메뉴 건너뛰기




Volumn 24, Issue 2-3, 2002, Pages 188-196

Brain iron metabolism and neurodegenerative disorders

Author keywords

Gene; Iron; Metabolism; Mutation; Neurodegeneration; Single nucleotide polymorphism

Indexed keywords

M PROTEIN;

EID: 0036970185     PISSN: 03785866     EISSN: None     Source Type: Journal    
DOI: 10.1159/000065701     Document Type: Review
Times cited : (81)

References (111)
  • 2
    • 0033826764 scopus 로고    scopus 로고
    • Iron regulatory proteins and the molecular control of mammalian iron metabolism
    • Eisenstein R: Iron regulatory proteins and the molecular control of mammalian iron metabolism. Annu Rev Nutr 2000;20:627-662.
    • (2000) Annu Rev Nutr , vol.20 , pp. 627-662
    • Eisenstein, R.1
  • 3
    • 0034839086 scopus 로고    scopus 로고
    • Systemic iron metabolism: A review and implications for brain iron metabolism
    • Rouault T: Systemic iron metabolism: A review and implications for brain iron metabolism. Pediatr Neurol 2001;25:130-137.
    • (2001) Pediatr Neurol , vol.25 , pp. 130-137
    • Rouault, T.1
  • 4
    • 0029848477 scopus 로고    scopus 로고
    • Tryptophan hydroxylase: Cloning and expression of the rat brain enzyme in mammalian cells
    • D'Sa CM, Arthur RE Jr, States JC, Kuhn DM: Tryptophan hydroxylase: Cloning and expression of the rat brain enzyme in mammalian cells. J Neurochem 1996;67:900-906.
    • (1996) J Neurochem , vol.67 , pp. 900-906
    • D'Sa, C.M.1    Arthur R.E., Jr.2    States, J.C.3    Kuhn, D.M.4
  • 5
    • 0030174825 scopus 로고    scopus 로고
    • Relationship of iron to oligodendrocytes and myelination
    • Connor JR, Menzies SL: Relationship of iron to oligodendrocytes and myelination. Glia 1996;17:83-93.
    • (1996) Glia , vol.17 , pp. 83-93
    • Connor, J.R.1    Menzies, S.L.2
  • 6
    • 0029024235 scopus 로고
    • A histochemical study of iron-positive cells in the developing rat brain
    • Connor JR, Pavlick G, Karli D, Menzies SL, Palmer C: A histochemical study of iron-positive cells in the developing rat brain. J Comp Neurol 1995;355:111-123.
    • (1995) J Comp Neurol , vol.355 , pp. 111-123
    • Connor, J.R.1    Pavlick, G.2    Karli, D.3    Menzies, S.L.4    Palmer, C.5
  • 7
    • 0026590705 scopus 로고
    • Regional distribution of iron and iron-regulatory proteins in the brain in aging and Alzheimer's disease
    • Connor JR, Snyder BS, Beard JL, Fine RE, Mufson EJ: Regional distribution of iron and iron-regulatory proteins in the brain in aging and Alzheimer's disease. J Neurosci Res 1992;31:327-335.
    • (1992) J Neurosci Res , vol.31 , pp. 327-335
    • Connor, J.R.1    Snyder, B.S.2    Beard, J.L.3    Fine, R.E.4    Mufson, E.J.5
  • 9
    • 0030952974 scopus 로고    scopus 로고
    • MR evaluation of age-related increase of brain iron in young adult and older normal males
    • Bartzokis G, Beckson M, Hance D, Marx P, Foster J, Marder S: MR evaluation of age-related increase of brain iron in young adult and older normal males. Magn Reson Imaging 1997;15:29-35.
    • (1997) Magn Reson Imaging , vol.15 , pp. 29-35
    • Bartzokis, G.1    Beckson, M.2    Hance, D.3    Marx, P.4    Foster, J.5    Marder, S.6
  • 11
    • 0032504710 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in neurodegenerative diseases
    • Beal MF: Mitochondrial dysfunction in neurodegenerative diseases. Biochim Biophys Acta 1998;1366:211-223.
    • (1998) Biochim Biophys Acta , vol.1366 , pp. 211-223
    • Beal, M.F.1
  • 12
    • 0342598367 scopus 로고    scopus 로고
    • Iron homeostasis and Parkinson's disease
    • Faucheux B, Hirsch E: Iron homeostasis and Parkinson's disease (in French). Ann Biol Clin (Paris) 1998;56(Spec No):23-30.
    • (1998) Ann Biol Clin (Paris) , vol.56 , Issue.SPEC. NO. , pp. 23-30
    • Faucheux, B.1    Hirsch, E.2
  • 13
    • 0030424010 scopus 로고    scopus 로고
    • Iron metabolism: A comprehensive review
    • Beard JL, Dawson H, Pinero DJ: Iron metabolism: A comprehensive review. Nutr Rev 1996;54:295-317.
    • (1996) Nutr Rev , vol.54 , pp. 295-317
    • Beard, J.L.1    Dawson, H.2    Pinero, D.J.3
  • 14
    • 0030624029 scopus 로고    scopus 로고
    • Regulation of iron metabolism in eukaryotes
    • Rouault T, Klausner R: Regulation of iron metabolism in eukaryotes. Curr Top Cell Regul 1997;35:1-19.
    • (1997) Curr Top Cell Regul , vol.35 , pp. 1-19
    • Rouault, T.1    Klausner, R.2
  • 15
    • 0028868660 scopus 로고
    • Overview and mechanisms of iron regulation
    • Bothwell T: Overview and mechanisms of iron regulation. Nutr Rev 1995;53:237-245.
    • (1995) Nutr Rev , vol.53 , pp. 237-245
    • Bothwell, T.1
  • 17
    • 0030739637 scopus 로고    scopus 로고
    • Transport of iron in the blood-brain-cerebrospinal fluid system
    • Bradbury MW: Transport of iron in the blood-brain-cerebrospinal fluid system. J Neurochem 1997;69:443-454.
    • (1997) J Neurochem , vol.69 , pp. 443-454
    • Bradbury, M.W.1
  • 18
    • 0029976834 scopus 로고    scopus 로고
    • Immunohistochemical localization of intraneuronal transferrin receptor immunoreactivity in the adult mouse central nervous system
    • Moos T: Immunohistochemical localization of intraneuronal transferrin receptor immunoreactivity in the adult mouse central nervous system. J Comp Neurol 1996;375:675-692.
    • (1996) J Comp Neurol , vol.375 , pp. 675-692
    • Moos, T.1
  • 19
    • 0027723591 scopus 로고
    • Lactotransferrin immunocytochemistry in Alzheimer and normal human brain
    • Kawamata T, Tooyama I, Yamada T, Walker DG, McGeer PL: Lactotransferrin immunocytochemistry in Alzheimer and normal human brain. Am J Pathol 1993;142:1574-1585.
    • (1993) Am J Pathol , vol.142 , pp. 1574-1585
    • Kawamata, T.1    Tooyama, I.2    Yamada, T.3    Walker, D.G.4    McGeer, P.L.5
  • 20
    • 0028321575 scopus 로고
    • The iron-binding protein lacto-transferrin is present in pathologic lesions in a variety of neurodegenerative disorders: A comparative immunohistochemical analysis
    • Leveugle B, Spik G, Perl DP, Bouras C, Fillit HM, Hof PR: The iron-binding protein lacto-transferrin is present in pathologic lesions in a variety of neurodegenerative disorders: A comparative immunohistochemical analysis. Brain Res 1994;650:20-31.
    • (1994) Brain Res , vol.650 , pp. 20-31
    • Leveugle, B.1    Spik, G.2    Perl, D.P.3    Bouras, C.4    Fillit, H.M.5    Hof, P.R.6
  • 21
    • 0034635402 scopus 로고    scopus 로고
    • Alternative RNA splicing generates a glycosylphosphatidylinositol-anchored form of ceruloplasmin in mammalian brain
    • Patel B, Dunn R, David S: Alternative RNA splicing generates a glycosylphosphatidylinositol-anchored form of ceruloplasmin in mammalian brain. J Biol Chem 2000;275:4305-4310.
    • (2000) J Biol Chem , vol.275 , pp. 4305-4310
    • Patel, B.1    Dunn, R.2    David, S.3
  • 22
    • 0029800745 scopus 로고    scopus 로고
    • Expression of the ceruloplasmin gene in the human retina and brain: Implications for a pathogenic model in aceruloplasminemia
    • Klomp L, Gitlin J: Expression of the ceruloplasmin gene in the human retina and brain: Implications for a pathogenic model in aceruloplasminemia. Hum Mol Genet 1996;5:1989-1996.
    • (1996) Hum Mol Genet , vol.5 , pp. 1989-1996
    • Klomp, L.1    Gitlin, J.2
  • 23
    • 0033961913 scopus 로고    scopus 로고
    • Transferrin and transferrin receptor function in brain barrier systems
    • Moos T, Morgan E: Transferrin and transferrin receptor function in brain barrier systems. Cell Mol Neurobiol 2000;20:77-95.
    • (2000) Cell Mol Neurobiol , vol.20 , pp. 77-95
    • Moos, T.1    Morgan, E.2
  • 24
    • 0026779690 scopus 로고
    • Iron and transferrin uptake by brain and cerebrospinal fluid in the rat
    • Crowe A, Morgan EH: Iron and transferrin uptake by brain and cerebrospinal fluid in the rat. Brain Res 1992;592:8-16.
    • (1992) Brain Res , vol.592 , pp. 8-16
    • Crowe, A.1    Morgan, E.H.2
  • 26
    • 0033534589 scopus 로고    scopus 로고
    • Ceruloplasmin ferroxidase activity stimulates cellular iron uptake by a trivalent cation-specific transport mechanism
    • Attieh ZK, Mukhopadhyay CK, Seshadri V, Tripoulas NA, Fox PL: Ceruloplasmin ferroxidase activity stimulates cellular iron uptake by a trivalent cation-specific transport mechanism. J Biol Chem 1999;274:1116-1123.
    • (1999) J Biol Chem , vol.274 , pp. 1116-1123
    • Attieh, Z.K.1    Mukhopadhyay, C.K.2    Seshadri, V.3    Tripoulas, N.A.4    Fox, P.L.5
  • 29
  • 30
    • 0033137124 scopus 로고    scopus 로고
    • Distribution of transferrin and ferritin binding in normal and multiple sclerotic human brains
    • Hulet SW, Powers S, Connor JR: Distribution of transferrin and ferritin binding in normal and multiple sclerotic human brains. J Neurol Sci 1999;165:48-55.
    • (1999) J Neurol Sci , vol.165 , pp. 48-55
    • Hulet, S.W.1    Powers, S.2    Connor, J.R.3
  • 33
    • 0034733635 scopus 로고    scopus 로고
    • A novel mammalian iron-regulated protein involved in intracellular iron metabolism
    • Abboud S, Haile D: 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.2
  • 34
    • 0034282914 scopus 로고    scopus 로고
    • Intact human ceruloplasmin is required for the incorporation of iron into human ferritin
    • Van Eden ME, Aust SD: Intact human ceruloplasmin is required for the incorporation of iron into human ferritin. Arch Biochem Biophys 2000;381:119-126.
    • (2000) Arch Biochem Biophys , vol.381 , pp. 119-126
    • Van Eden, M.E.1    Aust, S.D.2
  • 38
    • 0032970494 scopus 로고    scopus 로고
    • Mitochondrial iron sequestration in dopamine-challenged astroglia: Role of heme oxygenase-1 and the permeability transition pore
    • Schipper HM, Bernier L, Mehindate K, Frankel D: Mitochondrial iron sequestration in dopamine-challenged astroglia: Role of heme oxygenase-1 and the permeability transition pore. J Neurochem 1999;72:1802-1811.
    • (1999) J Neurochem , vol.72 , pp. 1802-1811
    • Schipper, H.M.1    Bernier, L.2    Mehindate, K.3    Frankel, D.4
  • 40
    • 0030813487 scopus 로고    scopus 로고
    • Studies of human, mouse and yeast homologues indicate a mitochondrial function for frataxin
    • Koutnikova H, Campuzano V, Foury F, Dolle P, Cazzalini O, Koenig M: Studies of human, mouse and yeast homologues indicate a mitochondrial function for frataxin. Nat Genet 1997;16:345-351.
    • (1997) Nat Genet , vol.16 , pp. 345-351
    • Koutnikova, H.1    Campuzano, V.2    Foury, F.3    Dolle, P.4    Cazzalini, O.5    Koenig, M.6
  • 41
    • 0030791598 scopus 로고    scopus 로고
    • Frataxin gene of Friedreich's ataxia is targeted to mitochondria
    • Priller J, Scherzer C, Faber P, MacDonald M, Young A: Frataxin gene of Friedreich's ataxia is targeted to mitochondria. Ann Neurol 1997;42:265-269.
    • (1997) Ann Neurol , vol.42 , pp. 265-269
    • Priller, J.1    Scherzer, C.2    Faber, P.3    MacDonald, M.4    Young, A.5
  • 43
    • 0035474950 scopus 로고    scopus 로고
    • Recent advances in disorders of iron metabolism: Mutations, mechanisms and modifiers
    • Roy C, Andrews N: Recent advances in disorders of iron metabolism: Mutations, mechanisms and modifiers. Hum Mol Genet 2001;10:2181-2186.
    • (2001) Hum Mol Genet , vol.10 , pp. 2181-2186
    • Roy, C.1    Andrews, N.2
  • 44
    • 0029039795 scopus 로고
    • Time-dependent changes in iron levels and associated neuronal loss within the substantia nigra following lesions within the neostriatum/globus pallidus complex
    • Sastry S, Arendash GW: Time-dependent changes in iron levels and associated neuronal loss within the substantia nigra following lesions within the neostriatum/globus pallidus complex. Neuroscience 1995;67:649-666.
    • (1995) Neuroscience , vol.67 , pp. 649-666
    • Sastry, S.1    Arendash, G.W.2
  • 45
    • 0008881566 scopus 로고    scopus 로고
    • The heme oxygenase system and its functions in the brain
    • Maines M: The heme oxygenase system and its functions in the brain. Cell Mol Biol (Noisy-le-grand) 2000;46:573-585.
    • (2000) Cell Mol Biol (Noisy-le-grand) , vol.46 , pp. 573-585
    • Maines, M.1
  • 46
    • 0036212575 scopus 로고    scopus 로고
    • Regional distribution of heme oxygenase, HSP70, and glutathione in brain: Relevance for endogenous oxidant/antioxidant balance and stress tolerance
    • Calabrese V, Scapagnini G, Ravagna A, Fariello RG, Giuffrida Stella AM, Abraham NG: Regional distribution of heme oxygenase, HSP70, and glutathione in brain: Relevance for endogenous oxidant/antioxidant balance and stress tolerance. J Neurosci Res 2002;68:65-75.
    • (2002) J Neurosci Res , vol.68 , pp. 65-75
    • Calabrese, V.1    Scapagnini, G.2    Ravagna, A.3    Fariello, R.G.4    Giuffrida Stella, A.M.5    Abraham, N.G.6
  • 47
    • 0030886381 scopus 로고    scopus 로고
    • Heme oxygenase 1 is required for mammalian iron reutilization
    • Poss K, Tonegawa S: Heme oxygenase 1 is required for mammalian iron reutilization. Proc Natl Acad Sci USA 1997;94:10919-10924.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 10919-10924
    • Poss, K.1    Tonegawa, S.2
  • 48
    • 0034999085 scopus 로고    scopus 로고
    • Proinflammatory cytokines promote glial heme oxygenase-1 expression and mitochondrial iron deposition: Implications for multiple sclerosis
    • Mehindate K, Sahlas DJ, Frankel D, Mawal Y, Liberman A, Corcos J, Dion S, Schipper HM: Proinflammatory cytokines promote glial heme oxygenase-1 expression and mitochondrial iron deposition: Implications for multiple sclerosis. J Neurochem 2001;77:1386-1395.
    • (2001) J Neurochem , vol.77 , pp. 1386-1395
    • Mehindate, K.1    Sahlas, D.J.2    Frankel, D.3    Mawal, Y.4    Liberman, A.5    Corcos, J.6    Dion, S.7    Schipper, H.M.8
  • 49
    • 0035126635 scopus 로고    scopus 로고
    • Heme oxygenase-1 (HSP-32) and heme oxygenase-2 induction in neurons and glial cells of cerebral regions and its relation to iron accumulation after focal cortical photothrombosis
    • Bidmon HJ, Emde B, Oermann E, Kubitz R, Witte OW, Zilles K: Heme oxygenase-1 (HSP-32) and heme oxygenase-2 induction in neurons and glial cells of cerebral regions and its relation to iron accumulation after focal cortical photothrombosis. Exp Neurol 2001;168:1-22.
    • (2001) Exp Neurol , vol.168 , pp. 1-22
    • Bidmon, H.J.1    Emde, B.2    Oermann, E.3    Kubitz, R.4    Witte, O.W.5    Zilles, K.6
  • 51
    • 0032427653 scopus 로고    scopus 로고
    • Kupffer cell staining by an HFE-specific monoclonal antibody: Implications for hereditary haemochromatosis
    • Bastin J, Jones M, O'Callaghan C, Schimanski L, Mason D, Townsend A: Kupffer cell staining by an HFE-specific monoclonal antibody: Implications for hereditary haemochromatosis. Br J Haematol 1998;103:931-941.
    • (1998) Br J Haematol , vol.103 , pp. 931-941
    • Bastin, J.1    Jones, M.2    O'Callaghan, C.3    Schimanski, L.4    Mason, D.5    Townsend, A.6
  • 52
    • 0034935074 scopus 로고    scopus 로고
    • Iron on the brain
    • Rouault T: Iron on the brain. Nat Genet 2001;28:299-300.
    • (2001) Nat Genet , vol.28 , pp. 299-300
    • Rouault, T.1
  • 53
    • 0012809058 scopus 로고    scopus 로고
    • Neurodegeneration: Iron weighs in
    • Coburn B: Neurodegeneration: Iron weighs in. Clin Genet 2001;60:267-269.
    • (2001) Clin Genet , vol.60 , pp. 267-269
    • Coburn, B.1
  • 54
    • 0034851578 scopus 로고    scopus 로고
    • Iron overload, oxidative stress, and axonal dystrophy in brain disorders
    • Chiueh CC: Iron overload, oxidative stress, and axonal dystrophy in brain disorders. Pediatr Neurol 2001;25:138-147.
    • (2001) Pediatr Neurol , vol.25 , pp. 138-147
    • Chiueh, C.C.1
  • 55
    • 0031947244 scopus 로고    scopus 로고
    • Iron metabolism and Parkinson's disease
    • Hirsch E, Faucheux B: Iron metabolism and Parkinson's disease. Mov Disord 1998;13(suppl 1):39-45.
    • (1998) Mov Disord , vol.13 , Issue.SUPPL. 1 , pp. 39-45
    • Hirsch, E.1    Faucheux, B.2
  • 57
    • 0033577159 scopus 로고    scopus 로고
    • Oxidative stress induces amyloid-like aggregate formation of NACP/alpha-synuclein in vitro
    • Hashimoto M, Hsu LJ, Xia Y, Takeda A, Sisk A, Sundsmo M, Masliah E: Oxidative stress induces amyloid-like aggregate formation of NACP/alpha-synuclein in vitro. Neuroreport 1999;10:717-721.
    • (1999) Neuroreport , vol.10 , pp. 717-721
    • Hashimoto, M.1    Hsu, L.J.2    Xia, Y.3    Takeda, A.4    Sisk, A.5    Sundsmo, M.6    Masliah, E.7
  • 58
    • 0032748301 scopus 로고    scopus 로고
    • Hydroxyl radical and superoxide dismutase in blood of patients with Parkinson's disease: Relationship to clinical data
    • Ihara Y, Chuda M, Kuroda S, Hayabara T: Hydroxyl radical and superoxide dismutase in blood of patients with Parkinson's disease: Relationship to clinical data. J Neurol Sci 1999;170:90-95.
    • (1999) J Neurol Sci , vol.170 , pp. 90-95
    • Ihara, Y.1    Chuda, M.2    Kuroda, S.3    Hayabara, T.4
  • 63
    • 0026513756 scopus 로고
    • A histochemical study of iron, transferrin, and ferritin in Alzheimer's diseased brains
    • Connor JR, Menzies SL, St Martin SM, Mufson EJ: A histochemical study of iron, transferrin, and ferritin in Alzheimer's diseased brains. J Neurosci Res 1992;31:75-83.
    • (1992) J Neurosci Res , vol.31 , pp. 75-83
    • Connor, J.R.1    Menzies, S.L.2    St Martin, S.M.3    Mufson, E.J.4
  • 65
    • 0033525735 scopus 로고    scopus 로고
    • Translation of the Alzheimer amyloid precursor protein mRNA is up-regulated by interleukin-1 through 5′-untranslated region sequences
    • Rogers JT, Leiter LM, McPhee J, Cahill CM, Zhan SS, Potter H, Nilsson LN: Translation of the Alzheimer amyloid precursor protein mRNA is up-regulated by interleukin-1 through 5′-untranslated region sequences. J Biol Chem 1999;274:6421-6431.
    • (1999) J Biol Chem , vol.274 , pp. 6421-6431
    • Rogers, J.T.1    Leiter, L.M.2    McPhee, J.3    Cahill, C.M.4    Zhan, S.S.5    Potter, H.6    Nilsson, L.N.7
  • 68
    • 0030885482 scopus 로고    scopus 로고
    • Iron accumulation in Alzheimer disease is a source of redox-generated free radicals
    • Smith MA, Harris PL, Sayre LM, Perry G: Iron accumulation in Alzheimer disease is a source of redox-generated free radicals. Proc Natl Acad Sci USA 1997;94:9866-9868.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 9866-9868
    • Smith, M.A.1    Harris, P.L.2    Sayre, L.M.3    Perry, G.4
  • 69
    • 0033964859 scopus 로고    scopus 로고
    • In situ oxidative catalysis by neurofibrillary tangles and senile plaques in Alzheimer's disease: A central role for bound transition metals
    • Sayre LM, Perry G, Harris PL, Liu Y, Schubert KA, Smith MA: In situ oxidative catalysis by neurofibrillary tangles and senile plaques in Alzheimer's disease: A central role for bound transition metals. J Neurochem 2000;74:270-279.
    • (2000) J Neurochem , vol.74 , pp. 270-279
    • Sayre, L.M.1    Perry, G.2    Harris, P.L.3    Liu, Y.4    Schubert, K.A.5    Smith, M.A.6
  • 70
    • 0033793044 scopus 로고    scopus 로고
    • Heme oxygenase-1: Role in brain aging and neurodegeneration
    • Schipper HM: Heme oxygenase-1: Role in brain aging and neurodegeneration. Exp Gerontol 2000;35:821-830.
    • (2000) Exp Gerontol , vol.35 , pp. 821-830
    • Schipper, H.M.1
  • 71
    • 0029935613 scopus 로고    scopus 로고
    • Reactive microglia specifically associated with amyloid plaques in Alzheimer's disease brain tissue express melanotransferrin
    • Jefferies WA, Food MR, Gabathuler R, Rothenberger S, Yamada T, Yasuhara O, McGeer PL: Reactive microglia specifically associated with amyloid plaques in Alzheimer's disease brain tissue express melanotransferrin. Brain Res 1996;712:122-126.
    • (1996) Brain Res , vol.712 , pp. 122-126
    • Jefferies, W.A.1    Food, M.R.2    Gabathuler, R.3    Rothenberger, S.4    Yamada, T.5    Yasuhara, O.6    McGeer, P.L.7
  • 72
    • 0035756132 scopus 로고    scopus 로고
    • On the structural form of iron in ferritin cores associated with progressive supranuclear palsy and Alzheimer's disease
    • Online Pub
    • Dobson J: On the structural form of iron in ferritin cores associated with progressive supranuclear palsy and Alzheimer's disease. Cell Mol Biol (Noisy-le-grand) 2001;47(Online Pub):OL49-OL50.
    • (2001) Cell Mol Biol (Noisy-le-grand) , vol.47
    • Dobson, J.1
  • 73
    • 0035805163 scopus 로고    scopus 로고
    • Nanoscale biogenic iron oxides and neurodegenerative disease
    • Dobson J: Nanoscale biogenic iron oxides and neurodegenerative disease. FEBS Lett 2001;496:1-5.
    • (2001) FEBS Lett , vol.496 , pp. 1-5
    • Dobson, J.1
  • 80
    • 0026746512 scopus 로고
    • Neuromelanin-containing neurons of the substantia nigra accumulate iron and aluminum in Parkinson's disease: A LAMMA study
    • Good PF, Olanow CW, Perl DP: Neuromelanin-containing neurons of the substantia nigra accumulate iron and aluminum in Parkinson's disease: A LAMMA study. Brain Res 1992;593:343-346.
    • (1992) Brain Res , vol.593 , pp. 343-346
    • Good, P.F.1    Olanow, C.W.2    Perl, D.P.3
  • 81
    • 0034023930 scopus 로고    scopus 로고
    • MPTP selectively induces haem oxygenase-1 expression in striatal astrocytes
    • Fernandez-Gonzalez A, Perez-Otano I, Morgan JI: MPTP selectively induces haem oxygenase-1 expression in striatal astrocytes. Eur J Neurosci 2000;12:1573-1583.
    • (2000) Eur J Neurosci , vol.12 , pp. 1573-1583
    • Fernandez-Gonzalez, A.1    Perez-Otano, I.2    Morgan, J.I.3
  • 83
    • 0012896150 scopus 로고    scopus 로고
    • Mutations in iron-regulatory protein 2 (IRP2) and lack of association with sporadic Parkinson's disease
    • in press
    • Lee PL, Gelbart T, West C, Halloran C, Sipe JC, Beutler E: Mutations in iron-regulatory protein 2 (IRP2) and lack of association with sporadic Parkinson's disease. Mov Disord 2002, in press.
    • (2002) Mov Disord
    • Lee, P.L.1    Gelbart, T.2    West, C.3    Halloran, C.4    Sipe, J.C.5    Beutler, E.6
  • 84
    • 0033597299 scopus 로고    scopus 로고
    • Reduced ferroxidase activity in the cerebrospinal fluid from patients with Parkinson's disease
    • Boll MC, Sotelo J, Otero E, Alcaraz-Zubeldia M, Rios C: Reduced ferroxidase activity in the cerebrospinal fluid from patients with Parkinson's disease. Neurosci Lett 1999;265:155-158.
    • (1999) Neurosci Lett , vol.265 , pp. 155-158
    • Boll, M.C.1    Sotelo, J.2    Otero, E.3    Alcaraz-Zubeldia, M.4    Rios, C.5
  • 85
    • 0034966041 scopus 로고    scopus 로고
    • Polymorphisms in the transferrin 5′ flanking region associated with differences in total iron binding capacity: Possible implications in iron homeostasis
    • Lee PL, Halloran C, Beutler E: Polymorphisms in the transferrin 5′ flanking region associated with differences in total iron binding capacity: Possible implications in iron homeostasis. Blood Cells Mol Dis 2001;27:539-548.
    • (2001) Blood Cells Mol Dis , vol.27 , pp. 539-548
    • Lee, P.L.1    Halloran, C.2    Beutler, E.3
  • 86
    • 0030033775 scopus 로고    scopus 로고
    • Signal changes on MRI and increases in reactive microgliosis, astrogliosis, and iron in the putamen of two patients with multiple system atrophy
    • Schwarz J, Weis S, Kraft E, Tatsch K, Bandmann O, Mehraein P, Vogl T, Oertel WH: Signal changes on MRI and increases in reactive microgliosis, astrogliosis, and iron in the putamen of two patients with multiple system atrophy. J Neurol Neurosurg Psychiatry 1996;60:98-101.
    • (1996) J Neurol Neurosurg Psychiatry , vol.60 , pp. 98-101
    • Schwarz, J.1    Weis, S.2    Kraft, E.3    Tatsch, K.4    Bandmann, O.5    Mehraein, P.6    Vogl, T.7    Oertel, W.H.8
  • 87
    • 0035666667 scopus 로고    scopus 로고
    • Multiple system atrophy: Cellular and molecular pathology
    • Burn DJ, Jaros E: Multiple system atrophy: Cellular and molecular pathology. Mol Pathol 2001;54:419-426.
    • (2001) Mol Pathol , vol.54 , pp. 419-426
    • Burn, D.J.1    Jaros, E.2
  • 88
    • 0033045138 scopus 로고    scopus 로고
    • T1 and T2 in the brain of healthy subjects, patients with Parkinson disease, and patients with multiple system atrophy: Relation to iron content
    • Vymazal J, Righini A, Brooks RA, Canesi M, Mariani C, Leonardi M, Pezzoli G: T1 and T2 in the brain of healthy subjects, patients with Parkinson disease, and patients with multiple system atrophy: Relation to iron content. Radiology 1999;211:489-495.
    • (1999) Radiology , vol.211 , pp. 489-495
    • Vymazal, J.1    Righini, A.2    Brooks, R.A.3    Canesi, M.4    Mariani, C.5    Leonardi, M.6    Pezzoli, G.7
  • 92
  • 93
    • 0033546644 scopus 로고    scopus 로고
    • Hereditary ceruloplasmin deficiency increases advanced glycation end products in the brain
    • Tajima K, Kawanami T, Nagai R, Horiuchi S, Kato T: Hereditary ceruloplasmin deficiency increases advanced glycation end products in the brain. Neurology 1999;53:619-622.
    • (1999) Neurology , vol.53 , pp. 619-622
    • Tajima, K.1    Kawanami, T.2    Nagai, R.3    Horiuchi, S.4    Kato, T.5
  • 94
    • 0033897735 scopus 로고    scopus 로고
    • Neurodegeneration with brain iron accumulation, type 1 is characterized by alpha-, beta-, and gamma-synuclein neuropathology
    • Galvin JE, Giasson B, Hurtig HI, Lee VM, Trojanowski JQ: Neurodegeneration with brain iron accumulation, type 1 is characterized by alpha-, beta-, and gamma-synuclein neuropathology. Am J Pathol 2000;157:361-368.
    • (2000) Am J Pathol , vol.157 , pp. 361-368
    • Galvin, J.E.1    Giasson, B.2    Hurtig, H.I.3    Lee, V.M.4    Trojanowski, J.Q.5
  • 98
    • 0018165651 scopus 로고
    • Effects of iron deficiency exclusive of anaemia
    • Dallman PR, Beutler E, Finch CA: Effects of iron deficiency exclusive of anaemia. Br J Haematol 1978;40:179-184.
    • (1978) Br J Haematol , vol.40 , pp. 179-184
    • Dallman, P.R.1    Beutler, E.2    Finch, C.A.3
  • 99
    • 0017229624 scopus 로고
    • Iron deficiency and behavior
    • Pollitt E, Leibel RL: Iron deficiency and behavior. J Pediatr 1976;88:372-381.
    • (1976) J Pediatr , vol.88 , pp. 372-381
    • Pollitt, E.1    Leibel, R.L.2
  • 100
    • 0024344866 scopus 로고
    • Iron deficiency anemia: Adverse effects on infant psychomotor development
    • Walter T, De Andraca I, Chadud P, Perales CG: Iron deficiency anemia: Adverse effects on infant psychomotor development. Pediatrics 1989;84:7-17.
    • (1989) Pediatrics , vol.84 , pp. 7-17
    • Walter, T.1    De Andraca, I.2    Chadud, P.3    Perales, C.G.4
  • 101
    • 0024514432 scopus 로고
    • Latent iron deficiency alters gamma-aminobutyric acid and glutamate metabolism in rat brain
    • Shukla A, Agarwal KN, Shukla GS: Latent iron deficiency alters gamma-aminobutyric acid and glutamate metabolism in rat brain. Experientia 1989;45:343-345.
    • (1989) Experientia , vol.45 , pp. 343-345
    • Shukla, A.1    Agarwal, K.N.2    Shukla, G.S.3
  • 102
    • 0024593851 scopus 로고
    • Effect of latent iron deficiency on 5-hydroxytryptamine metabolism in rat brain
    • Shukla A, Agarwal KN, Chansuria JP, Taneja V: Effect of latent iron deficiency on 5-hydroxytryptamine metabolism in rat brain. J Neurochem 1989;52:730-735.
    • (1989) J Neurochem , vol.52 , pp. 730-735
    • Shukla, A.1    Agarwal, K.N.2    Chansuria, J.P.3    Taneja, V.4
  • 103
    • 0014860655 scopus 로고
    • Iron deficiency anemia and papilledema. Rapid resolution with oral iron therapy
    • Stoebner R, Kiser R, Alperin JB: Iron deficiency anemia and papilledema. Rapid resolution with oral iron therapy. Am J Dig Dis 1970;15:919-922.
    • (1970) Am J Dig Dis , vol.15 , pp. 919-922
    • Stoebner, R.1    Kiser, R.2    Alperin, J.B.3
  • 104
    • 0001338002 scopus 로고
    • The effects of iron deficiency
    • Jacobs A, Worwood M (eds). New York, Academic Press
    • Beutler E, Fairbanks V: The effects of iron deficiency; in Jacobs A, Worwood M (eds): Iron in Biochemistry and Medicine II. New York, Academic Press, 1980, pp 393-425.
    • (1980) Iron in Biochemistry and Medicine II , pp. 393-425
    • Beutler, E.1    Fairbanks, V.2
  • 105
    • 0017799101 scopus 로고
    • The effects of therapy on the developmental scores of iron-deficient infants
    • Oski FA, Honig AS: The effects of therapy on the developmental scores of iron-deficient infants. J Pediatr 1978;92:21-25.
    • (1978) J Pediatr , vol.92 , pp. 21-25
    • Oski, F.A.1    Honig, A.S.2
  • 106
    • 0029073154 scopus 로고
    • Brain iron, transferrin and ferritin concentrations are altered in developing iron-deficient rats
    • Chen Q, Connor JR, Beard JL: Brain iron, transferrin and ferritin concentrations are altered in developing iron-deficient rats. J Nutr 1995;125:1529-1535.
    • (1995) J Nutr , vol.125 , pp. 1529-1535
    • Chen, Q.1    Connor, J.R.2    Beard, J.L.3
  • 107
    • 0030001813 scopus 로고    scopus 로고
    • Brain iron and behavior of rats are not normalized by treatment of iron deficiency anemia during early development
    • Felt BT, Lozoff B: Brain iron and behavior of rats are not normalized by treatment of iron deficiency anemia during early development. J Nutr 1996;126:693-701.
    • (1996) J Nutr , vol.126 , pp. 693-701
    • Felt, B.T.1    Lozoff, B.2
  • 108
    • 0033944836 scopus 로고    scopus 로고
    • Perinatal iron deficiency decreases cytochrome c oxidase (CytOx) activity in selected regions of neonatal rat brain
    • de Deungria M, Rao R, Wobken JD, Luciana M, Nelson CA, Georgieff MK: Perinatal iron deficiency decreases cytochrome c oxidase (CytOx) activity in selected regions of neonatal rat brain. Pediatr Res 2000;48:169-176.
    • (2000) Pediatr Res , vol.48 , pp. 169-176
    • De Deungria, M.1    Rao, R.2    Wobken, J.D.3    Luciana, M.4    Nelson, C.A.5    Georgieff, M.K.6
  • 109
    • 0034184526 scopus 로고    scopus 로고
    • Cellular distribution of ferric iron, ferritin, transferrin and divalent metal transporter 1 (DMT 1) in substantia nigra and basal ganglia of normal and beta2 microglobulin deficient mouse brain
    • Moos T, Trinder D, Morgan EH: Cellular distribution of ferric iron, ferritin, transferrin and divalent metal transporter 1 (DMT 1) in substantia nigra and basal ganglia of normal and beta2 microglobulin deficient mouse brain. Cell Mol Biol (Noisy-le-grand) 2000;46:549-561.
    • (2000) Cell Mol Biol (Noisy-le-grand) , vol.46 , pp. 549-561
    • Moos, T.1    Trinder, D.2    Morgan, E.H.3
  • 110
    • 0034102395 scopus 로고    scopus 로고
    • Abnormalities in CSF concentrations of ferritin and transferrin in restless legs syndrome
    • Earley CJ, Connor JR, Beard JL, Malecki EA, Epstein DK, Allen RP: Abnormalities in CSF concentrations of ferritin and transferrin in restless legs syndrome. Neurology 2000;54:1698-1700.
    • (2000) Neurology , vol.54 , pp. 1698-1700
    • Earley, C.J.1    Connor, J.R.2    Beard, J.L.3    Malecki, E.A.4    Epstein, D.K.5    Allen, R.P.6
  • 111
    • 0035936633 scopus 로고    scopus 로고
    • MRI measurement of brain iron in patients with restless legs syndrome
    • Allen RP, Barker PB, Wehrl F, Song HK, Earley CJ: MRI measurement of brain iron in patients with restless legs syndrome. Neurology 2001;56:263-265.
    • (2001) Neurology , vol.56 , pp. 263-265
    • Allen, R.P.1    Barker, P.B.2    Wehrl, F.3    Song, H.K.4    Earley, C.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.