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Volumn 39, Issue 4, 2002, Pages 282-289

The copper-iron connection: Hereditary accruloplasminemia

Author keywords

[No Author keywords available]

Indexed keywords

ACERULOPASMINEMIA; ASTROCYTE; AUTOSOMAL RECESSIVE DISORDER; CERULOPLASMIN BLOOD LEVEL; DEMENTIA; DIABETES MELLITUS; DYSARTHRIA; DYSTONIA; ENZYME ACTIVITY; FERRITIN BLOOD LEVEL; GENE FUNCTION; GENE MUTATION; HUMAN; IRON OVERLOAD; IRON STORAGE; MICROCYTIC ANEMIA; NEUROLOGIC DISEASE; PANCREAS ISLET BETA CELL; PRIORITY JOURNAL; RETINA DEGENERATION; REVIEW; DEGENERATIVE DISEASE; DISORDERS OF METAL METABOLISM; ENZYMOLOGY; FAMILY HEALTH; GENETICS; METABOLISM; MUTATION; PATHOLOGY; PHYSIOLOGY;

EID: 0036800145     PISSN: 00371963     EISSN: None     Source Type: Journal    
DOI: 10.1053/shem.2002.35633     Document Type: Article
Times cited : (72)

References (63)
  • 1
    • 0034733635 scopus 로고    scopus 로고
    • A novel mammalian iron-regulated protein involved in intracellular iron metabolism
    • Abboud S, Haile DJ: A novel mammalian iron-regulated protein involved in intracellular iron metabolism. J Biol Chem 275:19906-19912, 2000
    • (2000) J Biol Chem , vol.275 , pp. 19906-19912
    • Abboud, S.1    Haile, D.J.2
  • 2
    • 0028058038 scopus 로고
    • The FET3 gene of S. cerevisiae encodes a multicopper oxidase required for ferrous iron uptake
    • Askwith C, Eide D, VanHo A, et al: The FET3 gene of S. cerevisiae encodes a multicopper oxidase required for ferrous iron uptake. Cell 76:403-410, 1994
    • (1994) Cell , vol.76 , pp. 403-410
    • Askwith, C.1    Eide, D.2    VanHo, A.3
  • 3
    • 0024564212 scopus 로고
    • Presence of coupled trinuclear copper cluster in mammalian ceruloplasmin is essential for efficient electron transfer to oxygen
    • Calabrese L, Carbonaro M, Musci G: Presence of coupled trinuclear copper cluster in mammalian ceruloplasmin is essential for efficient electron transfer to oxygen. J Biol Chem 264:6183-6187, 1989
    • (1989) J Biol Chem , vol.264 , pp. 6183-6187
    • Calabrese, L.1    Carbonaro, M.2    Musci, G.3
  • 5
    • 0013977884 scopus 로고
    • Factors influencing serum ceruloplasmin levels in normal individuals
    • Cox DW: Factors influencing serum ceruloplasmin levels in normal individuals. J Lab Clin Med 68:893-904, 1966
    • (1966) J Lab Clin Med , vol.68 , pp. 893-904
    • Cox, D.W.1
  • 6
    • 0011938460 scopus 로고
    • Tissue distribution and clearance kinetics of non-transferrin-bound iron in the hypotransferrinemic mouse: A rodent model for hemochromatosis
    • Craven CM, Alexander J, Eldridge 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 84:3457-3461, 1987
    • (1987) Proc Natl Acad Sci , vol.84 , pp. 3457-3461
    • Craven, C.M.1    Alexander, J.2    Eldridge, M.3
  • 7
    • 0034941118 scopus 로고    scopus 로고
    • Mutation in the gene encoding ferritin light polypeptide causes dominant adult-onset basal ganglia disease
    • Curtis AR, Fey C, Morris CM, et al: Mutation in the gene encoding ferritin light polypeptide causes dominant adult-onset basal ganglia disease. Nat Genet 28:350-354, 2001
    • (2001) Nat Genet , vol.28 , pp. 350-354
    • Curtis, A.R.1    Fey, C.2    Morris, C.M.3
  • 9
    • 0029618814 scopus 로고
    • A nonsense mutation of the ceruloplasmin gene in hereditary ceruloplasmin deficiency with diabetes mellitus
    • Daimon M, Kato T, Kawanami T, et al: A nonsense mutation of the ceruloplasmin gene in hereditary ceruloplasmin deficiency with diabetes mellitus. Biochem Biophys Res Commun 217:89-21795, 1995
    • (1995) Biochem Biophys Res Commun , vol.217 , pp. 89-21795
    • Daimon, M.1    Kato, T.2    Kawanami, T.3
  • 10
    • 0032984353 scopus 로고    scopus 로고
    • Hypocaeruloplasminaemia with heteroallelic caeruloplasmin gene mutation: MRI of the brain
    • Daimon M, Moriai S, Susa S, et al: Hypocaeruloplasminaemia with heteroallelic caeruloplasmin gene mutation: MRI of the brain. Neurorad 41:185-187, 1999
    • (1999) Neurorad , vol.41 , pp. 185-187
    • Daimon, M.1    Moriai, S.2    Susa, S.3
  • 11
    • 0034218151 scopus 로고    scopus 로고
    • A novel mutation of the ceruloplasmin gene in a patient with heteroallelic ceruloplasmin gene mutation (HypoCPGM)
    • Daimon M, Susa S, Ohizumi T, et al: A novel mutation of the ceruloplasmin gene in a patient with heteroallelic ceruloplasmin gene mutation (HypoCPGM). Tohoku J Exp Med 191: 119-125, 2000
    • (2000) Tohoku J Exp Med , vol.191 , pp. 119-125
    • Daimon, M.1    Susa, S.2    Ohizumi, T.3
  • 12
    • 0032506116 scopus 로고    scopus 로고
    • Chloride is an allosteric effector of copper assembly for the yeast multicopper oxidase Fet3p: An unexpected role for intracellular chloride channels
    • Davis-Kaplan SR, Askwith CC, Bengtzen AC, et al: Chloride is an allosteric effector of copper assembly for the yeast multicopper oxidase Fet3p: An unexpected role for intracellular chloride channels. Proc Natl Acad Sci USA 95:13641-13645, 1998
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 13641-13645
    • Davis-Kaplan, S.R.1    Askwith, C.C.2    Bengtzen, A.C.3
  • 13
    • 0034677467 scopus 로고    scopus 로고
    • Positional cloning of zebrafish ferroportinl identifies a conserved vertebrate iron exporter
    • Donovan A, Brownlie A, Zhou Y, et al: Positional cloning of zebrafish ferroportinl identifies a conserved vertebrate iron exporter. Nature 403:776-781, 2000
    • (2000) Nature , vol.403 , pp. 776-781
    • Donovan, A.1    Brownlie, A.2    Zhou, Y.3
  • 15
    • 0032881432 scopus 로고    scopus 로고
    • Glycosyl phosphatidylinositol-anchored ceruloplasmin is expressed by rat Sertoli cells and is concentrated in detergent-insoluble membrane fractions
    • Fortna RR, Watson HA, Nyquist SE: Glycosyl phosphatidylinositol-anchored ceruloplasmin is expressed by rat Sertoli cells and is concentrated in detergent-insoluble membrane fractions. Biol Reprod 61:1042-1049, 1999
    • (1999) Biol Reprod , vol.61 , pp. 1042-1049
    • Fortna, R.R.1    Watson, H.A.2    Nyquist, S.E.3
  • 16
    • 0000016319 scopus 로고
    • Turnover of the copper and protein moieties of ceruloplasmin
    • Gitlin D, Janeway CA: Turnover of the copper and protein moieties of ceruloplasmin. Nature 185:693, 1960
    • (1960) Nature , vol.185 , pp. 693
    • Gitlin, D.1    Janeway, C.A.2
  • 17
    • 0014559248 scopus 로고
    • Development of gamma G, gamma A, gamma M, beta 1C, beta 1A, Cl esterase inhibitor, ceruloplasmin, transferrin, hemopexin, haptoglobin, fibrinogen, plasminogen, alpha 1-antritrypsin, orosomucoid, beta-lipoprotein, alpha 2 macroglobulin and prealbumin in the human conceptus
    • Gitlin D, Biasucci A: Development of gamma G, gamma A, gamma M, beta 1C, beta 1A, Cl esterase inhibitor, ceruloplasmin, transferrin, hemopexin, haptoglobin, fibrinogen, plasminogen, alpha 1-antritrypsin, orosomucoid, beta-lipoprotein, alpha 2 macroglobulin and prealbumin in the human conceptus. J Clin Invest 48:1433-1446, 1966
    • (1966) J Clin Invest , vol.48 , pp. 1433-1446
    • Gitlin, D.1    Biasucci, A.2
  • 18
    • 0026521529 scopus 로고
    • Mechanisms of caeruloplasmin biosynthesis in normal and copper-deficient rats
    • Gitlin JD, Schroeder JJ, Lee-Ambrose LM, et al: Mechanisms of caeruloplasmin biosynthesis in normal and copper-deficient rats. Biochem J 282:835-839, 1992
    • (1992) Biochem J , vol.282 , pp. 835-839
    • Gitlin, J.D.1    Schroeder, J.J.2    Lee-Ambrose, L.M.3
  • 19
    • 0028903259 scopus 로고
    • Aceruloplasminemia: Molecular characterization of this disorder of iron metabolism
    • Harris ZL, Takahashi Y, Miyajima H, et al: Aceruloplasminemia: Molecular characterization of this disorder of iron metabolism. Proc Natl Acad Sci USA 92:2539-2543, 1995
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 2539-2543
    • Harris, Z.L.1    Takahashi, Y.2    Miyajima, H.3
  • 20
    • 0030014701 scopus 로고    scopus 로고
    • Familial dementia due to a frameshift mutation in the ceruloplasmin gene
    • Harris ZL, Migas MD, Hughes AE, et al: Familial dementia due to a frameshift mutation in the ceruloplasmin gene. Q J Med 89:355-359, 1996
    • (1996) Q J Med , vol.89 , pp. 355-359
    • Harris, Z.L.1    Migas, M.D.2    Hughes, A.E.3
  • 21
    • 0032875387 scopus 로고    scopus 로고
    • Targeted gene disruption reveals an essential role for ceruloplasmin in cellular iron efflux
    • Harris ZL, Durley AP, Man TK, et al: Targeted gene disruption reveals an essential role for ceruloplasmin in cellular iron efflux. Proc Natl Acad Sci USA 96:10812-10817, 1999
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 10812-10817
    • Harris, Z.L.1    Durley, A.P.2    Man, T.K.3
  • 22
    • 0033665697 scopus 로고    scopus 로고
    • Hepatic iron overload in aceruloplasminaemia
    • Hellman NE, Schaefer M, Gehrke S, et al: Hepatic iron overload in aceruloplasminaemia. Gut 47:858-860, 2000
    • (2000) Gut , vol.47 , pp. 858-860
    • Hellman, N.E.1    Schaefer, M.2    Gehrke, S.3
  • 23
    • 0037059741 scopus 로고    scopus 로고
    • Biochemical analysis of a missense mutation in aceruloplasminemia
    • Hellman NE, Kono S, Miyajima H, et al: Biochemical analysis of a missense mutation in aceruloplasminemia. J Biol Chem 277:1375-1380, 2002
    • (2002) J Biol Chem , vol.277 , pp. 1375-1380
    • Hellman, N.E.1    Kono, S.2    Miyajima, H.3
  • 24
    • 0001036447 scopus 로고
    • Investigations in serum copper. II. Isolation of the copper-containing protein and a description of some of its properties
    • Holmberg CG, Laurell CB: Investigations in serum copper. II. Isolation of the copper-containing protein and a description of some of its properties. Acta Chem Scand 2:550-556, 1948
    • (1948) Acta Chem Scand , vol.2 , pp. 550-556
    • Holmberg, C.G.1    Laurell, C.B.2
  • 25
    • 0014939589 scopus 로고
    • Identification of an apoceruloplasmin-like substance in the plasma of copper-deficient rats
    • Holtzman NA, Gaumnitz BM: Identification of an apoceruloplasmin-like substance in the plasma of copper-deficient rats. J Biol Chem 245:2350-2353, 1970
    • (1970) J Biol Chem , vol.245 , pp. 2350-2353
    • Holtzman, N.A.1    Gaumnitz, B.M.2
  • 26
    • 0014939521 scopus 로고
    • Studies on the rate of release and turnover of ceruloplasmin and apoceruloplasmin in rat plasma
    • Holtzman NA, Gaumnitz BM: Studies on the rate of release and turnover of ceruloplasmin and apoceruloplasmin in rat plasma. J Biol Chem 245:2354-2358, 1970
    • (1970) J Biol Chem , vol.245 , pp. 2354-2358
    • Holtzman, N.A.1    Gaumnitz, B.M.2
  • 27
    • 0030803730 scopus 로고    scopus 로고
    • Biochemical characterization of the Wilson disease protein and functional expression in the yeast Saccharomyces cerevisiae
    • Hung IH, Suzuki M, Yamaguchi Y, et al: Biochemical characterization of the Wilson disease protein and functional expression in the yeast Saccharomyces cerevisiae. J Biol Chem 272:21461-21466, 1997
    • (1997) J Biol Chem , vol.272 , pp. 21461-21466
    • Hung, I.H.1    Suzuki, M.2    Yamaguchi, Y.3
  • 28
    • 0030036172 scopus 로고    scopus 로고
    • Ceruloplasmin gene expression in the murine central nervous system
    • Klomp LWJ, Farhangrazi ZS, Dugan LL, et al: Ceruloplasmin gene expression in the murine central nervous system. J Clin Invest 98:207-215, 1996
    • (1996) J Clin Invest , vol.98 , pp. 207-215
    • Klomp, L.W.J.1    Farhangrazi, Z.S.2    Dugan, L.L.3
  • 29
    • 0029800745 scopus 로고    scopus 로고
    • Expression of the ceruloplasmin gene in the human retina and brain: Implications for a pathogenic model in aceruloplasminemia
    • Klomp LWJ, Gitlin JD: Expression of the ceruloplasmin gene in the human retina and brain: Implications for a pathogenic model in aceruloplasminemia. Hum Mol Genet 5:1989-1996, 1996
    • (1996) Hum Mol Genet , vol.5 , pp. 1989-1996
    • Klomp, L.W.J.1    Gitlin, J.D.2
  • 30
    • 0034081056 scopus 로고    scopus 로고
    • Aceruloplasminemia with a novel mutation associated with parkinsonism
    • Kohno S, Miyajima H, Takahashi Y, et al: Aceruloplasminemia with a novel mutation associated with parkinsonism. Neurogenetics 2:237-248, 2000
    • (2000) Neurogenetics , vol.2 , pp. 237-248
    • Kohno, S.1    Miyajima, H.2    Takahashi, Y.3
  • 31
    • 0023501968 scopus 로고
    • Isolation and characterization of a processed gene for human ceruloplasmin
    • Koschinsky ML, Chow BK-C, Schwartz J, et al: Isolation and characterization of a processed gene for human ceruloplasmin. Biochemistry 26:7760-7767, 1987
    • (1987) Biochemistry , vol.26 , pp. 7760-7767
    • Koschinsky, M.L.1    Chow, B.K.-C.2    Schwartz, J.3
  • 32
    • 0014336133 scopus 로고
    • Iron metabolism in copper-deficient swine
    • Lee GR, Nacht S, Lukens JN, et al: Iron metabolism in copper-deficient swine. J Clin Invest 47:2058-2069, 1968
    • (1968) J Clin Invest , vol.47 , pp. 2058-2069
    • Lee, G.R.1    Nacht, S.2    Lukens, J.N.3
  • 33
    • 0028090209 scopus 로고
    • Hereditary caeruloplasmin deficiency, dementia and diabetes mellitus
    • Logan JL, Harveyson KB, Wisdom GB, et al: Hereditary caeruloplasmin deficiency, dementia and diabetes mellitus. Q J Med 87:663-670, 1994
    • (1994) Q J Med , vol.87 , pp. 663-670
    • Logan, J.L.1    Harveyson, K.B.2    Wisdom, G.B.3
  • 34
    • 0033861745 scopus 로고    scopus 로고
    • A novel duodenal iron-regulated transporter, IREG 1, implicated in the basolateral transfer of iron to the circulation
    • McKie AT, Marciani P, Rolfs A, et al: A novel duodenal iron-regulated transporter, IREG1, implicated in the basolateral transfer of iron to the circulation. Mol Cell 5:299-209, 2000
    • (2000) Mol Cell , vol.5 , pp. 299-209
    • McKie, A.T.1    Marciani, P.2    Rolfs, A.3
  • 35
    • 0035965212 scopus 로고    scopus 로고
    • Copper transport and metabolism are normal in aceruloplasminemic mice
    • Meyer LA, Durley AP, Prohaska JR, et al: Copper transport and metabolism are normal in aceruloplasminemic mice. J Biol Chem 276:36857-36861, 2001
    • (2001) J Biol Chem , vol.276 , pp. 36857-36861
    • Meyer, L.A.1    Durley, A.P.2    Prohaska, J.R.3
  • 36
    • 0023240051 scopus 로고
    • Familial apoceruloplasmin deficiency associated with blepharospasm and retinal degeneration
    • Miyajima H, Nishimura Y, Mizoguchi K, et al: Familial apoceruloplasmin deficiency associated with blepharospasm and retinal degeneration. Neurology 37:761-767, 1987
    • (1987) Neurology , vol.37 , pp. 761-767
    • Miyajima, H.1    Nishimura, Y.2    Mizoguchi, K.3
  • 37
    • 0030003830 scopus 로고    scopus 로고
    • Increased plasma lipid peroxidation in patients with aceruloplasminemia
    • Miyajima H, Takahashi Y, Serizawa M, et al: Increased plasma lipid peroxidation in patients with aceruloplasminemia. Free Radic Biol Med 20:757-760, 1996
    • (1996) Free Radic Biol Med , vol.20 , pp. 757-760
    • Miyajima, H.1    Takahashi, Y.2    Serizawa, M.3
  • 38
    • 0031058837 scopus 로고    scopus 로고
    • Use of desferrioxamine in the treatment of aceruloplasminemia
    • Miyajima H, Takahashi Y, Kamata T, et al: Use of desferrioxamine in the treatment of aceruloplasminemia. Ann Neurol 41:404-407, 1997
    • (1997) Ann Neurol , vol.41 , pp. 404-407
    • Miyajima, H.1    Takahashi, Y.2    Kamata, T.3
  • 39
    • 0031684169 scopus 로고    scopus 로고
    • CSF abnormalities in patients with aceruloplasminemia
    • Miyajima H, Fujimoto M, Kohno S, et al: CSF abnormalities in patients with aceruloplasminemia. Neurology 51:1188-1190, 1998
    • (1998) Neurology , vol.51 , pp. 1188-1190
    • Miyajima, H.1    Fujimoto, M.2    Kohno, S.3
  • 40
    • 0031907553 scopus 로고    scopus 로고
    • Increased very long-chain fatty acids in erythrocyte membranes of patients with aceruloplasminemia
    • Miyajima H, Adachi J, Tatsuno Y, et al: Increased very long-chain fatty acids in erythrocyte membranes of patients with aceruloplasminemia. Neurology 50:130-136, 1998
    • (1998) Neurology , vol.50 , pp. 130-136
    • Miyajima, H.1    Adachi, J.2    Tatsuno, Y.3
  • 41
    • 0033546624 scopus 로고    scopus 로고
    • Estimation of the gene frequency of aceruloplasminemia in Japan
    • Miyajima H, Kohno S, Takahashi Y, et al: Estimation of the gene frequency of aceruloplasminemia in Japan. Neurology 53:617-629, 1999
    • (1999) Neurology , vol.53 , pp. 617-629
    • Miyajima, H.1    Kohno, S.2    Takahashi, Y.3
  • 42
    • 0035956555 scopus 로고    scopus 로고
    • Cerebellar ataxia associated with heteroallelic ceruloplasmin gene mutation
    • Miyajima H, Kono S, Takahashi Y, et al: Cerebellar ataxia associated with heteroallelic ceruloplasmin gene mutation. Neurology 57:2205-2210, 2001
    • (2001) Neurology , vol.57 , pp. 2205-2210
    • Miyajima, H.1    Kono, S.2    Takahashi, Y.3
  • 43
    • 0034891099 scopus 로고    scopus 로고
    • Increased oxysterols associated with iron accumulation in the brains and visceral organs of acaeruloplasminaemia patients
    • Miyajima H, Adachi J, Kohno S, et al: Increased oxysterols associated with iron accumulation in the brains and visceral organs of acaeruloplasminaemia patients, Q J Med 94:417-422, 2001
    • (2001) Q J Med , vol.94 , pp. 417-422
    • Miyajima, H.1    Adachi, J.2    Kohno, S.3
  • 44
    • 17944380796 scopus 로고    scopus 로고
    • Autosomal-dominant hemochromatosis is associated with a mutation in the ferroportin (SLC11A3) gene
    • Montosi G, Donovan A, Totaro A, et al: Autosomal-dominant hemochromatosis is associated with a mutation in the ferroportin (SLC11A3) gene. J Clin Invest 108:619-623, 2001
    • (2001) J Clin Invest , vol.108 , pp. 619-623
    • Montosi, G.1    Donovan, A.2    Totaro, A.3
  • 45
    • 0029007765 scopus 로고
    • Hereditary ceruloplasmin deficiency with hemosiderosis: A clinicopathological study of a Japanese family
    • Morita H, Ikeda S, Yamamoto K, et al: Hereditary ceruloplasmin deficiency with hemosiderosis: A clinicopathological study of a Japanese family. Ann Neurol 37:646-656, 1995
    • (1995) Ann Neurol , vol.37 , pp. 646-656
    • Morita, H.1    Ikeda, S.2    Yamamoto, K.3
  • 46
    • 0034930197 scopus 로고    scopus 로고
    • Mutation in SLC11A3 is associated with autosomal dominant hemochromatosis
    • Njajou OT, Vaessen N, Joosse M, et al: Mutation in SLC11A3 is associated with autosomal dominant hemochromatosis. Nat Genet 28:213-214, 2001
    • (2001) Nat Genet , vol.28 , pp. 213-214
    • Njajou, O.T.1    Vaessen, N.2    Joosse, M.3
  • 47
    • 0029872996 scopus 로고    scopus 로고
    • Hereditary ceruloplasmin deficiency with hemosiderosis
    • Okamoto N, Wada S, Oga T, et al: Hereditary ceruloplasmin deficiency with hemosiderosis. Hum Genet 97:755-758, 1996
    • (1996) Hum Genet , vol.97 , pp. 755-758
    • Okamoto, N.1    Wada, S.2    Oga, T.3
  • 48
    • 0014027719 scopus 로고
    • The possible significance of the ferrous oxidase activity of ceruloplasmin in normal human serum
    • Osaki S, Johnson D, Frieden E: The possible significance of the ferrous oxidase activity of ceruloplasmin in normal human serum. J Biol Chem 241:2746-2757, 1966
    • (1966) J Biol Chem , vol.241 , pp. 2746-2757
    • Osaki, S.1    Johnson, D.2    Frieden, E.3
  • 49
    • 0015217690 scopus 로고
    • The mobilization of iron from the perfused mammalian liver by a serum copper enzyme, ferroxidase
    • Osaki S, Johnson DA, Frieden E: The mobilization of iron from the perfused mammalian liver by a serum copper enzyme, ferroxidase. J Biol Chem 246:3018-3023, 1971
    • (1971) J Biol Chem , vol.246 , pp. 3018-3023
    • Osaki, S.1    Johnson, D.A.2    Frieden, E.3
  • 50
    • 0030856558 scopus 로고    scopus 로고
    • A novel glycosylphosphatidylinositol-anchored form of ceruloplasmin is expressed by mammalian astrocytes
    • Patel BN, David S: A novel glycosylphosphatidylinositol-anchored form of ceruloplasmin is expressed by mammalian astrocytes. J Biol Chem 272:20185-20190, 1997
    • (1997) J Biol Chem , vol.272 , pp. 20185-20190
    • Patel, B.N.1    David, S.2
  • 51
    • 0034635402 scopus 로고    scopus 로고
    • Alternative RNA splicing generates a glycosylphosphatidylinositol-anchored form of ceruloplasmin in mammalian brain
    • Patel BN, Dunn RJ, David S: Alternative RNA splicing generates a glycosylphosphatidylinositol-anchored form of ceruloplasmin in mammalian brain. J Biol Chem 275:4305-4310, 2000
    • (2000) J Biol Chem , vol.275 , pp. 4305-4310
    • Patel, B.N.1    Dunn, R.J.2    David, S.3
  • 52
    • 0014905840 scopus 로고
    • The role of ceruloplasmin in iron metabolism
    • Roeser HP, Lee GR, Nacht S, et al: The role of ceruloplasmin in iron metabolism. J Clin Invest 49:2408-2417, 1970
    • (1970) J Clin Invest , vol.49 , pp. 2408-2417
    • Roeser, H.P.1    Lee, G.R.2    Nacht, S.3
  • 53
    • 0032532332 scopus 로고    scopus 로고
    • Ran-2, a glial lineage marker, is a GPI-anchored form of ceruloplasmin
    • Salzer JL, Lovejoy L, Linder MC, et al: Ran-2, a glial lineage marker, is a GPI-anchored form of ceruloplasmin. J Neurosci Res 54:147-157, 1998
    • (1998) J Neurosci Res , vol.54 , pp. 147-157
    • Salzer, J.L.1    Lovejoy, L.2    Linder, M.C.3
  • 54
    • 0025729544 scopus 로고
    • Mechanisms of copper incorporation during the biosynthesis of human ceruloplasmin
    • Sato M, Gitlin JD: Mechanisms of copper incorporation during the biosynthesis of human ceruloplasmin. J Biol Chem 266:5128-5134, 1991
    • (1991) J Biol Chem , vol.266 , pp. 5128-5134
    • Sato, M.1    Gitlin, J.D.2
  • 55
    • 0032920935 scopus 로고    scopus 로고
    • Hepatocyte-specific localization and copper-dependent trafficking of the Wilson's disease protein in the liver
    • Schaefer M, Hopkins R, Failla M et al: Hepatocyte-specific localization and copper-dependent trafficking of the Wilson's disease protein in the liver. Am J Physiol 276:G639-G646, 1999
    • (1999) Am J Physiol , vol.276
    • Schaefer, M.1    Hopkins, R.2    Failla, M.3
  • 56
    • 0000852301 scopus 로고
    • Deficiency of ceruloplasmin in patients with hepatolenticular degeneration (Wilson's disease)
    • Scheinberg IH, Gitlin D: Deficiency of ceruloplasmin in patients with hepatolenticular degeneration (Wilson's disease). Science 116:484-489, 1952
    • (1952) Science , vol.116 , pp. 484-489
    • Scheinberg, I.H.1    Gitlin, D.2
  • 57
    • 0029921680 scopus 로고    scopus 로고
    • A permeaseoxidase complex involved in high-affinity iron uptake in yeast
    • Stearman R, Yuan DS, Yamaguchi-Iwa Y, et al: A permeaseoxidase complex involved in high-affinity iron uptake in yeast. Science 271:1552-1557, 1996
    • (1996) Science , vol.271 , pp. 1552-1557
    • Stearman, R.1    Yuan, D.S.2    Yamaguchi-Iwa, Y.3
  • 58
    • 0030027565 scopus 로고
    • Characterization of a nonsense mutation in the ceruloplasmin gene resulting in diabetes and neurodegenerative disease
    • Takahashi Y, Miyajima H, Shirabe S, et al: Characterization of a nonsense mutation in the ceruloplasmin gene resulting in diabetes and neurodegenerative disease. Hum Mol Genet 51:81-84, 1995
    • (1995) Hum Mol Genet , vol.51 , pp. 81-84
    • Takahashi, Y.1    Miyajima, H.2    Shirabe, S.3
  • 59
    • 0032909207 scopus 로고    scopus 로고
    • Hephaestin, a ceruloplasmin homologue implicated in intestinal iron transport, is defective in the sla mouse
    • Vulpe CD, Kuo YM, Murphy TL, et al: Hephaestin, a ceruloplasmin homologue implicated in intestinal iron transport, is defective in the sla mouse. Nat Genet 21:195-199, 1999
    • (1999) Nat Genet , vol.21 , pp. 195-199
    • Vulpe, C.D.1    Kuo, Y.M.2    Murphy, T.L.3
  • 60
    • 0032539831 scopus 로고    scopus 로고
    • A novel splicing mutation in the ceruloplasmin gene responsible for hereditary ceruloplasmin deficiency with hemosiderosis
    • Yazaki M, Yoshida K, Nakamura A, et al: A novel splicing mutation in the ceruloplasmin gene responsible for hereditary ceruloplasmin deficiency with hemosiderosis. J Neurol Sci 156:30-34, 1998
    • (1998) J Neurol Sci , vol.156 , pp. 30-34
    • Yazaki, M.1    Yoshida, K.2    Nakamura, A.3
  • 61
    • 0032843885 scopus 로고    scopus 로고
    • A case of hereditary ceruloplasmin deficiency with iron deposition in the brain associated with chorea, dementia, diabetes mellitus and retinal pigmentation: Administration of fresh-frozen human plasma
    • Yonekawa M, Okabe T, Asamoto Y, et al: A case of hereditary ceruloplasmin deficiency with iron deposition in the brain associated with chorea, dementia, diabetes mellitus and retinal pigmentation: administration of fresh-frozen human plasma. Eur Neurol 42:157-162, 1999
    • (1999) Eur Neurol , vol.42 , pp. 157-162
    • Yonekawa, M.1    Okabe, T.2    Asamoto, Y.3
  • 62
    • 0028895749 scopus 로고
    • A mutation in the ceruloplasmin gene is associated with systemic hemosiderosis in humans
    • Yoshida K, Furihata K, Takeda S, et al: A mutation in the ceruloplasmin gene is associated with systemic hemosiderosis in humans. Nat Genet 9:267-272, 1995
    • (1995) Nat Genet , vol.9 , pp. 267-272
    • Yoshida, K.1    Furihata, K.2    Takeda, S.3
  • 63
    • 0034656236 scopus 로고    scopus 로고
    • Increased lipid peroxidation in the brains of aceruloplasminemia patients
    • Yoshida K, Kaneko K, Miyajima H, et al: Increased lipid peroxidation in the brains of aceruloplasminemia patients. J Neurol Sci 175:91-95, 2000
    • (2000) J Neurol Sci , vol.175 , pp. 91-95
    • Yoshida, K.1    Kaneko, K.2    Miyajima, H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.