메뉴 건너뛰기




Volumn 28, Issue 5, 2008, Pages 466-471

Redox active iron accumulation in aceruloplasminemia

Author keywords

Aceruloplasminemia; Ceruloplasmin; Iron; Oxidative stress

Indexed keywords

IRON;

EID: 49749087615     PISSN: 09196544     EISSN: 14401789     Source Type: Journal    
DOI: 10.1111/j.1440-1789.2008.00901.x     Document Type: Article
Times cited : (41)

References (39)
  • 1
    • 0031981976 scopus 로고    scopus 로고
    • Aceruloplasminemia: An inherited neurodegenerative disease with impairment of iron homeostasis
    • Harris ZL, Klomp LW, Gitlin JD. Aceruloplasminemia: an inherited neurodegenerative disease with impairment of iron homeostasis. Am J Clin Nutr 1998 67 : 972S 77S.
    • (1998) Am J Clin Nutr , vol.67
    • Harris, Z.L.1    Klomp, L.W.2    Gitlin, J.D.3
  • 2
    • 0346847502 scopus 로고    scopus 로고
    • Aceruloplasminemia, an iron metabolic disorder
    • Miyajima H. Aceruloplasminemia, an iron metabolic disorder. Neuropathology 2003 23 : 345 350.
    • (2003) Neuropathology , vol.23 , pp. 345-350
    • Miyajima, H.1
  • 4
    • 1842504248 scopus 로고    scopus 로고
    • Aceruloplasminemia: An inherited neurodegenerative disease with impairment of iron homeostasis
    • Xu X, Pin S, Gathinji M, Fuchs R, Harris ZL. Aceruloplasminemia: an inherited neurodegenerative disease with impairment of iron homeostasis. Ann N Y Acad Sci 2004 1012 : 299 305.
    • (2004) Ann N Y Acad Sci , vol.1012 , pp. 299-305
    • Xu, X.1    Pin, S.2    Gathinji, M.3    Fuchs, R.4    Harris, Z.L.5
  • 5
    • 0036212028 scopus 로고    scopus 로고
    • Glucose and oxygen hypometabolism in aceruloplasminemia brains
    • Miyajima H, Takahashi Y, Kono S et al. Glucose and oxygen hypometabolism in aceruloplasminemia brains. Intern Med 2002 41 : 186 190.
    • (2002) Intern Med , vol.41 , pp. 186-190
    • Miyajima, H.1    Takahashi, Y.2    Kono, S.3
  • 6
    • 33644944155 scopus 로고    scopus 로고
    • Iron overload and antioxidative role of perivascular astrocytes in aceruloplasminemia
    • Oide T, Yoshida K, Kaneko K, Ohta M, Arima K. Iron overload and antioxidative role of perivascular astrocytes in aceruloplasminemia. Neuropathol Appl Neurobiol 2006 32 : 170 176.
    • (2006) Neuropathol Appl Neurobiol , vol.32 , pp. 170-176
    • Oide, T.1    Yoshida, K.2    Kaneko, K.3    Ohta, M.4    Arima, K.5
  • 8
    • 0026466060 scopus 로고
    • [a case of ceruloplasmin deficiency which showed dementia, ataxia and iron deposition in the brain]
    • Morita H, Inoue A, Yanagisawa N. [A case of ceruloplasmin deficiency which showed dementia, ataxia and iron deposition in the brain]. Rinsho Shinkeigaku 1992 32 : 483 487.
    • (1992) Rinsho Shinkeigaku , vol.32 , pp. 483-487
    • Morita, H.1    Inoue, A.2    Yanagisawa, N.3
  • 11
    • 0036522005 scopus 로고    scopus 로고
    • Glial fibrillary acidic protein is greatly modified by oxidative stress in aceruloplasminemia brain
    • Kaneko K, Nakamura A, Yoshida K, Kametani F, Higuchi K, Ikeda S. Glial fibrillary acidic protein is greatly modified by oxidative stress in aceruloplasminemia brain. Free Radic Res 2002 36 : 303 306.
    • (2002) Free Radic Res , vol.36 , pp. 303-306
    • Kaneko, K.1    Nakamura, A.2    Yoshida, K.3    Kametani, F.4    Higuchi, K.5    Ikeda, S.6
  • 12
    • 3042838351 scopus 로고    scopus 로고
    • Contribution of redox-active iron and copper to oxidative damage in Alzheimer disease
    • Castellani RJ, Honda K, Zhu X et al. Contribution of redox-active iron and copper to oxidative damage in Alzheimer disease. Ageing Res Rev 2004 3 : 319 326.
    • (2004) Ageing Res Rev , vol.3 , pp. 319-326
    • Castellani, R.J.1    Honda, K.2    Zhu, X.3
  • 14
    • 26444549058 scopus 로고    scopus 로고
    • Redox metals and oxidative abnormalities in human prion diseases
    • Petersen RB, Siedlak SL, Lee HG et al. Redox metals and oxidative abnormalities in human prion diseases. Acta Neuropathol (Berl) 2005 110 : 232 238.
    • (2005) Acta Neuropathol (Berl) , vol.110 , pp. 232-238
    • Petersen, R.B.1    Siedlak, S.L.2    Lee, H.G.3
  • 15
    • 0023706899 scopus 로고
    • Amyloid precursor protein in senile plaques of Alzheimer disease
    • Perry G, Lipphardt S, Mulvihill P et al. Amyloid precursor protein in senile plaques of Alzheimer disease. Lancet 1988 2 : 746.
    • (1988) Lancet , vol.2 , pp. 746
    • Perry, G.1    Lipphardt, S.2    Mulvihill, P.3
  • 16
    • 0031981072 scopus 로고    scopus 로고
    • Amyloid-beta deposition in Alzheimer transgenic mice is associated with oxidative stress
    • Smith MA, Hirai K, Hsiao K et al. Amyloid-beta deposition in Alzheimer transgenic mice is associated with oxidative stress. J Neurochem 1998 70 : 2212 2215.
    • (1998) J Neurochem , vol.70 , pp. 2212-2215
    • Smith, M.A.1    Hirai, K.2    Hsiao, K.3
  • 17
    • 0022459980 scopus 로고
    • The unlabeled antibody method: Comparison of peroxidase-antiperoxidase with avidin-biotin complex by a new method of quantification
    • Sternberger LA, Sternberger NH. The unlabeled antibody method: comparison of peroxidase-antiperoxidase with avidin-biotin complex by a new method of quantification. J Histochem Cytochem 1986 34 : 599 605.
    • (1986) J Histochem Cytochem , vol.34 , pp. 599-605
    • Sternberger, L.A.1    Sternberger, N.H.2
  • 18
    • 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
  • 19
    • 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
  • 20
    • 0023240051 scopus 로고
    • Familial apoceruloplasmin deficiency associated with blepharospasm and retinal degeneration
    • Miyajima H, Nishimura Y, Mizoguchi K, Sakamoto M, Shimizu T, Honda N. Familial apoceruloplasmin deficiency associated with blepharospasm and retinal degeneration. Neurology 1987 37 : 761 767.
    • (1987) Neurology , vol.37 , pp. 761-767
    • Miyajima, H.1    Nishimura, Y.2    Mizoguchi, K.3    Sakamoto, M.4    Shimizu, T.5    Honda, N.6
  • 21
    • 0037059741 scopus 로고    scopus 로고
    • Biochemical analysis of a missense mutation in aceruloplasminemia
    • Hellman NE, Kono S, Miyajima H, Gitlin JD. Biochemical analysis of a missense mutation in aceruloplasminemia. J Biol Chem 2002 277 : 1375 1380.
    • (2002) J Biol Chem , vol.277 , pp. 1375-1380
    • Hellman, N.E.1    Kono, S.2    Miyajima, H.3    Gitlin, J.D.4
  • 25
    • 0037105376 scopus 로고    scopus 로고
    • Anemia and iron overload due to compound heterozygosity for novel ceruloplasmin mutations
    • Bosio S, De Gobbi M, Roetto A et al. Anemia and iron overload due to compound heterozygosity for novel ceruloplasmin mutations. Blood 2002 100 : 2246 2248.
    • (2002) Blood , vol.100 , pp. 2246-2248
    • Bosio, S.1    De Gobbi, M.2    Roetto, A.3
  • 26
    • 4644293303 scopus 로고    scopus 로고
    • Disruption of ceruloplasmin and hephaestin in mice causes retinal iron overload and retinal degeneration with features of age-related macular degeneration
    • Hahn P, Qian Y, Dentchev T et al. Disruption of ceruloplasmin and hephaestin in mice causes retinal iron overload and retinal degeneration with features of age-related macular degeneration. Proc Natl Acad Sci USA 2004 101 : 13850 13855.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 13850-13855
    • Hahn, P.1    Qian, Y.2    Dentchev, T.3
  • 27
    • 0041670918 scopus 로고    scopus 로고
    • Aceruloplasminemia with juvenile-onset diabetes mellitus caused by exon skipping in the ceruloplasmin gene
    • Hatanaka Y, Okano T, Oda K, Yamamoto K, Yoshida K. Aceruloplasminemia with juvenile-onset diabetes mellitus caused by exon skipping in the ceruloplasmin gene. Intern Med 2003 42 : 599 604.
    • (2003) Intern Med , vol.42 , pp. 599-604
    • Hatanaka, Y.1    Okano, T.2    Oda, K.3    Yamamoto, K.4    Yoshida, K.5
  • 28
    • 0030027565 scopus 로고    scopus 로고
    • Characterization of a nonsense mutation in the ceruloplasmin gene resulting in diabetes and neurodegenerative disease
    • Takahashi Y, Miyajima H, Shirabe S, Nagataki S, Suenaga A, Gitlin JD. Characterization of a nonsense mutation in the ceruloplasmin gene resulting in diabetes and neurodegenerative disease. Hum Mol Genet 1996 5 : 81 84.
    • (1996) Hum Mol Genet , vol.5 , pp. 81-84
    • Takahashi, Y.1    Miyajima, H.2    Shirabe, S.3    Nagataki, S.4    Suenaga, A.5    Gitlin, J.D.6
  • 29
    • 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 1997 272 : 20185 20190.
    • (1997) J Biol Chem , vol.272 , pp. 20185-20190
    • Patel, B.N.1    David, S.2
  • 30
    • 0031964341 scopus 로고    scopus 로고
    • Expression of ceruloplasmin in the retina: Induction after optic nerve crush
    • Levin LA, Geszvain KM. Expression of ceruloplasmin in the retina: induction after optic nerve crush. Invest Ophthalmol Vis Sci 1998 39 : 157 163.
    • (1998) Invest Ophthalmol Vis Sci , vol.39 , pp. 157-163
    • Levin, L.A.1    Geszvain, K.M.2
  • 31
    • 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 1991 266 : 5128 5134.
    • (1991) J Biol Chem , vol.266 , pp. 5128-5134
    • Sato, M.1    Gitlin, J.D.2
  • 32
    • 0026521529 scopus 로고
    • Mechanisms of caeruloplasmin biosynthesis in normal and copper-deficient rats
    • Gitlin JD, Schroeder JJ, Lee-Ambrose LM, Cousins RJ. Mechanisms of caeruloplasmin biosynthesis in normal and copper-deficient rats. Biochem J 1992 282 (3 835 839.
    • (1992) Biochem J , vol.282 , Issue.3 , pp. 835-839
    • Gitlin, J.D.1    Schroeder, J.J.2    Lee-Ambrose, L.M.3    Cousins, R.J.4
  • 33
    • 0034677467 scopus 로고    scopus 로고
    • Positional cloning of zebrafish ferroportin1 identifies a conserved vertebrate iron exporter
    • Donovan A, Brownlie A, Zhou Y 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    Zhou, Y.3
  • 34
    • 0038711587 scopus 로고    scopus 로고
    • Glycosylphosphatidylinositol-anchored ceruloplasmin is required for iron efflux from cells in the central nervous system
    • Jeong SY, David S. Glycosylphosphatidylinositol-anchored ceruloplasmin is required for iron efflux from cells in the central nervous system. J Biol Chem 2003 278 : 27144 27148.
    • (2003) J Biol Chem , vol.278 , pp. 27144-27148
    • Jeong, S.Y.1    David, S.2
  • 35
    • 0025058305 scopus 로고
    • The blue oxidases, ascorbate oxidase, laccase and ceruloplasmin. Modelling and structural relationships
    • Messerschmidt A, Huber R. The blue oxidases, ascorbate oxidase, laccase and ceruloplasmin. Modelling and structural relationships. Eur J Biochem 1990 187 : 341 352.
    • (1990) Eur J Biochem , vol.187 , pp. 341-352
    • Messerschmidt, A.1    Huber, R.2
  • 36
    • 0014691028 scopus 로고
    • Mobilization of liver iron by ferroxidase (ceruloplasmin)
    • Osaki S, Johnson DA. Mobilization of liver iron by ferroxidase (ceruloplasmin). J Biol Chem 1969 244 : 5757 5758.
    • (1969) J Biol Chem , vol.244 , pp. 5757-5758
    • Osaki, S.1    Johnson, D.A.2
  • 37
    • 0017254918 scopus 로고
    • Alloxan-induced diabetes-evidence for hydroxyl radical as a cytotoxic intermediate
    • Heikkila RE, Winston B, Cohen G. Alloxan-induced diabetes-evidence for hydroxyl radical as a cytotoxic intermediate. Biochem Pharmacol 1976 25 : 1085 1092.
    • (1976) Biochem Pharmacol , vol.25 , pp. 1085-1092
    • Heikkila, R.E.1    Winston, B.2    Cohen, G.3
  • 38
    • 0345860774 scopus 로고    scopus 로고
    • Increased lipid peroxidation and mitochondrial dysfunction in aceruloplasminemia brains
    • Miyajima H, Kono S, Takahashi Y, Sugimoto M. Increased lipid peroxidation and mitochondrial dysfunction in aceruloplasminemia brains. Blood Cells Mol Dis 2002 29 : 433 438.
    • (2002) Blood Cells Mol Dis , vol.29 , pp. 433-438
    • Miyajima, H.1    Kono, S.2    Takahashi, Y.3    Sugimoto, M.4
  • 39
    • 0033006576 scopus 로고    scopus 로고
    • Is increased redox-active iron in Alzheimer disease a failure of the copper-binding protein ceruloplasmin?
    • Castellani RJ, Smith MA, Nunomura A, Harris PL, Perry G. Is increased redox-active iron in Alzheimer disease a failure of the copper-binding protein ceruloplasmin? Free Radic Biol Med 1999 26 : 1508 1512.
    • (1999) Free Radic Biol Med , vol.26 , pp. 1508-1512
    • Castellani, R.J.1    Smith, M.A.2    Nunomura, A.3    Harris, P.L.4    Perry, G.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.