Genet. 37 (2005) 1270-1273
    • (2005) Nat. Genet. , vol.37 , pp. 1270-1273
    • Lim, J.E.1
  • 27
    • 28644444443 scopus 로고    scopus 로고
    • Iron metabolism mutant hbd mice have a deletion in Sec15l1, which has homology to a yeast gene for vesicle docking
    • White R.A., et al. Iron metabolism mutant hbd mice have a deletion in Sec15l1, which has homology to a yeast gene for vesicle docking. Genomics 86 (2005) 668-673
    • (2005) Genomics , vol.86 , pp. 668-673
    • White, R.A.1
  • 28
    • 33646104690 scopus 로고    scopus 로고
    • The anemia of "haemoglobin-deficit" (hbd/hbd) mice is caused by a defect in transferrin cycling
    • Zhang A.S., et al. The anemia of "haemoglobin-deficit" (hbd/hbd) mice is caused by a defect in transferrin cycling. Exp. Hematol. 34 (2006) 593-598
    • (2006) Exp. Hematol. , vol.34 , pp. 593-598
    • Zhang, A.S.1
  • 29
    • 33644748145 scopus 로고    scopus 로고
    • Mitoferrin is essential for erythroid iron assimilation
    • Shaw G.C., et al. Mitoferrin is essential for erythroid iron assimilation. Nature 440 (2006) 96-100
    • (2006) Nature , vol.440 , pp. 96-100
    • Shaw, G.C.1
  • 30
    • 12644292903 scopus 로고    scopus 로고
    • Characterization of zebrafish mutants with defects in embryonic hematopoiesis
    • Ransom D.G., et al. Characterization of zebrafish mutants with defects in embryonic hematopoiesis. Development 123 (1996) 311-319
    • (1996) Development , vol.123 , pp. 311-319
    • Ransom, D.G.1
  • 31
    • 33747330134 scopus 로고    scopus 로고
    • Mrs3p, mrs4p, and frataxin provide iron for Fe-S cluster synthesis in mitochondria
    • Zhang Y., et al. Mrs3p, mrs4p, and frataxin provide iron for Fe-S cluster synthesis in mitochondria. J. Biol. Chem. 281 (2006) 22493-22502
    • (2006) J. Biol. Chem. , vol.281 , pp. 22493-22502
    • Zhang, Y.1
  • 32
    • 0037180446 scopus 로고    scopus 로고
    • The breast cancer resistance protein protects against a major chlorophyll-derived dietary phototoxin and protoporphyria
    • Jonker J.W., et al. The breast cancer resistance protein protects against a major chlorophyll-derived dietary phototoxin and protoporphyria. Proc. Natl. Acad. Sci. U. S. A. 99 (2002) 15649-15654
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 15649-15654
    • Jonker, J.W.1
  • 33
    • 0034213588 scopus 로고    scopus 로고
    • ABC-me: a novel mitochondrial transporter induced by GATA-1 during erythroid differentiation
    • Shirihai O.S., et al. ABC-me: a novel mitochondrial transporter induced by GATA-1 during erythroid differentiation. EMBO J. 19 (2000) 2492-2502
    • (2000) EMBO J. , vol.19 , pp. 2492-2502
    • Shirihai, O.S.1
  • 34
    • 4544264523 scopus 로고    scopus 로고
    • Identification of a human heme exporter that is essential for erythropoiesis
    • Quigley J.G., et al. Identification of a human heme exporter that is essential for erythropoiesis. Cell 118 (2004) 757-766
    • (2004) Cell , vol.118 , pp. 757-766
    • Quigley, J.G.1
  • 35
    • 0037093206 scopus 로고    scopus 로고
    • Erythroid differentiation and protoporphyrin IX down-regulate frataxin expression in Friend cells: characterization of frataxin expression compared to molecules involved in iron metabolism and hemoglobinization
    • Becker E.M., et al. Erythroid differentiation and protoporphyrin IX down-regulate frataxin expression in Friend cells: characterization of frataxin expression compared to molecules involved in iron metabolism and hemoglobinization. Blood 99 (2002) 3813-3822
    • (2002) Blood , vol.99 , pp. 3813-3822
    • Becker, E.M.1
  • 36
    • 0034192352 scopus 로고    scopus 로고
    • Inactivation of the Friedreich ataxia mouse gene leads to early embryonic lethality without iron accumulation
    • Cossee M., et al. Inactivation of the Friedreich ataxia mouse gene leads to early embryonic lethality without iron accumulation. Hum. Mol. Genet. 9 (2000) 1219-1226
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 1219-1226
    • Cossee, M.1
  • 37
    • 0035138072 scopus 로고    scopus 로고
    • Mouse models for Friedreich ataxia exhibit cardiomyopathy, sensory nerve defect and Fe-S enzyme deficiency followed by intramitochondrial iron deposits
    • Puccio H., et al. Mouse models for Friedreich ataxia exhibit cardiomyopathy, sensory nerve defect and Fe-S enzyme deficiency followed by intramitochondrial iron deposits. Nat. Genet. 27 (2001) 181-186
    • (2001) Nat. Genet. , vol.27 , pp. 181-186
    • Puccio, H.1
  • 38
    • 0037372442 scopus 로고    scopus 로고
    • Mitochondrial ferritin expression in erythroid cells from patients with sideroblastic anemia
    • Cazzola M., et al. Mitochondrial ferritin expression in erythroid cells from patients with sideroblastic anemia. Blood 101 (2003) 1996-2000
    • (2003) Blood , vol.101 , pp. 1996-2000
    • Cazzola, M.1
  • 39
    • 0034329310 scopus 로고    scopus 로고
    • Human ABC7 transporter: gene structure and mutation causing X-linked sideroblastic anemia with ataxia with disruption of cytosolic iron-sulfur protein maturation
    • Bekri S., et al. Human ABC7 transporter: gene structure and mutation causing X-linked sideroblastic anemia with ataxia with disruption of cytosolic iron-sulfur protein maturation. Blood 96 (2000) 3256-3264
    • (2000) Blood , vol.96 , pp. 3256-3264
    • Bekri, S.1
  • 40
    • 0035896642 scopus 로고    scopus 로고
    • Hepcidin, a urinary antimicrobial peptide synthesized in the liver
    • Park C.H., et al. 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
  • 41
    • 30144432585 scopus 로고    scopus 로고
    • The N-terminus of hepcidin is essential for its interaction with ferroportin: structure-function study
    • Nemeth E., et al. 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
  • 42
    • 0345688910 scopus 로고    scopus 로고
    • Iron loading and erythrophagocytosis increase ferroportin 1 (FPN1) expression in J774 macrophages
    • Knutson M.D., et al. Iron loading and erythrophagocytosis increase ferroportin 1 (FPN1) expression in J774 macrophages. Blood 102 (2003) 4191-4197
    • (2003) Blood , vol.102 , pp. 4191-4197
    • Knutson, M.D.1
  • 43
    • 33745860670 scopus 로고    scopus 로고
    • Regulation of transepithelial transport of iron by hepcidin
    • Mena N.P., et al. Regulation of transepithelial transport of iron by hepcidin. Biol. Res. 39 (2006) 191-193
    • (2006) Biol. Res. , vol.39 , pp. 191-193
    • Mena, N.P.1
  • 44
    • 20444413054 scopus 로고    scopus 로고
    • Deregulation of proteins involved in iron metabolism in hepcidin-deficient mice
    • Viatte L., et al. Deregulation of proteins involved in iron metabolism in hepcidin-deficient mice. Blood 105 (2005) 4861-4864
    • (2005) Blood , vol.105 , pp. 4861-4864
    • Viatte, L.1
  • 45
    • 4143117032 scopus 로고    scopus 로고
    • Molecular analysis of iron overload in beta2-microglobulin-deficient mice
    • Muckenthaler M.U., et al. Molecular analysis of iron overload in beta2-microglobulin-deficient mice. Blood Cells Mol. Dis. 33 (2004) 125-131
    • (2004) Blood Cells Mol. Dis. , vol.33 , pp. 125-131
    • Muckenthaler, M.U.1
  • 46
    • 33646370235 scopus 로고    scopus 로고
    • Bone morphogenetic protein signaling by hemojuvelin regulates hepcidin expression
    • Babitt J.L., et al. Bone morphogenetic protein signaling by hemojuvelin regulates hepcidin expression. Nat. Genet. 38 (2006) 531-539
    • (2006) Nat. Genet. , vol.38 , pp. 531-539
    • Babitt, J.L.1
  • 47
    • 33644876815 scopus 로고    scopus 로고
    • A role of SMAD4 in iron metabolism through the positive regulation of hepcidin expression
    • Wang R.H., et al. A role of SMAD4 in iron metabolism through the positive regulation of hepcidin expression. Cell Metab. 2 (2005) 399-409
    • (2005) Cell Metab. , vol.2 , pp. 399-409
    • Wang, R.H.1
  • 48
    • 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., et al. 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. U. S. A. 103 (2006) 10289-10293
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 10289-10293
    • Truksa, J.1
  • 49
    • 27144459908 scopus 로고    scopus 로고
    • Competitive regulation of hepcidin mRNA by soluble and cell-associated hemojuvelin
    • Lin L., et al. Competitive regulation of hepcidin mRNA by soluble and cell-associated hemojuvelin. Blood 106 (2005) 2884-2889
    • (2005) Blood , vol.106 , pp. 2884-2889
    • Lin, L.1
  • 50
    • 33645509481 scopus 로고    scopus 로고
    • Hepcidin inhibits in vitro erythroid colony formation at reduced erythropoietin concentrations
    • Dallalio G., et al. Hepcidin inhibits in vitro erythroid colony formation at reduced erythropoietin concentrations. Blood 107 (2006) 2702-2704
    • (2006) Blood , vol.107 , pp. 2702-2704
    • Dallalio, G.1
  • 51
    • 33745755350 scopus 로고    scopus 로고
    • The effects of erythropoetic activity and iron burden on hepcidin expression in patients with thalassemia major
    • Kattamis A., et al. The effects of erythropoetic activity and iron burden on hepcidin expression in patients with thalassemia major. Haematologica 91 (2006) 809-812
    • (2006) Haematologica , vol.91 , pp. 809-812
    • Kattamis, A.1
  • 52
    • 33845245942 scopus 로고    scopus 로고
    • Suppression of hepcidin during anemia requires erythropoietic activity
    • Pak M., et al. Suppression of hepcidin during anemia requires erythropoietic activity. Blood 108 (2006) 3730-3735
    • (2006) Blood , vol.108 , pp. 3730-3735
    • Pak, M.1
  • 53
    • 33745742487 scopus 로고    scopus 로고
    • Vokurka, M. et al. (2006) Hepcidin mRNA levels in mouse liver respond to inhibition of erythropoiesis. Physiol. Res. in press (www.biomed.cas.cz)
  • 54
    • 32644437864 scopus 로고    scopus 로고
    • Iron metabolism in the hemoglobin-deficit mouse: correlation of diferric transferrin with hepcidin expression
    • Wilkins S.J., et al. Iron metabolism in the hemoglobin-deficit mouse: correlation of diferric transferrin with hepcidin expression. Blood 107 (2006) 1659-1664
    • (2006) Blood , vol.107 , pp. 1659-1664
    • Wilkins, S.J.1
  • 55
    • 33645314044 scopus 로고    scopus 로고
    • Molecular pathogenesis of anemia of chronic disease
    • Ganz T. Molecular pathogenesis of anemia of chronic disease. Pediatr. Blood Cancer 46 (2006) 554-557
    • (2006) Pediatr. Blood Cancer , vol.46 , pp. 554-557
    • Ganz, T.1
  • 56
    • 33646427702 scopus 로고    scopus 로고
    • TLR4-dependent hepcidin expression by myeloid cells in response to bacterial pathogens
    • Peyssonnaux C., et al. TLR4-dependent hepcidin expression by myeloid cells in response to bacterial pathogens. Blood 107 (2006) 3727-3732
    • (2006) Blood , vol.107 , pp. 3727-3732
    • Peyssonnaux, C.1
  • 57
    • 33845985236 scopus 로고    scopus 로고
    • STAT-3 mediates hepatic hepcidin expression and its inflammatory stimulation
    • Verga Falzacappa M.V., et al. STAT-3 mediates hepatic hepcidin expression and its inflammatory stimulation. Blood 109 (2007) 353-358
    • (2007) Blood , vol.109 , pp. 353-358
    • Verga Falzacappa, M.V.1
  • 58
    • 29244457829 scopus 로고    scopus 로고
    • 24p3 and its receptor: dawn of a new iron age?
    • Richardson D.R. 24p3 and its receptor: dawn of a new iron age?. Cell 123 (2005) 1175-1177
    • (2005) Cell , vol.123 , pp. 1175-1177
    • Richardson, D.R.1
  • 59
    • 32444442757 scopus 로고    scopus 로고
    • Lipocalin 2-deficient mice exhibit increased sensitivity to Escherichia coli infection but not to ischemia-reperfusion injury
    • Berger T., et al. Lipocalin 2-deficient mice exhibit increased sensitivity to Escherichia coli infection but not to ischemia-reperfusion injury. Proc. Natl. Acad. Sci. U. S. A. 103 (2006) 1834-1839
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 1834-1839
    • Berger, T.1
  • 60
    • 29244492306 scopus 로고    scopus 로고
    • A cell-surface receptor for lipocalin 24p3 selectively mediates apoptosis and iron uptake
    • Devireddy L.R., et al. A cell-surface receptor for lipocalin 24p3 selectively mediates apoptosis and iron uptake. Cell 123 (2005) 1293-1305
    • (2005) Cell , vol.123 , pp. 1293-1305
    • Devireddy, L.R.1
  • 61
    • 24744441902 scopus 로고    scopus 로고
    • On mouse and man: neutrophil gelatinase associated lipocalin is not involved in apoptosis or acute response
    • Klausen P., et al. On mouse and man: neutrophil gelatinase associated lipocalin is not involved in apoptosis or acute response. Eur. J. Haematol. 75 (2005) 332-340
    • (2005) Eur. J. Haematol. , vol.75 , pp. 332-340
    • Klausen, P.1
  • 62
    • 0034603062 scopus 로고    scopus 로고
    • Early embryonic lethality of H ferritin gene deletion in mice
    • Ferreira C., et al. Early embryonic lethality of H ferritin gene deletion in mice. J. Biol. Chem. 275 (2000) 3021-3024
    • (2000) J. Biol. Chem. , vol.275 , pp. 3021-3024
    • Ferreira, C.1
  • 63
    • 0011938460 scopus 로고
    • Tissue distribution and clearance kinetics of non-transferrin-bound iron in the hypotransferrinemic mouse: a rodent model for hemochromatosis
    • Craven C.M., et al. Tissue distribution and clearance kinetics of non-transferrin-bound iron in the hypotransferrinemic mouse: a rodent model for hemochromatosis. Proc. Natl. Acad. Sci. U. S. A. 84 (1987) 3457-3461
    • (1987) Proc. Natl. Acad. Sci. U. S. A. , vol.84 , pp. 3457-3461
    • Craven, C.M.1
  • 64
    • 0032959574 scopus 로고    scopus 로고
    • Transferrin receptor is necessary for development of erythrocytes and the nervous system
    • Levy J.E., et al. 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
  • 65
    • 0034054183 scopus 로고    scopus 로고
    • The role of the membrane-bound tumour antigen, melanotransferrin (p97), in iron uptake by the human malignant melanoma cell
    • Richardson D.R. The role of the membrane-bound tumour antigen, melanotransferrin (p97), in iron uptake by the human malignant melanoma cell. Eur. J. Biochem. 267 (2000) 1290-1298
    • (2000) Eur. J. Biochem. , vol.267 , pp. 1290-1298
    • Richardson, D.R.1
  • 66
    • 14544273227 scopus 로고    scopus 로고
    • Examination of the distribution of the transferrin homologue, melanotransferrin (tumour antigen p97), in mouse and human
    • Sekyere E.O., et al. Examination of the distribution of the transferrin homologue, melanotransferrin (tumour antigen p97), in mouse and human. Biochim. Biophys. Acta 1722 (2005) 131-142
    • (2005) Biochim. Biophys. Acta , vol.1722 , pp. 131-142
    • Sekyere, E.O.1
  • 67
    • 1442357038 scopus 로고    scopus 로고
    • Identification of a novel route of iron transcytosis across the mammalian blood-brain barrier
    • Moroo I., et al. Identification of a novel route of iron transcytosis across the mammalian blood-brain barrier. Microcirculation 10 (2003) 457-462
    • (2003) Microcirculation , vol.10 , pp. 457-462
    • Moroo, I.1
  • 68
    • 0042442134 scopus 로고    scopus 로고
    • Regulation of plasminogen activation: a role for melanotransferrin (p97) in cell migration
    • Demeule M., et al. Regulation of plasminogen activation: a role for melanotransferrin (p97) in cell migration. Blood 102 (2003) 1723-1731
    • (2003) Blood , vol.102 , pp. 1723-1731
    • Demeule, M.1
  • 69
    • 24944475751 scopus 로고    scopus 로고
    • Stimulation of cell surface plasminogen activation by membrane-bound melanotransferrin: a key phenomenon for cell invasion
    • Michaud-Levesque J., et al. Stimulation of cell surface plasminogen activation by membrane-bound melanotransferrin: a key phenomenon for cell invasion. Exp. Cell Res. 308 (2005) 479-490
    • (2005) Exp. Cell Res. , vol.308 , pp. 479-490
    • Michaud-Levesque, J.1
  • 70
    • 33847251150 scopus 로고    scopus 로고
    • In vivo inhibition of angiogenesis by a soluble form of melanotransferrin
    • 10.1093/carcin/bgl123 (carcin.oxfordjournals.org)
    • Michaud-Levesque J., et al. In vivo inhibition of angiogenesis by a soluble form of melanotransferrin. Carcinogenesis (2006) 10.1093/carcin/bgl123 (carcin.oxfordjournals.org)
    • (2006) Carcinogenesis
    • Michaud-Levesque, J.1


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