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Volumn 63, Issue 4, 2004, Pages 363-380

Intracellular Ferritin Accumulation in Neural and Extraneural Tissue Characterizes A Neurodegenerative Disease Associated with A Mutation in the Ferritin Light Polypeptide Gene

Author keywords

Ataxia; Dementia; Extrapyramidal signs; Ferritin; Iron; Neurodegeneration; Tremor

Indexed keywords

FERRITIN;

EID: 12144288949     PISSN: 00223069     EISSN: None     Source Type: Journal    
DOI: 10.1093/jnen/63.4.363     Document Type: Article
Times cited : (144)

References (43)
  • 1
    • 0030608152 scopus 로고    scopus 로고
    • The ferritins: Molecular properties, iron storage function and cellular regulation
    • Harrison PM, Arosio P. The ferritins: Molecular properties, iron storage function and cellular regulation. Biochim Biophys Acta 1996;1275:161-203
    • (1996) Biochim Biophys Acta , vol.1275 , pp. 161-203
    • Harrison, P.M.1    Arosio, P.2
  • 2
    • 0022199982 scopus 로고
    • Structural and functional relationships of human ferritin H and L chains deduced from cDNA clones
    • Boyd D, Vecoli C, Belcher DM, Jain SK, Drysdale JW. Structural and functional relationships of human ferritin H and L chains deduced from cDNA clones. J Biol Chem 1985;260:11755-61
    • (1985) J Biol Chem , vol.260 , pp. 11755-11761
    • Boyd, D.1    Vecoli, C.2    Belcher, D.M.3    Jain, S.K.4    Drysdale, J.W.5
  • 4
    • 0034964604 scopus 로고    scopus 로고
    • A mutation in the iron-responsive element of H ferritin mRNA, causing autosomal dominant iron overload
    • Kato J, Fujikawa K, Kanda M, et al. A mutation in the iron-responsive element of H ferritin mRNA, causing autosomal dominant iron overload. Am J Hum Genet 2001;69:191-97
    • (2001) Am J Hum Genet , vol.69 , pp. 191-197
    • Kato, J.1    Fujikawa, K.2    Kanda, M.3
  • 5
    • 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 2001;28:350-54
    • (2001) Nat Genet , vol.28 , pp. 350-354
    • Curtis, A.R.1    Fey, C.2    Morris, C.M.3
  • 6
    • 1842562623 scopus 로고    scopus 로고
    • A neurodegenerative disease with intranuclear deposits: Clinical and neuropathologic studies
    • Delisle MB, Uro-Coste E, Rascol O, et al. A neurodegenerative disease with intranuclear deposits: Clinical and neuropathologic studies [Abstract]. J Neuropathol Exp Neurol 2001;60:514
    • (2001) J Neuropathol Exp Neurol , vol.60 , pp. 514
    • Delisle, M.B.1    Uro-Coste, E.2    Rascol, O.3
  • 7
    • 1842457990 scopus 로고    scopus 로고
    • A neurodegenerative disease with intranuclear protein deposits: Electron microscopic and biochemical studies
    • Vidal R, Benson MD, Liepnieks JM, et al. A neurodegenerative disease with intranuclear protein deposits: Electron microscopic and biochemical studies [Abstract]. J Neuropathol Exp Neurol 2001;60:515
    • (2001) J Neuropathol Exp Neurol , vol.60 , pp. 515
    • Vidal, R.1    Benson, M.D.2    Liepnieks, J.M.3
  • 9
    • 0034528319 scopus 로고    scopus 로고
    • Neuroserpin mutation S52R causes neuroserpin accumulation in neurons and is associated with progressive myoclonus epilepsy
    • Takao M, Benson MD, Murrell JR, et al. Neuroserpin mutation S52R causes neuroserpin accumulation in neurons and is associated with progressive myoclonus epilepsy. J Neuropathol Exp Neurol 2000;59:1070-86
    • (2000) J Neuropathol Exp Neurol , vol.59 , pp. 1070-1086
    • Takao, M.1    Benson, M.D.2    Murrell, J.R.3
  • 10
    • 0034712749 scopus 로고    scopus 로고
    • A decamer duplication in the 3′ region of the BRI gene originates an amyloid peptide that is associated with dementia in a Danish kindred
    • Vidal R, Revesz T, Rostagno A, et al. A decamer duplication in the 3′ region of the BRI gene originates an amyloid peptide that is associated with dementia in a Danish kindred. Proc Natl Acad Sci U S A 2000;97:4920-25
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 4920-4925
    • Vidal, R.1    Revesz, T.2    Rostagno, A.3
  • 11
    • 0031452755 scopus 로고    scopus 로고
    • Neuroserpin, a brain-associated inhibitor of tissue plasminogen activator is localized primarily in neurons. Implications for the regulation of motor learning and neuronal survival
    • Hastings GA, Coleman TA, Haudenschild CC, et al. Neuroserpin, a brain-associated inhibitor of tissue plasminogen activator is localized primarily in neurons. Implications for the regulation of motor learning and neuronal survival. J Biol Chem 1997;272:33062-67
    • (1997) J Biol Chem , vol.272 , pp. 33062-33067
    • Hastings, G.A.1    Coleman, T.A.2    Haudenschild, C.C.3
  • 13
    • 0034213595 scopus 로고    scopus 로고
    • ProFound: An expert system for protein identification using mass spectrometric peptide mapping information
    • Zhang W, Chait BT. ProFound: An expert system for protein identification using mass spectrometric peptide mapping information. Anal Chem 2000;72:2482-89
    • (2000) Anal Chem , vol.72 , pp. 2482-2489
    • Zhang, W.1    Chait, B.T.2
  • 15
    • 0034663597 scopus 로고    scopus 로고
    • Application of enhanced multiple sequence alignment profiles to improve protein secondary structure prediction
    • Cuff JA, Barton GJ. Application of enhanced multiple sequence alignment profiles to improve protein secondary structure prediction. Proteins 1999;40:502-11
    • (1999) Proteins , vol.40 , pp. 502-511
    • Cuff, J.A.1    Barton, G.J.2
  • 16
    • 0018110116 scopus 로고
    • Prediction of the secondary structure of proteins from their amino acid sequence
    • Chou PY, Fasman GD. Prediction of the secondary structure of proteins from their amino acid sequence. Adv Enzymol Relat Areas Mol Biol 1978;47:45-148
    • (1978) Adv Enzymol Relat Areas Mol Biol , vol.47 , pp. 45-148
    • Chou, P.Y.1    Fasman, G.D.2
  • 18
    • 0026455697 scopus 로고
    • Ferritin and hemosiderin in pathological tissues
    • Iancu TC. Ferritin and hemosiderin in pathological tissues. Electron Microsc Rev 1992;5:209-29
    • (1992) Electron Microsc Rev , vol.5 , pp. 209-229
    • Iancu, T.C.1
  • 21
    • 0031547971 scopus 로고    scopus 로고
    • Comparison of the three-dimensional structures of recombinant human H and horse L ferritins at high resolution
    • Hempstead PD, Yewdall SJ, Fernie AR, et al. Comparison of the three-dimensional structures of recombinant human H and horse L ferritins at high resolution. J Mol Biol 1997;268:424-48
    • (1997) J Mol Biol , vol.268 , pp. 424-448
    • Hempstead, P.D.1    Yewdall, S.J.2    Fernie, A.R.3
  • 23
    • 0026700576 scopus 로고
    • Loop mutations can cause a substantial conformational change in the carboxy terminus of the ferritin protein
    • Jappelli R, Luzzago A, Tataseo P, Pernice I, Cesareni G. Loop mutations can cause a substantial conformational change in the carboxy terminus of the ferritin protein. J Mol Biol 1992;227:532-43
    • (1992) J Mol Biol , vol.227 , pp. 532-543
    • Jappelli, R.1    Luzzago, A.2    Tataseo, P.3    Pernice, I.4    Cesareni, G.5
  • 24
    • 0032544542 scopus 로고    scopus 로고
    • Cooperativity of mutational effects within a six amino acid residues substitution that induces a major conformational change in human H ferritin
    • Jappelli R, Cesareni G. Cooperativity of mutational effects within a six amino acid residues substitution that induces a major conformational change in human H ferritin. Biochem Biophys Res Commun 1998;250:342-46
    • (1998) Biochem Biophys Res Commun , vol.250 , pp. 342-346
    • Jappelli, R.1    Cesareni, G.2
  • 25
    • 0037092516 scopus 로고    scopus 로고
    • Regulation, mechanisms and proposed function of ferritin translocation to cell nuclei
    • Thompson KJ, Fried MG, Ye Z, Boyer P, Connor JR. Regulation, mechanisms and proposed function of ferritin translocation to cell nuclei. J Cell Sci 2002;115:2165-77
    • (2002) J Cell Sci , vol.115 , pp. 2165-2177
    • Thompson, K.J.1    Fried, M.G.2    Ye, Z.3    Boyer, P.4    Connor, J.R.5
  • 26
    • 0030992780 scopus 로고    scopus 로고
    • Ferritin is a developmentally regulated nuclear protein of avian corneal epithelial cells
    • Cai CX, Birk DE, Linsenmayer TF. Ferritin is a developmentally regulated nuclear protein of avian corneal epithelial cells. J Biol Chem 1997;272:12831-39
    • (1997) J Biol Chem , vol.272 , pp. 12831-12839
    • Cai, C.X.1    Birk, D.E.2    Linsenmayer, T.F.3
  • 27
    • 0034935874 scopus 로고    scopus 로고
    • Nuclear translocation of ferritin in corneal epithelial cells
    • Cai CX, Linsenmayer TF. Nuclear translocation of ferritin in corneal epithelial cells. J Cell Sci 2001;114:2327-34
    • (2001) J Cell Sci , vol.114 , pp. 2327-2334
    • Cai, C.X.1    Linsenmayer, T.F.2
  • 28
    • 1842269298 scopus 로고
    • Intranuclear ferritin
    • Ladda R. Intranuclear ferritin. Exp Cell Res 1962;28:595-97
    • (1962) Exp Cell Res , vol.28 , pp. 595-597
    • Ladda, R.1
  • 29
    • 1842614582 scopus 로고
    • The transport and distribution of colloidal iron and its relation to the ultrastructure of the cell
    • Moore RD, Mumaw YR, Schoenberg MD. The transport and distribution of colloidal iron and its relation to the ultrastructure of the cell. J Ultrastruct Res 1961;5:244-56
    • (1961) J Ultrastruct Res , vol.5 , pp. 244-256
    • Moore, R.D.1    Mumaw, Y.R.2    Schoenberg, M.D.3
  • 30
    • 0031743986 scopus 로고    scopus 로고
    • Intranuclear iron deposition in hepatocytes and renal tubular cells in mice treated with ferric nitrilotriacetate
    • Kondo A, Deguchi J, Okada S. Intranuclear iron deposition in hepatocytes and renal tubular cells in mice treated with ferric nitrilotriacetate. Virchows Arch 1998;433:543-48
    • (1998) Virchows Arch , vol.433 , pp. 543-548
    • Kondo, A.1    Deguchi, J.2    Okada, S.3
  • 31
    • 78651118305 scopus 로고
    • On the carcinogenicity of an iron dextran complex
    • Haddow A, Horning ES. On the carcinogenicity of an iron dextran complex. J Natl Cancer Inst 1960;24:109-47
    • (1960) J Natl Cancer Inst , vol.24 , pp. 109-147
    • Haddow, A.1    Horning, E.S.2
  • 32
    • 0000927208 scopus 로고
    • Intranuclear aggregates of ferritin in liver cells of mice treated with saccharated iron oxide
    • Goetz W, Richter MD. Intranuclear aggregates of ferritin in liver cells of mice treated with saccharated iron oxide. J. Biophysic Biochem Cytol 1961;9:263-70
    • (1961) J Biophysic Biochem Cytol , vol.9 , pp. 263-270
    • Goetz, W.1    Richter, M.D.2
  • 33
    • 0025668709 scopus 로고
    • Characterization and accumulation of ferritin in hepatocyte nuclei of mice with iron overload
    • Smith AG, Carthew P, Francis JE, Edwards RE, Dinsdale D. Characterization and accumulation of ferritin in hepatocyte nuclei of mice with iron overload. Hepatology 1990;12:1399-405
    • (1990) Hepatology , vol.12 , pp. 1399-1405
    • Smith, A.G.1    Carthew, P.2    Francis, J.E.3    Edwards, R.E.4    Dinsdale, D.5
  • 35
    • 0032900602 scopus 로고    scopus 로고
    • The identification of ferritin in the nucleus of K562 cells, and investigation of a possible role in the transcriptional regulation of adult beta-globin gene expression
    • Pountney D, Trugnan G, Bourgeois M, Beaumont C. The identification of ferritin in the nucleus of K562 cells, and investigation of a possible role in the transcriptional regulation of adult beta-globin gene expression. J Cell Sci 1999;112:825-31
    • (1999) J Cell Sci , vol.112 , pp. 825-831
    • Pountney, D.1    Trugnan, G.2    Bourgeois, M.3    Beaumont, C.4
  • 37
    • 0041952925 scopus 로고    scopus 로고
    • Neuroferritinopathy: A window on the role of iron in neurodegeneration
    • Crompton DE, Chinnery PF, Fey C, et al. Neuroferritinopathy: A window on the role of iron in neurodegeneration. Blood Cells Mol Dis 2002;29:522-31
    • (2002) Blood Cells Mol Dis , vol.29 , pp. 522-531
    • Crompton, D.E.1    Chinnery, P.F.2    Fey, C.3
  • 38
    • 0043280850 scopus 로고    scopus 로고
    • Neuroferritinopathy in a French family with late onset dominant dystonia
    • Chinnery PF, Curtis AR, Fey C, et al. Neuroferritinopathy in a French family with late onset dominant dystonia. J Med Genet 2003;40:e69
    • (2003) J Med Genet , vol.40
    • Chinnery, P.F.1    Curtis, A.R.2    Fey, C.3
  • 39
    • 0037413484 scopus 로고    scopus 로고
    • Genetic, clinical, and radiographic delineation of Hallervorden-Spatz syndrome
    • Hayflick SJ, Westaway SK, Levinson B, et al. Genetic, clinical, and radiographic delineation of Hallervorden-Spatz syndrome. N Engl J Med 2003;348:33-40
    • (2003) N Engl J Med , vol.348 , pp. 33-40
    • Hayflick, S.J.1    Westaway, S.K.2    Levinson, B.3
  • 40
    • 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-977S
    • (1998) Am J Clin Nutr , vol.67
    • Harris, Z.L.1    Klomp, L.W.2    Gitlin, J.D.3
  • 42
    • 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;100:2246-68
    • (2002) Blood , vol.100 , pp. 2246-2268
    • Bosio, S.1    De Gobbi, M.2    Roetto, A.3
  • 43
    • 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, Cooperman 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;27:209-14
    • (2001) Nat Genet , vol.27 , pp. 209-214
    • LaVaute, T.1    Smith, S.2    Cooperman, S.3


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