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Volumn 81, Issue , 2015, Pages 66-75

Iron misregulation and neurodegenerative disease in mouse models that lack iron regulatory proteins

Author keywords

Amino cupric silver stain; Anemia; Axonal degeneration; Erythropoietic protoporphyria; Iron; Iron regulatory protein; Motor neuron; Neurodegeneration; Polycythemia; Pulmonary hypertension

Indexed keywords

HEPCIDIN; IRON; IRON REGULATORY PROTEIN 1; IRON REGULATORY PROTEIN 2; IRON REGULATORY FACTOR;

EID: 84946873089     PISSN: 09699961     EISSN: 1095953X     Source Type: Journal    
DOI: 10.1016/j.nbd.2015.02.026     Document Type: Review
Times cited : (50)

References (79)
  • 1
    • 0034733635 scopus 로고    scopus 로고
    • A novel mammalian iron-regulated protein involved in intracellular iron metabolism
    • Abboud S., Haile D.J. A novel mammalian iron-regulated protein involved in intracellular iron metabolism. J. Biol. Chem. 2000, 275:19906-19912.
    • (2000) J. Biol. Chem. , vol.275 , pp. 19906-19912
    • Abboud, S.1    Haile, D.J.2
  • 3
    • 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., et al. The IRP1-HIF-2alpha axis coordinates iron and oxygen sensing with erythropoiesis and iron absorption. Cell Metab. 2013, 17(2):282-290.
    • (2013) Cell Metab. , vol.17 , Issue.2 , pp. 282-290
    • Anderson, S.A.1    Nizzi, C.P.2
  • 4
    • 84897954519 scopus 로고    scopus 로고
    • Alzheimer's disease therapeutics targeted to the control of amyloid precursor protein translation: maintenance of brain iron homeostasis
    • Bandyopadhyay S., Rogers J.T. Alzheimer's disease therapeutics targeted to the control of amyloid precursor protein translation: maintenance of brain iron homeostasis. Biochem. Pharmacol. 2014, 88(4):486-494.
    • (2014) Biochem. Pharmacol. , vol.88 , Issue.4 , pp. 486-494
    • Bandyopadhyay, S.1    Rogers, J.T.2
  • 5
    • 84881193458 scopus 로고    scopus 로고
    • Novel 5' untranslated region directed blockers of iron-regulatory protein-1 dependent amyloid precursor protein translation: implications for down syndrome and Alzheimer's disease
    • Bandyopadhyay S., Cahill C., et al. Novel 5' untranslated region directed blockers of iron-regulatory protein-1 dependent amyloid precursor protein translation: implications for down syndrome and Alzheimer's disease. PLoS One 2013, 8(7):e65978.
    • (2013) PLoS One , vol.8 , Issue.7 , pp. e65978
    • Bandyopadhyay, S.1    Cahill, C.2
  • 6
    • 77954534911 scopus 로고    scopus 로고
    • Synergistic accumulation of iron and zinc by cultured astrocytes
    • Bishop G.M., Scheiber I.F., et al. Synergistic accumulation of iron and zinc by cultured astrocytes. J. Neural Transm. 2010, 117:809-817.
    • (2010) J. Neural Transm. , vol.117 , pp. 809-817
    • Bishop, G.M.1    Scheiber, I.F.2
  • 7
    • 0348111398 scopus 로고    scopus 로고
    • The role of endogenous heme synthesis and degradation domain cysteines in cellular iron-dependent degradation of IRP2
    • Bourdon E., et al. The role of endogenous heme synthesis and degradation domain cysteines in cellular iron-dependent degradation of IRP2. Blood Cells Mol. Dis. 2003, 31:247-255.
    • (2003) Blood Cells Mol. Dis. , vol.31 , pp. 247-255
    • Bourdon, E.1
  • 9
    • 77952544962 scopus 로고    scopus 로고
    • Iron regulatory protein-2 knockout increases perihematomal ferritin expression and cell viability after intracerebral hemorrhage
    • Chen M., Awe O.O., et al. Iron regulatory protein-2 knockout increases perihematomal ferritin expression and cell viability after intracerebral hemorrhage. Brain Res. 2010, 1337:95-103.
    • (2010) Brain Res. , vol.1337 , pp. 95-103
    • Chen, M.1    Awe, O.O.2
  • 10
    • 77957771842 scopus 로고    scopus 로고
    • Selective translational control of the Alzheimer amyloid precursor protein transcript by iron regulatory protein-1
    • Cho H.H., Cahill C.M., et al. Selective translational control of the Alzheimer amyloid precursor protein transcript by iron regulatory protein-1. J. Biol. Chem. 2010, 285(41):31217-31232.
    • (2010) J. Biol. Chem. , vol.285 , Issue.41 , pp. 31217-31232
    • Cho, H.H.1    Cahill, C.M.2
  • 11
    • 84869128204 scopus 로고    scopus 로고
    • Duodenal reductase activity and spleen iron stores are reduced and erythropoiesis is abnormal in Dcytb knockout mice exposed to hypoxic conditions
    • Choi J., Masaratana P., et al. Duodenal reductase activity and spleen iron stores are reduced and erythropoiesis is abnormal in Dcytb knockout mice exposed to hypoxic conditions. J. Nutr. 2012, 142:1929-1934.
    • (2012) J. Nutr. , vol.142 , pp. 1929-1934
    • Choi, J.1    Masaratana, P.2
  • 12
    • 4444226451 scopus 로고    scopus 로고
    • Nontransferrin-bound iron uptake by hepatocytes is increased in the Hfe knockout mouse model of hereditary hemochromatosis
    • Chua A.C., Olynyk J.K., et al. Nontransferrin-bound iron uptake by hepatocytes is increased in the Hfe knockout mouse model of hereditary hemochromatosis. Blood 2004, 104(5):1519-1525.
    • (2004) Blood , vol.104 , Issue.5 , pp. 1519-1525
    • Chua, A.C.1    Olynyk, J.K.2
  • 13
    • 23044503950 scopus 로고    scopus 로고
    • Microcytic anemia, erythropoietic protoporphyria, and neurodegeneration in mice with targeted deletion of iron-regulatory protein 2
    • Cooperman S., Meyron-Holtz E.G., et al. Microcytic anemia, erythropoietic protoporphyria, and neurodegeneration in mice with targeted deletion of iron-regulatory protein 2. Blood 2005, 106(3):1084-1091.
    • (2005) Blood , vol.106 , Issue.3 , pp. 1084-1091
    • Cooperman, S.1    Meyron-Holtz, E.G.2
  • 14
    • 0025822118 scopus 로고
    • Identification of a novel iron-responsive element in murine and human erythroid delta-aminolevulinic acid synthase mRNA
    • Dandekar T., Stripecke R., et al. Identification of a novel iron-responsive element in murine and human erythroid delta-aminolevulinic acid synthase mRNA. EMBO J. 1991, 10(7):1903-1909.
    • (1991) EMBO J. , vol.10 , Issue.7 , pp. 1903-1909
    • Dandekar, T.1    Stripecke, R.2
  • 15
    • 0034677467 scopus 로고    scopus 로고
    • Positional cloning of zebrafish ferroportin1 identifies a conserved vertebrate iron exporter
    • Donovan A., Brownlie A., et al. Positional cloning of zebrafish ferroportin1 identifies a conserved vertebrate iron exporter. Nature 2000, 403:776-781.
    • (2000) Nature , vol.403 , pp. 776-781
    • Donovan, A.1    Brownlie, A.2
  • 16
    • 60249084746 scopus 로고    scopus 로고
    • Cell-autonomous and systemic context-dependent functions of iron regulatory protein 2 in mammalian iron metabolism
    • Ferring-Appel D., Hentze M.W., et al. Cell-autonomous and systemic context-dependent functions of iron regulatory protein 2 in mammalian iron metabolism. Blood 2009, 113(3):679-687.
    • (2009) Blood , vol.113 , Issue.3 , pp. 679-687
    • Ferring-Appel, D.1    Hentze, M.W.2
  • 17
    • 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., 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. 1998, 95(3):1148-1153.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , Issue.3 , pp. 1148-1153
    • Fleming, M.D.1    Romano, M.A.2
  • 18
    • 3042577347 scopus 로고    scopus 로고
    • Targeted mutagenesis of the murine IRP1 and IRP2 genes reveals context-dependent RNA processing differences in vivo
    • Galy B., Ferring D., et al. Targeted mutagenesis of the murine IRP1 and IRP2 genes reveals context-dependent RNA processing differences in vivo. RNA 2004, 10(7):1019-1025.
    • (2004) RNA , vol.10 , Issue.7 , pp. 1019-1025
    • Galy, B.1    Ferring, D.2
  • 19
    • 27144467097 scopus 로고    scopus 로고
    • Altered body iron distribution and microcytosis in mice deficient in iron regulatory protein 2 (IRP2)
    • Galy B., Ferring D., et al. Altered body iron distribution and microcytosis in mice deficient in iron regulatory protein 2 (IRP2). Blood 2005, 106(7):2580-2589.
    • (2005) Blood , vol.106 , Issue.7 , pp. 2580-2589
    • Galy, B.1    Ferring, D.2
  • 20
    • 33748297526 scopus 로고    scopus 로고
    • Iron homeostasis in the brain: complete iron regulatory protein 2 deficiency without symptomatic neurodegeneration in the mouse
    • (discussion 969-970)
    • Galy B., Holter S.M., et al. Iron homeostasis in the brain: complete iron regulatory protein 2 deficiency without symptomatic neurodegeneration in the mouse. Nat. Genet. 2006, 38(9):967-969. (discussion 969-970).
    • (2006) Nat. Genet. , vol.38 , Issue.9 , pp. 967-969
    • Galy, B.1    Holter, S.M.2
  • 21
    • 37449009448 scopus 로고    scopus 로고
    • Iron regulatory proteins are essential for intestinal function and control key iron absorption molecules in the duodenum
    • Galy B., Ferring-Appel D., et al. Iron regulatory proteins are essential for intestinal function and control key iron absorption molecules in the duodenum. Cell Metab. 2008, 7(1):79-85.
    • (2008) Cell Metab. , vol.7 , Issue.1 , pp. 79-85
    • Galy, B.1    Ferring-Appel, D.2
  • 22
    • 77954287921 scopus 로고    scopus 로고
    • Iron regulatory proteins secure mitochondrial iron sufficiency and function
    • Galy B., Ferring-Appel D., et al. Iron regulatory proteins secure mitochondrial iron sufficiency and function. Cell Metab. 2010, 12(2):194-201.
    • (2010) Cell Metab. , vol.12 , Issue.2 , pp. 194-201
    • Galy, B.1    Ferring-Appel, D.2
  • 23
    • 84875805891 scopus 로고    scopus 로고
    • Iron regulatory proteins control a mucosal block to intestinal iron absorption
    • Galy B., Ferring-Appel D., et al. Iron regulatory proteins control a mucosal block to intestinal iron absorption. Cell Rep. 2013, 3(3):844-857.
    • (2013) Cell Rep. , vol.3 , Issue.3 , pp. 844-857
    • Galy, B.1    Ferring-Appel, D.2
  • 24
    • 84885768132 scopus 로고    scopus 로고
    • Systemic iron homeostasis
    • Ganz T. Systemic iron homeostasis. Physiol. Rev. 2013, 93(4):1721-1741.
    • (2013) Physiol. Rev. , vol.93 , Issue.4 , pp. 1721-1741
    • Ganz, T.1
  • 25
    • 79551583056 scopus 로고    scopus 로고
    • Hepcidin and disorders of iron metabolism
    • Ganz T., Nemeth E. Hepcidin and disorders of iron metabolism. Annu. Rev. Med. 2011, 62:347-360.
    • (2011) Annu. Rev. Med. , vol.62 , pp. 347-360
    • Ganz, T.1    Nemeth, E.2
  • 26
    • 84861355868 scopus 로고    scopus 로고
    • Hepcidin and iron homeostasis
    • Ganz T., Nemeth E. Hepcidin and iron homeostasis. Biochim. Biophys. Acta 2012, 1823(9):1434-1443.
    • (2012) Biochim. Biophys. Acta , vol.1823 , Issue.9 , pp. 1434-1443
    • Ganz, T.1    Nemeth, E.2
  • 27
    • 0037354265 scopus 로고    scopus 로고
    • DMT1: a mammalian transporter for multiple metals
    • Garrick M.D., Dolan K.G., et al. DMT1: a mammalian transporter for multiple metals. Biometals 2003, 16(1):41-54.
    • (2003) Biometals , vol.16 , Issue.1 , pp. 41-54
    • Garrick, M.D.1    Dolan, K.G.2
  • 28
    • 33748292869 scopus 로고    scopus 로고
    • Reply to "Iron homeostasis in the brain: complete iron regulatory protein 2 deficiency without symptomatic neurodegeneration in the mouse"
    • Ghosh M.C., Ollivierre-Wilson H., Cooperman S., Rouault T.A. Reply to "Iron homeostasis in the brain: complete iron regulatory protein 2 deficiency without symptomatic neurodegeneration in the mouse". Nat. Genet. 2006, 38:969-970.
    • (2006) Nat. Genet. , vol.38 , pp. 969-970
    • Ghosh, M.C.1    Ollivierre-Wilson, H.2    Cooperman, S.3    Rouault, T.A.4
  • 29
    • 50149099153 scopus 로고    scopus 로고
    • Tempol-mediated activation of latent iron regulatory protein activity prevents symptoms of neurodegenerative disease in IRP2 knockout mice
    • Ghosh M.C., Tong W.H., et al. Tempol-mediated activation of latent iron regulatory protein activity prevents symptoms of neurodegenerative disease in IRP2 knockout mice. Proc. Natl. Acad. Sci. U. S. A. 2008, 105(33):12028-12033.
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , Issue.33 , pp. 12028-12033
    • Ghosh, M.C.1    Tong, W.H.2
  • 30
    • 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., et al. Deletion of iron regulatory protein 1 causes polycythemia and pulmonary hypertension in mice through translational derepression of HIF2alpha. Cell Metab. 2013, 17(2):271-281.
    • (2013) Cell Metab. , vol.17 , Issue.2 , pp. 271-281
    • Ghosh, M.C.1    Zhang, D.L.2
  • 31
    • 0347367315 scopus 로고    scopus 로고
    • MRI detection of ferritin iron overload and associated neuronal pathology in iron regulatory protein-2 knockout mice
    • Grabill C., Silva A.C., et al. MRI detection of ferritin iron overload and associated neuronal pathology in iron regulatory protein-2 knockout mice. Brain Res. 2003, 971(1):95-106.
    • (2003) Brain Res. , vol.971 , Issue.1 , pp. 95-106
    • Grabill, C.1    Silva, A.C.2
  • 32
    • 0030755366 scopus 로고    scopus 로고
    • Cloning and characterization of a mammalian proton-coupled metal-ion transporter
    • Gunshin H.B., Mackenzie U., et al. Cloning and characterization of a mammalian proton-coupled metal-ion transporter. Nature 1997, 388:482-488.
    • (1997) Nature , vol.388 , pp. 482-488
    • Gunshin, H.B.1    Mackenzie, U.2
  • 33
    • 52049125740 scopus 로고    scopus 로고
    • The hereditary hemochromatosis protein, HFE, inhibits iron uptake via down-regulation of Zip14 in HepG2 cells
    • Guo J., Zhao N., et al. The hereditary hemochromatosis protein, HFE, inhibits iron uptake via down-regulation of Zip14 in HepG2 cells. J. Biol. Chem. 2008, 283:21462-21468.
    • (2008) J. Biol. Chem. , vol.283 , pp. 21462-21468
    • Guo, J.1    Zhao, N.2
  • 34
    • 0023612118 scopus 로고
    • Identification of the iron-responsive element for the translational regulation of human ferritin mRNA
    • Hentze M.W., Caughman S.W., et al. Identification of the iron-responsive element for the translational regulation of human ferritin mRNA. Science 1987, 238(4833):1570-1573.
    • (1987) Science , vol.238 , Issue.4833 , pp. 1570-1573
    • Hentze, M.W.1    Caughman, S.W.2
  • 35
    • 77954249308 scopus 로고    scopus 로고
    • Two to tango: regulation of Mammalian iron metabolism
    • Hentze M.W., Muckenthaler M.U., Galy B., Camaschella C. Two to tango: regulation of Mammalian iron metabolism. Cell 2010, 142:24-38.
    • (2010) Cell , vol.142 , pp. 24-38
    • Hentze, M.W.1    Muckenthaler, M.U.2    Galy, B.3    Camaschella, C.4
  • 36
    • 80053902000 scopus 로고    scopus 로고
    • Iron insufficiency compromises motor neurons and their mitochondrial function in irp2-null mice
    • Jeong S.Y., Crooks D.R., et al. Iron insufficiency compromises motor neurons and their mitochondrial function in irp2-null mice. PLoS One 2011, 6(10):e25404.
    • (2011) PLoS One , vol.6 , Issue.10 , pp. e25404
    • Jeong, S.Y.1    Crooks, D.R.2
  • 37
    • 0029793466 scopus 로고    scopus 로고
    • Identification of a conserved and functional iron-responsive element in the 5'-untranslated region of mammalian mitochondrial aconitase
    • Kim H.Y., LaVaute T., et al. Identification of a conserved and functional iron-responsive element in the 5'-untranslated region of mammalian mitochondrial aconitase. J. Biol. Chem. 1996, 271(39):24226-24230.
    • (1996) J. Biol. Chem. , vol.271 , Issue.39 , pp. 24226-24230
    • Kim, H.Y.1    LaVaute, T.2
  • 38
    • 0035138456 scopus 로고    scopus 로고
    • Targeted deletion of the gene encoding iron regulatory protein-2 causes misregulation of iron metabolism and neurodegenerative disease in mice
    • LaVaute T., Smith S., et al. Targeted deletion of the gene encoding iron regulatory protein-2 causes misregulation of iron metabolism and neurodegenerative disease in mice. Nat. Genet. 2001, 27(2):209-214.
    • (2001) Nat. Genet. , vol.27 , Issue.2 , pp. 209-214
    • LaVaute, T.1    Smith, S.2
  • 39
    • 33748798494 scopus 로고    scopus 로고
    • Zip14 (Slc39a14) mediates non-transferrin-bound iron uptake into cells
    • Liuzzi J.P., Aydemir F., et al. Zip14 (Slc39a14) mediates non-transferrin-bound iron uptake into cells. Proc. Natl. Acad. Sci. U. S. A. 2006, 103(37):13612-13617.
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , Issue.37 , pp. 13612-13617
    • Liuzzi, J.P.1    Aydemir, F.2
  • 40
    • 84863116742 scopus 로고    scopus 로고
    • A systematic survey of loss-of-function variants in human protein-coding genes
    • MacArthur D.G., Balasubramanian S., et al. A systematic survey of loss-of-function variants in human protein-coding genes. Science 2012, 335(6070):823-828.
    • (2012) Science , vol.335 , Issue.6070 , pp. 823-828
    • MacArthur, D.G.1    Balasubramanian, S.2
  • 41
    • 34447550646 scopus 로고    scopus 로고
    • Regional dissection and determination of loosely bound and non-heme iron in the developing mouse brain
    • Magaki S., Mueller C., et al. Regional dissection and determination of loosely bound and non-heme iron in the developing mouse brain. Brain Res. 2007, 1158:144-150.
    • (2007) Brain Res. , vol.1158 , pp. 144-150
    • Magaki, S.1    Mueller, C.2
  • 42
    • 0033861745 scopus 로고    scopus 로고
    • A novel duodenal iron-regulated transporter, IREG1, implicated in the basolateral transfer of iron to the circulation
    • McKie A.T., Marciani P., et al. A novel duodenal iron-regulated transporter, IREG1, implicated in the basolateral transfer of iron to the circulation. Mol. Cell 2000, 5:299-309.
    • (2000) Mol. Cell , vol.5 , pp. 299-309
    • McKie, A.T.1    Marciani, P.2
  • 43
    • 0035793856 scopus 로고    scopus 로고
    • An iron-regulated ferric reductase associated with the absorption of dietary iron
    • McKie A.T., Barrow D., et al. An iron-regulated ferric reductase associated with the absorption of dietary iron. Science 2001, 291:1755-1759.
    • (2001) Science , vol.291 , pp. 1755-1759
    • McKie, A.T.1    Barrow, D.2
  • 44
    • 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., Ghosh M.C., et al. Genetic ablations of iron regulatory proteins 1 and 2 reveal why iron regulatory protein 2 dominates iron homeostasis. EMBO J. 2004, 23(2):386-395.
    • (2004) EMBO J. , vol.23 , Issue.2 , pp. 386-395
    • Meyron-Holtz, E.G.1    Ghosh, M.C.2
  • 45
    • 10844282789 scopus 로고    scopus 로고
    • Mammalian tissue oxygen levels modulate iron-regulatory protein activities in vivo
    • Meyron-Holtz E.G., Ghosh M.C., et al. Mammalian tissue oxygen levels modulate iron-regulatory protein activities in vivo. Science 2004, 306(5704):2087-2090.
    • (2004) Science , vol.306 , Issue.5704 , pp. 2087-2090
    • Meyron-Holtz, E.G.1    Ghosh, M.C.2
  • 46
    • 80052698326 scopus 로고    scopus 로고
    • The FBXL5-IRP2 axis is integral to control of iron metabolism in vivo
    • Moroishi T., Nishiyama M., et al. The FBXL5-IRP2 axis is integral to control of iron metabolism in vivo. Cell Metab. 2011, 14(3):339-351.
    • (2011) Cell Metab. , vol.14 , Issue.3 , pp. 339-351
    • Moroishi, T.1    Nishiyama, M.2
  • 47
    • 70349094837 scopus 로고    scopus 로고
    • Iron regulatory protein 2 is involved in brain copper homeostasis
    • Mueller C., Magaki S., et al. Iron regulatory protein 2 is involved in brain copper homeostasis. J. Alzheimers Dis. 2009, 18:201-210.
    • (2009) J. Alzheimers Dis. , vol.18 , pp. 201-210
    • Mueller, C.1    Magaki, S.2
  • 48
    • 0024276911 scopus 로고
    • A stem-loop in the 3' untranslated region mediates iron-dependent regulation of transferrin receptor mRNA stability in the cytoplasm
    • Mullner E.W., Kuhn L.C. A stem-loop in the 3' untranslated region mediates iron-dependent regulation of transferrin receptor mRNA stability in the cytoplasm. Cell 1988, 53(5):815-825.
    • (1988) Cell , vol.53 , Issue.5 , pp. 815-825
    • Mullner, E.W.1    Kuhn, L.C.2
  • 49
    • 10844258104 scopus 로고    scopus 로고
    • Hepcidin regulates cellular iron efflux by binding to ferroportin and inducing its internalization
    • Nemeth E., Tuttle M.S., et al. Hepcidin regulates cellular iron efflux by binding to ferroportin and inducing its internalization. Science 2004, 306(5704):2090-2093.
    • (2004) Science , vol.306 , Issue.5704 , pp. 2090-2093
    • Nemeth, E.1    Tuttle, M.S.2
  • 50
    • 27644455133 scopus 로고    scopus 로고
    • Identification of a ferrireductase required for efficient transferrin-dependent iron uptake in erythroid cells
    • Ohgami R.S., Campagna D.R., et al. Identification of a ferrireductase required for efficient transferrin-dependent iron uptake in erythroid cells. Nat. Genet. 2005, 37(11):1264-1269.
    • (2005) Nat. Genet. , vol.37 , Issue.11 , pp. 1264-1269
    • Ohgami, R.S.1    Campagna, D.R.2
  • 51
    • 1842608845 scopus 로고    scopus 로고
    • Iron metabolism and the IRE/IRP regulatory system: an update
    • Pantopoulos K. Iron metabolism and the IRE/IRP regulatory system: an update. Ann. N. Y. Acad. Sci. 2004, 1012:1-13.
    • (2004) Ann. N. Y. Acad. Sci. , vol.1012 , pp. 1-13
    • Pantopoulos, K.1
  • 52
    • 80053210392 scopus 로고    scopus 로고
    • Zip14 is a complex broad-scope metal ion transporter whose functional properties support roles in the cellular uptake of zinc and nontransferrin-bound iron
    • Pinilla-Tenas J.J., Sparkman B.K., et al. Zip14 is a complex broad-scope metal ion transporter whose functional properties support roles in the cellular uptake of zinc and nontransferrin-bound iron. Am. J. Physiol. Cell Physiol. 2011, 301:C862-C871.
    • (2011) Am. J. Physiol. Cell Physiol. , vol.301 , pp. C862-C871
    • Pinilla-Tenas, J.J.1    Sparkman, B.K.2
  • 53
    • 47149093139 scopus 로고    scopus 로고
    • Neurons lacking iron regulatory protein-2 are highly resistant to the toxicity of hemoglobin
    • Regan R.F., Chen M., et al. Neurons lacking iron regulatory protein-2 are highly resistant to the toxicity of hemoglobin. Neurobiol. Dis. 2008, 31(2):242-249.
    • (2008) Neurobiol. Dis. , vol.31 , Issue.2 , pp. 242-249
    • Regan, R.F.1    Chen, M.2
  • 54
    • 33746361251 scopus 로고    scopus 로고
    • The role of iron regulatory proteins in mammalian iron homeostasis and disease
    • Rouault T.A. The role of iron regulatory proteins in mammalian iron homeostasis and disease. Nat. Chem. Biol. 2006, 2(8):406-414.
    • (2006) Nat. Chem. Biol. , vol.2 , Issue.8 , pp. 406-414
    • Rouault, T.A.1
  • 55
    • 70350588653 scopus 로고    scopus 로고
    • Cell biology. An ancient gauge for iron
    • Rouault T.A. Cell biology. An ancient gauge for iron. Science 2009, 326:676-677.
    • (2009) Science , vol.326 , pp. 676-677
    • Rouault, T.A.1
  • 56
    • 84880805523 scopus 로고    scopus 로고
    • Iron metabolism in the CNS: implications for neurodegenerative diseases
    • Rouault T.A. Iron metabolism in the CNS: implications for neurodegenerative diseases. Nat. Rev. Neurosci. 2013, 14(8):551-564.
    • (2013) Nat. Rev. Neurosci. , vol.14 , Issue.8 , pp. 551-564
    • Rouault, T.A.1
  • 57
    • 84897107855 scopus 로고    scopus 로고
    • F-box and leucine-rich repeat protein 5 (FBXL5): sensing intracellular iron and oxygen
    • Ruiz J.C., Bruick R.K. F-box and leucine-rich repeat protein 5 (FBXL5): sensing intracellular iron and oxygen. J. Inorg. Biochem. 2014, 133:73-77.
    • (2014) J. Inorg. Biochem. , vol.133 , pp. 73-77
    • Ruiz, J.C.1    Bruick, R.K.2
  • 58
    • 70350576223 scopus 로고    scopus 로고
    • An E3 ligase possessing an iron-responsive hemerythrin domain is a regulator of iron homeostasis
    • Salahudeen A.A., Thompson J.W., et al. An E3 ligase possessing an iron-responsive hemerythrin domain is a regulator of iron homeostasis. Science 2009, 326(5953):722-726.
    • (2009) Science , vol.326 , Issue.5953 , pp. 722-726
    • Salahudeen, A.A.1    Thompson, J.W.2
  • 59
    • 24944457215 scopus 로고    scopus 로고
    • Neurochemical investigations of dopamine neuronal systems in iron-regulatory protein 2 (IRP-2) knockout mice
    • Salvatore M.F., Fisher B., et al. Neurochemical investigations of dopamine neuronal systems in iron-regulatory protein 2 (IRP-2) knockout mice. Brain Res. Mol. Brain Res. 2005, 139(2):341-347.
    • (2005) Brain Res. Mol. Brain Res. , vol.139 , Issue.2 , pp. 341-347
    • Salvatore, M.F.1    Fisher, B.2
  • 60
    • 34247628002 scopus 로고    scopus 로고
    • Iron-regulatory proteins limit hypoxia-inducible factor-2alpha expression in iron deficiency
    • Sanchez M., Galy B., et al. Iron-regulatory proteins limit hypoxia-inducible factor-2alpha expression in iron deficiency. Nat. Struct. Mol. Biol. 2007, 14(5):420-426.
    • (2007) Nat. Struct. Mol. Biol. , vol.14 , Issue.5 , pp. 420-426
    • Sanchez, M.1    Galy, B.2
  • 61
    • 0014907456 scopus 로고
    • State of iron(III) in normal human serum: low molecular weight and protein ligands besides transferrin
    • Sarkar B. State of iron(III) in normal human serum: low molecular weight and protein ligands besides transferrin. Can. J. Biochem. 1970, 48(12):1339-1350.
    • (1970) Can. J. Biochem. , vol.48 , Issue.12 , pp. 1339-1350
    • Sarkar, B.1
  • 62
    • 0032488980 scopus 로고    scopus 로고
    • Iron differentially stimulates translation of mitochondrial aconitase and ferritin mRNAs in mammalian cells. Implications for iron regulatory proteins as regulators of mitochondrial citrate utilization
    • Schalinske K.L., Chen O.S., et al. Iron differentially stimulates translation of mitochondrial aconitase and ferritin mRNAs in mammalian cells. Implications for iron regulatory proteins as regulators of mitochondrial citrate utilization. J. Biol. Chem. 1998, 273(6):3740-3746.
    • (1998) J. Biol. Chem. , vol.273 , Issue.6 , pp. 3740-3746
    • Schalinske, K.L.1    Chen, O.S.2
  • 63
    • 0032579795 scopus 로고    scopus 로고
    • Abnormal localization of iron regulatory protein in Alzheimer's disease
    • Smith M.A., Wehr K., et al. Abnormal localization of iron regulatory protein in Alzheimer's disease. Brain Res. 1998, 788(1-2):232-236.
    • (1998) Brain Res. , vol.788 , Issue.1-2 , pp. 232-236
    • Smith, M.A.1    Wehr, K.2
  • 64
    • 11144353669 scopus 로고    scopus 로고
    • Severity of neurodegeneration correlates with compromise of iron metabolism in mice with iron regulatory protein deficiencies
    • Smith S.R., Cooperman S., et al. Severity of neurodegeneration correlates with compromise of iron metabolism in mice with iron regulatory protein deficiencies. Ann. N. Y. Acad. Sci. 2004, 1012:65-83.
    • (2004) Ann. N. Y. Acad. Sci. , vol.1012 , pp. 65-83
    • Smith, S.R.1    Cooperman, S.2
  • 65
    • 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., Ghosh M.C., 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. 2006, 36(2):283-287.
    • (2006) Blood Cells Mol. Dis. , vol.36 , Issue.2 , pp. 283-287
    • Smith, S.R.1    Ghosh, M.C.2
  • 66
    • 0025248551 scopus 로고
    • Regulation of ferritin and transferrin receptor mRNAs
    • Theil E.C. Regulation of ferritin and transferrin receptor mRNAs. J. Biol. Chem. 1990, 265(9):4771-4774.
    • (1990) J. Biol. Chem. , vol.265 , Issue.9 , pp. 4771-4774
    • Theil, E.C.1
  • 67
    • 0031020884 scopus 로고    scopus 로고
    • Endothelial PAS domain protein 1 (EPAS1), a transcription factor selectively expressed in endothelial cells
    • Tian H., McKnight S.L., et al. Endothelial PAS domain protein 1 (EPAS1), a transcription factor selectively expressed in endothelial cells. Genes Dev. 1997, 11:72-82.
    • (1997) Genes Dev. , vol.11 , pp. 72-82
    • Tian, H.1    McKnight, S.L.2
  • 68
    • 77956327702 scopus 로고    scopus 로고
    • Intestinal ferritin H is required for an accurate control of iron absorption
    • Vanoaica L., Darshan D., et al. Intestinal ferritin H is required for an accurate control of iron absorption. Cell Metab. 2010, 12:273-282.
    • (2010) Cell Metab. , vol.12 , pp. 273-282
    • Vanoaica, L.1    Darshan, D.2
  • 69
    • 70350613915 scopus 로고    scopus 로고
    • Control of iron homeostasis by an iron-regulated ubiquitin ligase
    • Vashisht A.A., Zumbrennen K.B., et al. Control of iron homeostasis by an iron-regulated ubiquitin ligase. Science 2009, 326(5953):718-721.
    • (2009) Science , vol.326 , Issue.5953 , pp. 718-721
    • Vashisht, A.A.1    Zumbrennen, K.B.2
  • 70
    • 0032909207 scopus 로고    scopus 로고
    • Hephaestin, a ceruloplasmin homologue implicated in intestinal iron transport, is defective in the sla mouse
    • Vulpe C.D., Kuo Y.M., et al. Hephaestin, a ceruloplasmin homologue implicated in intestinal iron transport, is defective in the sla mouse. Nat. Genet. 1999, 21(2):195-199.
    • (1999) Nat. Genet. , vol.21 , Issue.2 , pp. 195-199
    • Vulpe, C.D.1    Kuo, Y.M.2
  • 71
    • 1642458415 scopus 로고    scopus 로고
    • Iron-mediated degradation of IRP2, an unexpected pathway involving a 2-oxoglutarate-dependent oxygenase activity
    • Wang J., Chen G., et al. Iron-mediated degradation of IRP2, an unexpected pathway involving a 2-oxoglutarate-dependent oxygenase activity. Mol. Cell. Biol. 2004, 24(3):954-965.
    • (2004) Mol. Cell. Biol. , vol.24 , Issue.3 , pp. 954-965
    • Wang, J.1    Chen, G.2
  • 72
    • 84888037689 scopus 로고    scopus 로고
    • IRP1 regulates erythropoiesis and systemic iron homeostasis by controlling HIF2alpha mRNA translation
    • Wilkinson N., Pantopoulos K. IRP1 regulates erythropoiesis and systemic iron homeostasis by controlling HIF2alpha mRNA translation. Blood 2013, 122(9):1658-1668.
    • (2013) Blood , vol.122 , Issue.9 , pp. 1658-1668
    • Wilkinson, N.1    Pantopoulos, K.2
  • 73
    • 84904764584 scopus 로고    scopus 로고
    • The IRP/IRE system in vivo: insights from mouse models
    • Wilkinson N., Pantopoulos K. The IRP/IRE system in vivo: insights from mouse models. Front. Pharmacol. 2014, 5(176):1-15.
    • (2014) Front. Pharmacol. , vol.5 , Issue.176 , pp. 1-15
    • Wilkinson, N.1    Pantopoulos, K.2
  • 74
    • 33747151612 scopus 로고    scopus 로고
    • Plasma copper, iron, ceruloplasmin and ferroxidase activity in schizophrenia
    • Wolf T.L., Kotun J., Meador-Woodruff J.H. Plasma copper, iron, ceruloplasmin and ferroxidase activity in schizophrenia. Schizophr. Res. 2006, 86(1-3):167-171.
    • (2006) Schizophr. Res. , vol.86 , Issue.1-3 , pp. 167-171
    • Wolf, T.L.1    Kotun, J.2    Meador-Woodruff, J.H.3
  • 75
    • 8344265251 scopus 로고    scopus 로고
    • Iron, brain ageing and neurodegenerative disorders
    • Zecca L., Youdim M.B., et al. Iron, brain ageing and neurodegenerative disorders. Nat. Rev. Neurosci. 2004, 5(11):863-873.
    • (2004) Nat. Rev. Neurosci. , vol.5 , Issue.11 , pp. 863-873
    • Zecca, L.1    Youdim, M.B.2
  • 76
    • 20944442873 scopus 로고    scopus 로고
    • Electron tomography of degenerating neurons in mice with abnormal regulation of iron metabolism
    • Zhang P., Land W., et al. Electron tomography of degenerating neurons in mice with abnormal regulation of iron metabolism. J. Struct. Biol. 2005, 150(2):144-153.
    • (2005) J. Struct. Biol. , vol.150 , Issue.2 , pp. 144-153
    • Zhang, P.1    Land, W.2
  • 77
    • 84904738032 scopus 로고    scopus 로고
    • The physiological functions of iron regulatory proteins in iron homeostasis-an update
    • Zhang D.-L., Ghosh M.C., Rouault T.A. The physiological functions of iron regulatory proteins in iron homeostasis-an update. Front. Pharmacol. 2014, 5(124):1-12.
    • (2014) Front. Pharmacol. , vol.5 , Issue.124 , pp. 1-12
    • Zhang, D.-L.1    Ghosh, M.C.2    Rouault, T.A.3
  • 78
    • 57849147670 scopus 로고    scopus 로고
    • Small-molecule inhibitors of HIF-2a translation link its 5'UTR iron-responsive element to oxygen sensing
    • Zimmer M., Ebert B.L., et al. Small-molecule inhibitors of HIF-2a translation link its 5'UTR iron-responsive element to oxygen sensing. Mol. Cell 2008, 32(6):838-848.
    • (2008) Mol. Cell , vol.32 , Issue.6 , pp. 838-848
    • Zimmer, M.1    Ebert, B.L.2
  • 79
    • 84902438197 scopus 로고    scopus 로고
    • Abnormal brain iron metabolism in Irp2 deficient mice is associated with mild neurological and behavioral impairments
    • Zumbrennen-Bullough K.B., Becker L., et al. Abnormal brain iron metabolism in Irp2 deficient mice is associated with mild neurological and behavioral impairments. PLoS One 2014, 9(6):e98072.
    • (2014) PLoS One , vol.9 , Issue.6 , pp. e98072
    • Zumbrennen-Bullough, K.B.1    Becker, L.2


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