메뉴 건너뛰기




Volumn 17, Issue 6, 2011, Pages 423-430

Ferritin as an important player in neurodegeneration

Author keywords

Ferritin; Iron; Neurodegeneration; Oxidative stress

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATASE TYPE 13A2; CERULOPLASMIN; FATTY ACID 2 HYDROXYLASE; FERRITIN; FERRITIN H; FERRITIN L; IRON; OXYGENASE; PANTOTHENATE KINASE 2; PHOSPHOLIPASE A2; UNCLASSIFIED DRUG;

EID: 79959523068     PISSN: 13538020     EISSN: 18735126     Source Type: Journal    
DOI: 10.1016/j.parkreldis.2011.03.016     Document Type: Review
Times cited : (118)

References (85)
  • 1
    • 0029869189 scopus 로고    scopus 로고
    • Mechanisms involved in the generation of free radicals
    • Halliwell B. Mechanisms involved in the generation of free radicals. Pathol Biol 1996, 44:6-13.
    • (1996) Pathol Biol , vol.44 , pp. 6-13
    • Halliwell, B.1
  • 3
    • 33745850084 scopus 로고    scopus 로고
    • Peroxyl radicals: inductors of neurodegenerative and other inflammatory diseases. Their origin and how they transform cholesterol, phospholipids, plasmalogens, polyunsaturated fatty acids, sugars, and proteins into deleterious products
    • Spiteller G. Peroxyl radicals: inductors of neurodegenerative and other inflammatory diseases. Their origin and how they transform cholesterol, phospholipids, plasmalogens, polyunsaturated fatty acids, sugars, and proteins into deleterious products. Free Radic Biol Med 2006, 41:362-387.
    • (2006) Free Radic Biol Med , vol.41 , pp. 362-387
    • Spiteller, G.1
  • 4
    • 0030608152 scopus 로고    scopus 로고
    • The ferritins: molecular properties, iron storage function and cellular regulation
    • Harrison P.M., 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
  • 5
    • 67349100157 scopus 로고    scopus 로고
    • Ferritins: a family of molecules for iron storage, antioxidation and more
    • Arosio P., Ingrassia R., Cavadini P. Ferritins: a family of molecules for iron storage, antioxidation and more. Biochim Biophys Acta 2009, 1790:589-599.
    • (2009) Biochim Biophys Acta , vol.1790 , pp. 589-599
    • Arosio, P.1    Ingrassia, R.2    Cavadini, P.3
  • 6
    • 77953809618 scopus 로고
    • The iron redox and hydrolysis chemistry of the ferritins
    • Bou-Abdallah F. The iron redox and hydrolysis chemistry of the ferritins. Biochim Biophys Acta 1800, 2010:719-731.
    • (1800) Biochim Biophys Acta , vol.2010 , pp. 719-731
    • Bou-Abdallah, F.1
  • 8
    • 33644867367 scopus 로고    scopus 로고
    • Iron(II) and hydrogen peroxide detoxification by human H-chain ferritin. An EPR spin-trapping study
    • Zhao G., Bou-Abdallahl F., Yang X., Arosio P., Chasteen D. Iron(II) and hydrogen peroxide detoxification by human H-chain ferritin. An EPR spin-trapping study. Biochemistry 2006, 45:3429-3436.
    • (2006) Biochemistry , vol.45 , pp. 3429-3436
    • Zhao, G.1    Bou-Abdallahl, F.2    Yang, X.3    Arosio, P.4    Chasteen, D.5
  • 9
    • 0027198736 scopus 로고
    • Production and characterization of recombinant heteropolymers of human ferritin H and L chains
    • Santambrogio P., Levi S., Cozzi A., Rovida E., Albertini A., Arosio A. Production and characterization of recombinant heteropolymers of human ferritin H and L chains. J Biol Chem 1993, 268:12744-12748.
    • (1993) J Biol Chem , vol.268 , pp. 12744-12748
    • Santambrogio, P.1    Levi, S.2    Cozzi, A.3    Rovida, E.4    Albertini, A.5    Arosio, A.6
  • 10
    • 45849123222 scopus 로고    scopus 로고
    • A cytosolic iron chaperone that delivers iron to ferritin
    • Shi H., Bencze K.Z., Stemmler T.L., Philpott C.C. A cytosolic iron chaperone that delivers iron to ferritin. Science 2008, 320:1207-1210.
    • (2008) Science , vol.320 , pp. 1207-1210
    • Shi, H.1    Bencze, K.Z.2    Stemmler, T.L.3    Philpott, C.C.4
  • 11
    • 0031605490 scopus 로고    scopus 로고
    • Ferritin. Uptake, storage, and release of iron
    • Chasteen N.D. Ferritin. Uptake, storage, and release of iron. Met Ions Biol Syst 1998, 35:479-514.
    • (1998) Met Ions Biol Syst , vol.35 , pp. 479-514
    • Chasteen, N.D.1
  • 12
    • 0035810653 scopus 로고    scopus 로고
    • Sulfide is an efficient iron releasing agent for mammalian ferritins
    • Cassanelli S., Moulis J. Sulfide is an efficient iron releasing agent for mammalian ferritins. Biochim Biophys Acta 2001, 1547:174-182.
    • (2001) Biochim Biophys Acta , vol.1547 , pp. 174-182
    • Cassanelli, S.1    Moulis, J.2
  • 13
    • 33748370752 scopus 로고    scopus 로고
    • Ferritins: iron/oxygen biominerals in protein nanocages
    • Theil E.C., Matzapetakis M., Liu X. Ferritins: iron/oxygen biominerals in protein nanocages. J Biol Inorg Chem 2006, 11:803-810.
    • (2006) J Biol Inorg Chem , vol.11 , pp. 803-810
    • Theil, E.C.1    Matzapetakis, M.2    Liu, X.3
  • 14
    • 57649121590 scopus 로고    scopus 로고
    • Ferritin contains less iron (59Fe) in cells when the protein pores are unfolded by mutation
    • Hasan M.R., Tosha T., Theil E.C. Ferritin contains less iron (59Fe) in cells when the protein pores are unfolded by mutation. J Biol Chem 2008, 283:31394-31400.
    • (2008) J Biol Chem , vol.283 , pp. 31394-31400
    • Hasan, M.R.1    Tosha, T.2    Theil, E.C.3
  • 15
    • 0035954391 scopus 로고    scopus 로고
    • "Opening" the ferritin pore for iron release by mutation of conserved amino acids at interhelix and loop sites
    • Jin W., Takagi H., Pancorbo B., Theil E.C. "Opening" the ferritin pore for iron release by mutation of conserved amino acids at interhelix and loop sites. Biochemistry 2001, 40:7525-7532.
    • (2001) Biochemistry , vol.40 , pp. 7525-7532
    • Jin, W.1    Takagi, H.2    Pancorbo, B.3    Theil, E.C.4
  • 16
    • 70449519036 scopus 로고    scopus 로고
    • Oxidative stress and cell death in cells expressing L-ferritin variants causing neuroferritinopathy
    • Cozzi A., Rovelli E., Frizzale G., Campanella A., Amendola M., Arosio P., et al. Oxidative stress and cell death in cells expressing L-ferritin variants causing neuroferritinopathy. Neurobiol Dis 2009, 37:77-85.
    • (2009) Neurobiol Dis , vol.37 , pp. 77-85
    • Cozzi, A.1    Rovelli, E.2    Frizzale, G.3    Campanella, A.4    Amendola, M.5    Arosio, P.6
  • 17
    • 33747154110 scopus 로고    scopus 로고
    • Characterization of the l-ferritin variant 460InsA responsible of a hereditary ferritinopathy disorder
    • Cozzi A., Santambrogio P., Corsi B., Campanella A., Arosio P., Levi S. Characterization of the l-ferritin variant 460InsA responsible of a hereditary ferritinopathy disorder. Neurobiol Dis 2006, 23:644-652.
    • (2006) Neurobiol Dis , vol.23 , pp. 644-652
    • Cozzi, A.1    Santambrogio, P.2    Corsi, B.3    Campanella, A.4    Arosio, P.5    Levi, S.6
  • 18
    • 77951249355 scopus 로고    scopus 로고
    • Mutant ferritin L-chains that cause neurodegeneration act in a dominant-negative manner to reduce ferritin iron incorporation
    • Luscieti S., Santambrogio P., Langlois d'Estaintot B., Granier T., Cozzi A., Poli M., et al. Mutant ferritin L-chains that cause neurodegeneration act in a dominant-negative manner to reduce ferritin iron incorporation. J Biol Chem 2010, 285:11948-11957.
    • (2010) J Biol Chem , vol.285 , pp. 11948-11957
    • Luscieti, S.1    Santambrogio, P.2    Langlois d'Estaintot, B.3    Granier, T.4    Cozzi, A.5    Poli, M.6
  • 19
    • 0016287813 scopus 로고
    • Ferritin iron uptake and release. Structure-function relationships
    • Harrison P.M., Hoy T.G., Macara I.G., Hoare R.J. Ferritin iron uptake and release. Structure-function relationships. Biochem J 1974, 143:445-451.
    • (1974) Biochem J , vol.143 , pp. 445-451
    • Harrison, P.M.1    Hoy, T.G.2    Macara, I.G.3    Hoare, R.J.4
  • 20
    • 3843101698 scopus 로고    scopus 로고
    • Neisseria meningitidis accelerates ferritin degradation in host epithelial cells to yield an essential iron source
    • Larson J.A., Howie H.L., So M. Neisseria meningitidis accelerates ferritin degradation in host epithelial cells to yield an essential iron source. Mol Microbiol 2004, 53:807-820.
    • (2004) Mol Microbiol , vol.53 , pp. 807-820
    • Larson, J.A.1    Howie, H.L.2    So, M.3
  • 22
    • 10644232372 scopus 로고    scopus 로고
    • Oxidation-induced ferritin turnover in microglial cells: role of proteasome
    • Mehlhase J., Sandig G., Pantopoulos K., Grune T. Oxidation-induced ferritin turnover in microglial cells: role of proteasome. Free Radic Biol Med 2005, 38:276-285.
    • (2005) Free Radic Biol Med , vol.38 , pp. 276-285
    • Mehlhase, J.1    Sandig, G.2    Pantopoulos, K.3    Grune, T.4
  • 23
    • 33751103909 scopus 로고    scopus 로고
    • Ferroportin-mediated mobilization of ferritin iron precedes ferritin degradation by the proteasome
    • De Domenico I., Vaughn M.B., Li L., Bagley D., Musci G., Ward D.M., et al. Ferroportin-mediated mobilization of ferritin iron precedes ferritin degradation by the proteasome. EMBO J 2006, 25:5396-5404.
    • (2006) EMBO J , vol.25 , pp. 5396-5404
    • De Domenico, I.1    Vaughn, M.B.2    Li, L.3    Bagley, D.4    Musci, G.5    Ward, D.M.6
  • 24
    • 79959512034 scopus 로고    scopus 로고
    • Specific iron chelators determine the route of ferritin degradation
    • De Domenico I., Vaughn M.B., Li L., Bagley D., Musci G., Ward D.M., et al. Specific iron chelators determine the route of ferritin degradation. Blood 2009, 25:5396-5404.
    • (2009) Blood , vol.25 , pp. 5396-5404
    • De Domenico, I.1    Vaughn, M.B.2    Li, L.3    Bagley, D.4    Musci, G.5    Ward, D.M.6
  • 28
    • 0037151089 scopus 로고    scopus 로고
    • Human mitochondrial ferritin expressed in HeLa cells incorporates iron and affects cellular iron metabolism
    • Corsi B., Cozzi A., Arosio P., Drysdale J., Santambrogio P., Campanella A., et al. Human mitochondrial ferritin expressed in HeLa cells incorporates iron and affects cellular iron metabolism. J Biol Chem 2002, 277:22430-22437.
    • (2002) J Biol Chem , vol.277 , pp. 22430-22437
    • Corsi, B.1    Cozzi, A.2    Arosio, P.3    Drysdale, J.4    Santambrogio, P.5    Campanella, A.6
  • 31
    • 0037372442 scopus 로고    scopus 로고
    • Mitochondrial ferritin expression in erythroid cells from patients with sideroblastic anemia
    • Cazzola M., Invernizzi R., Bergamaschi G., Levi S., Corsi B., Travaglino E., et al. Mitochondrial ferritin expression in erythroid cells from patients with sideroblastic anemia. Blood 2003, 101:1996-2000.
    • (2003) Blood , vol.101 , pp. 1996-2000
    • Cazzola, M.1    Invernizzi, R.2    Bergamaschi, G.3    Levi, S.4    Corsi, B.5    Travaglino, E.6
  • 33
    • 78149288408 scopus 로고    scopus 로고
    • Regional and cellular distribution of mitochondrial ferritin in the mouse brain
    • Snyder A.M., Neely E.B., Levi S., Arosio P., Connor J.R. Regional and cellular distribution of mitochondrial ferritin in the mouse brain. J Neurosci Res 2010, 88:3133-3143.
    • (2010) J Neurosci Res , vol.88 , pp. 3133-3143
    • Snyder, A.M.1    Neely, E.B.2    Levi, S.3    Arosio, P.4    Connor, J.R.5
  • 35
    • 14744304889 scopus 로고    scopus 로고
    • Unique iron binding and oxidation properties of human mitochondrial ferritin: a comparative analysis with human H-chain ferritin
    • Bou-Abdallah F., Santambrogio P., Levi S., Arosio P., Chasteen N.D. Unique iron binding and oxidation properties of human mitochondrial ferritin: a comparative analysis with human H-chain ferritin. J Mol Biol 2005, 347:543-554.
    • (2005) J Mol Biol , vol.347 , pp. 543-554
    • Bou-Abdallah, F.1    Santambrogio, P.2    Levi, S.3    Arosio, P.4    Chasteen, N.D.5
  • 36
    • 14944358625 scopus 로고    scopus 로고
    • Overexpression of mitochondrial ferritin causes cytosolic iron depletion and changes cellular iron homeostasis
    • Nie G., Sheftel A.D., Kim S.F., Ponka P. Overexpression of mitochondrial ferritin causes cytosolic iron depletion and changes cellular iron homeostasis. Blood 2005, 105:2161-2167.
    • (2005) Blood , vol.105 , pp. 2161-2167
    • Nie, G.1    Sheftel, A.D.2    Kim, S.F.3    Ponka, P.4
  • 37
    • 5444262935 scopus 로고    scopus 로고
    • The expression of human mitochondrial ferritin rescues respiratory function in frataxin-deficient yeast
    • Campanella A., Isaya G., O'Neill H.A., Santambrogio P., Cozzi A., Arosio P., et al. The expression of human mitochondrial ferritin rescues respiratory function in frataxin-deficient yeast. Hum Mol Genet 2004, 13:2279-2288.
    • (2004) Hum Mol Genet , vol.13 , pp. 2279-2288
    • Campanella, A.1    Isaya, G.2    O'Neill, H.A.3    Santambrogio, P.4    Cozzi, A.5    Arosio, P.6
  • 38
    • 57649243073 scopus 로고    scopus 로고
    • Mitochondrial ferritin limits oxidative damage regulating mitochondrial iron availability: hypothesis for a protective role in Friedreich ataxia
    • Campanella A., Rovelli E., Santambrogio P., Cozzi A., Taroni F., Levi S. Mitochondrial ferritin limits oxidative damage regulating mitochondrial iron availability: hypothesis for a protective role in Friedreich ataxia. Hum Mol Genet 2009, 18:1-11.
    • (2009) Hum Mol Genet , vol.18 , pp. 1-11
    • Campanella, A.1    Rovelli, E.2    Santambrogio, P.3    Cozzi, A.4    Taroni, F.5    Levi, S.6
  • 39
    • 39149096860 scopus 로고    scopus 로고
    • The effects of frataxin silencing in HeLa cells are rescued by the expression of human mitochondrial ferritin
    • Zanella I., Derosas M., Corrado M., Cocco E., Cavadini P., Biasiotto G., et al. The effects of frataxin silencing in HeLa cells are rescued by the expression of human mitochondrial ferritin. Biochim Biophys Acta 2008, 1782:90-98.
    • (2008) Biochim Biophys Acta , vol.1782 , pp. 90-98
    • Zanella, I.1    Derosas, M.2    Corrado, M.3    Cocco, E.4    Cavadini, P.5    Biasiotto, G.6
  • 40
    • 34147165135 scopus 로고    scopus 로고
    • RNA silencing of the mitochondrial ABCB7 transporter in HeLa cells causes an iron-deficient phenotype with mitochondrial iron overload
    • Cavadini P., Biasiotto G., Poli M., Levi S., Verardi R., Zanella I., et al. RNA silencing of the mitochondrial ABCB7 transporter in HeLa cells causes an iron-deficient phenotype with mitochondrial iron overload. Blood 2007, 109:3552-3559.
    • (2007) Blood , vol.109 , pp. 3552-3559
    • Cavadini, P.1    Biasiotto, G.2    Poli, M.3    Levi, S.4    Verardi, R.5    Zanella, I.6
  • 41
    • 77954929704 scopus 로고    scopus 로고
    • Neuroprotective mechanism of mitochondrial ferritin on 6-Hydroxydopamine-induced Dopaminergic cell damage: implication for Neuroprotection in Parkinson's disease
    • Shi Z.H., Nie G., Duan X.L., Rouault T., Wu W.S., Ning B., et al. Neuroprotective mechanism of mitochondrial ferritin on 6-Hydroxydopamine-induced Dopaminergic cell damage: implication for Neuroprotection in Parkinson's disease. Antioxid Redox Signal 2010, 13:783-796.
    • (2010) Antioxid Redox Signal , vol.13 , pp. 783-796
    • Shi, Z.H.1    Nie, G.2    Duan, X.L.3    Rouault, T.4    Wu, W.S.5    Ning, B.6
  • 42
    • 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., Iwai K., Land W., Meyron-Holtz E., 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, 27:209-214.
    • (2001) Nat Genet , vol.27 , pp. 209-214
    • LaVaute, T.1    Smith, S.2    Cooperman, S.3    Iwai, K.4    Land, W.5    Meyron-Holtz, E.6
  • 46
    • 34247151294 scopus 로고    scopus 로고
    • ELISA reveals a difference in the structure of substantia nigra ferritin in Parkinson's disease and Incidental Lewy Body compared to control
    • Koziorowski D., Friedman A., Arosio Santambrogio P., Dziewulska D. ELISA reveals a difference in the structure of substantia nigra ferritin in Parkinson's disease and Incidental Lewy Body compared to control. Parkinsonism Relat Disord 2007, 13:214-218.
    • (2007) Parkinsonism Relat Disord , vol.13 , pp. 214-218
    • Koziorowski, D.1    Friedman, A.2    Arosio Santambrogio, P.3    Dziewulska, D.4
  • 48
    • 33646628395 scopus 로고    scopus 로고
    • Mssbauer spectroscopy, electron microscopy and electron diffraction studies of ferritin-like iron in human heart, liver and brain
    • Galazka-Friedman J., Bauminger E.R., Tymosz T., Friedman A. Mssbauer spectroscopy, electron microscopy and electron diffraction studies of ferritin-like iron in human heart, liver and brain. Hyperfine Interactions (C) 1998, 3:49-52.
    • (1998) Hyperfine Interactions (C) , vol.3 , pp. 49-52
    • Galazka-Friedman, J.1    Bauminger, E.R.2    Tymosz, T.3    Friedman, A.4
  • 49
    • 0023804321 scopus 로고
    • Increased iron (III) and total iron content in post mortem substantia nigra of parkinsonian brain
    • Sofic E., Riederer P., Heinsen H., Beckmann H., Reynolds G.P., Hebenstreit G., et al. Increased iron (III) and total iron content in post mortem substantia nigra of parkinsonian brain. J Neural Transm 1988, 74:199-205.
    • (1988) J Neural Transm , vol.74 , pp. 199-205
    • Sofic, E.1    Riederer, P.2    Heinsen, H.3    Beckmann, H.4    Reynolds, G.P.5    Hebenstreit, G.6
  • 51
    • 0030755867 scopus 로고    scopus 로고
    • Controversies about iron in parkinsonian and control substantia nigra
    • Gałazka-Friedman J., Friedman A. Controversies about iron in parkinsonian and control substantia nigra. Acta Neurobiol Exp 1997, 57:210-225.
    • (1997) Acta Neurobiol Exp , vol.57 , pp. 210-225
    • Gałazka-Friedman, J.1    Friedman, A.2
  • 52
    • 78249252333 scopus 로고    scopus 로고
    • Defective FA2H leads to a novel form of neurodegeneration with brain iron accumulation (NBIA)
    • Kruer M.C., Paisan-Ruiz C., Boddaert N., Yoon M.Y., Hama H., Gregory A., et al. Defective FA2H leads to a novel form of neurodegeneration with brain iron accumulation (NBIA). Ann Neurol 2010, 68:611-618.
    • (2010) Ann Neurol , vol.68 , pp. 611-618
    • Kruer, M.C.1    Paisan-Ruiz, C.2    Boddaert, N.3    Yoon, M.Y.4    Hama, H.5    Gregory, A.6
  • 54
    • 79959509957 scopus 로고
    • GeneReviews [Internet], University of Washington, Seattle, Seattle (WA), R.A. Pagon, T.C. Bird, C.R. Dolan, K. Stephens (Eds.)
    • Gregory A., Hayflick S.J. Pantothenate kinase-associated neurodegeneration 1993, GeneReviews [Internet], University of Washington, Seattle, Seattle (WA). http://www.ncbi.nlm.nih.gov/books/NBK1490/, R.A. Pagon, T.C. Bird, C.R. Dolan, K. Stephens (Eds.).
    • (1993) Pantothenate kinase-associated neurodegeneration
    • Gregory, A.1    Hayflick, S.J.2
  • 55
    • 0022381482 scopus 로고
    • Hallervorden-Spatz disease: cysteine accumulation and cysteine dioxygenase deficiency in the globus pallidus
    • Perry T.L., Norman M.G., Yong V.W., Whiting S., Crichton J.U., Hansen S., et al. Hallervorden-Spatz disease: cysteine accumulation and cysteine dioxygenase deficiency in the globus pallidus. Ann Neurol 1985, 18:482-489.
    • (1985) Ann Neurol , vol.18 , pp. 482-489
    • Perry, T.L.1    Norman, M.G.2    Yong, V.W.3    Whiting, S.4    Crichton, J.U.5    Hansen, S.6
  • 56
    • 12344334370 scopus 로고    scopus 로고
    • Deficiency of pantothenate kinase 2 (Pank2) in mice leads to retinal degeneration and azoospermia
    • Kuo Y.M., Duncan J.L., Westaway S.K., Yang H., Nune G., Xu E.Y., et al. Deficiency of pantothenate kinase 2 (Pank2) in mice leads to retinal degeneration and azoospermia. Hum Mol Genet 2005, 14:49-57.
    • (2005) Hum Mol Genet , vol.14 , pp. 49-57
    • Kuo, Y.M.1    Duncan, J.L.2    Westaway, S.K.3    Yang, H.4    Nune, G.5    Xu, E.Y.6
  • 57
    • 77953703758 scopus 로고    scopus 로고
    • Pantothenate kinase-2 (Pank2) silencing causes cell growth reduction, cell-specific ferroportin upregulation and iron deregulation
    • Poli M., Derosas M., Luscieti S., Cavadini P., Campanella A., Verardi R., et al. Pantothenate kinase-2 (Pank2) silencing causes cell growth reduction, cell-specific ferroportin upregulation and iron deregulation. Neurobiol Dis 2010, 39:204-210.
    • (2010) Neurobiol Dis , vol.39 , pp. 204-210
    • Poli, M.1    Derosas, M.2    Luscieti, S.3    Cavadini, P.4    Campanella, A.5    Verardi, R.6
  • 59
    • 77956052050 scopus 로고    scopus 로고
    • Lipid raft-dependent endocytosis: a new route for hepcidin-mediated regulation of ferroportin in macrophages
    • Auriac A., Willemetz A., Canonne-Hergaux F. Lipid raft-dependent endocytosis: a new route for hepcidin-mediated regulation of ferroportin in macrophages. Haematologica 2010, 95:1269-1277.
    • (2010) Haematologica , vol.95 , pp. 1269-1277
    • Auriac, A.1    Willemetz, A.2    Canonne-Hergaux, F.3
  • 60
    • 33745553895 scopus 로고    scopus 로고
    • PLA2G6, encoding a phospholipase A2, is mutated in neurodegenerative disorders with high brain iron
    • Morgan N.V., Westaway S.K., Morton J.E., Gregory A., Gissen P., Sonek S., et al. PLA2G6, encoding a phospholipase A2, is mutated in neurodegenerative disorders with high brain iron. Nat Genet 2006, 38:752-754.
    • (2006) Nat Genet , vol.38 , pp. 752-754
    • Morgan, N.V.1    Westaway, S.K.2    Morton, J.E.3    Gregory, A.4    Gissen, P.5    Sonek, S.6
  • 61
    • 79959532519 scopus 로고
    • Aug 12, University of Washington, Seattle, [updated 2008 May 15], R.A. Pagon, T.C. Bird, C.R. Dolan, K. Stephens (Eds.)
    • Miyajima H. Aceruloplasminemia 1993-2003 Aug 12, University of Washington, Seattle, [updated 2008 May 15]. R.A. Pagon, T.C. Bird, C.R. Dolan, K. Stephens (Eds.).
    • (1993) Aceruloplasminemia, 12
    • Miyajima, H.1
  • 62
    • 34250800318 scopus 로고    scopus 로고
    • Ferroxidase activity is required for the stability of cell surface ferroportin in cells expressing GPI-ceruloplasmin
    • De Domenico I., Ward D.M., di Patti M.C., Jeong S.Y., David S., Musci G., et al. Ferroxidase activity is required for the stability of cell surface ferroportin in cells expressing GPI-ceruloplasmin. EMBO J 2007, 26:2823-2831.
    • (2007) EMBO J , vol.26 , pp. 2823-2831
    • De Domenico, I.1    Ward, D.M.2    di Patti, M.C.3    Jeong, S.Y.4    David, S.5    Musci, G.6
  • 63
    • 0034941118 scopus 로고    scopus 로고
    • Mutation in the gene encoding ferritin light polypeptide causes dominant adult- onset basal ganglia disease
    • Curtis A.R.J., Fey C., Morris C.M., Bindoff L.A., Ince P.G., Chinnery P.F., et al. Mutation in the gene encoding ferritin light polypeptide causes dominant adult- onset basal ganglia disease. Nat Genet 2001, 28:350-354.
    • (2001) Nat Genet , vol.28 , pp. 350-354
    • Curtis, A.R.J.1    Fey, C.2    Morris, C.M.3    Bindoff, L.A.4    Ince, P.G.5    Chinnery, P.F.6
  • 65
    • 14544294357 scopus 로고    scopus 로고
    • Neuroferritinopathy: a neurodegenerative disorder associated with L-ferritin mutation
    • Levi S., Cozzi A., Arosio P. Neuroferritinopathy: a neurodegenerative disorder associated with L-ferritin mutation. Best Pract Res Clin Heamatol 2005, 18:265-276.
    • (2005) Best Pract Res Clin Heamatol , vol.18 , pp. 265-276
    • Levi, S.1    Cozzi, A.2    Arosio, P.3
  • 66
    • 84996111069 scopus 로고
    • Is Parkinson's disease a progressive siderosis of substantia nigra resulting in iron and melanin induced neurodegeneration?
    • Youdim M.B.H., Ben-Shachar D., Riederer P. Is Parkinson's disease a progressive siderosis of substantia nigra resulting in iron and melanin induced neurodegeneration?. Acta Neurol Scand 1989, 126:47-54.
    • (1989) Acta Neurol Scand , vol.126 , pp. 47-54
    • Youdim, M.B.H.1    Ben-Shachar, D.2    Riederer, P.3
  • 67
    • 0014240538 scopus 로고
    • Studies on Parkinson's disease including x-ray fluorescent spectroscopy of formalin fixed brain tissue
    • Earle K.M. Studies on Parkinson's disease including x-ray fluorescent spectroscopy of formalin fixed brain tissue. J Neuropathol Exp Neurol 1968, 27:1-13.
    • (1968) J Neuropathol Exp Neurol , vol.27 , pp. 1-13
    • Earle, K.M.1
  • 68
    • 0027193251 scopus 로고
    • Distribution of iron in the basal ganglia and neocortex in postmortem tissue in Parkinson's disease and Alzheimer's disease
    • Griffiths P.D., Crossman A.R. Distribution of iron in the basal ganglia and neocortex in postmortem tissue in Parkinson's disease and Alzheimer's disease. Dementia 1993, 4:61-65.
    • (1993) Dementia , vol.4 , pp. 61-65
    • Griffiths, P.D.1    Crossman, A.R.2
  • 69
    • 0024339772 scopus 로고
    • Regional metal concentrations in Parkinson's disease, other chronic neurological disease, and control brains
    • Uitti R.J., Rajput A.H., Rozdilsky B., Bickis M., Wollin T., Yuen W.K. Regional metal concentrations in Parkinson's disease, other chronic neurological disease, and control brains. Can J Neurol Sci 1989, 16:310-314.
    • (1989) Can J Neurol Sci , vol.16 , pp. 310-314
    • Uitti, R.J.1    Rajput, A.H.2    Rozdilsky, B.3    Bickis, M.4    Wollin, T.5    Yuen, W.K.6
  • 70
    • 0029153619 scopus 로고
    • Transferrin and iron in normal, Alzheimer's disease, and Parkinson's disease brain regions
    • Loeffler D.A., Connor J.R., Juneau P.I., Snyder B.S., Kanaley L., DeMaggio A.J., et al. Transferrin and iron in normal, Alzheimer's disease, and Parkinson's disease brain regions. J Neurochem 1995, 65:710-716.
    • (1995) J Neurochem , vol.65 , pp. 710-716
    • Loeffler, D.A.1    Connor, J.R.2    Juneau, P.I.3    Snyder, B.S.4    Kanaley, L.5    DeMaggio, A.J.6
  • 72
    • 33749989574 scopus 로고    scopus 로고
    • A proposed dual role of neuromelanin in the pathogenesis of Parkinson's disease
    • Zecca L., Zucca F.A., Albertini A., Rizzio E., Fariello R.G. A proposed dual role of neuromelanin in the pathogenesis of Parkinson's disease. Neurology 2006, 67(Suppl 2):S8-S11.
    • (2006) Neurology , vol.67 , Issue.SUPPL 2
    • Zecca, L.1    Zucca, F.A.2    Albertini, A.3    Rizzio, E.4    Fariello, R.G.5
  • 73
    • 3042793602 scopus 로고    scopus 로고
    • The role of iron and copper molecules in the neuronal vulnerability of locus coeruleus and substantia nigra during aging
    • Zecca L., Stroppolo A., Gatti A., Tampellini D., Toscani M., Gallorini M., et al. The role of iron and copper molecules in the neuronal vulnerability of locus coeruleus and substantia nigra during aging. PNAS 2004, 101:9843-9848.
    • (2004) PNAS , vol.101 , pp. 9843-9848
    • Zecca, L.1    Stroppolo, A.2    Gatti, A.3    Tampellini, D.4    Toscani, M.5    Gallorini, M.6
  • 74
    • 1342285717 scopus 로고    scopus 로고
    • Mössbauer spectroscopy and ELISA studies reveal differences between Parkinson's disease and control substantia nigra
    • Galazka-Friedman J., Bauminger E.R., Koziorowski D., Friedman A. Mössbauer spectroscopy and ELISA studies reveal differences between Parkinson's disease and control substantia nigra. Biochim Biophys Acta 2004, 1688:130-136.
    • (2004) Biochim Biophys Acta , vol.1688 , pp. 130-136
    • Galazka-Friedman, J.1    Bauminger, E.R.2    Koziorowski, D.3    Friedman, A.4
  • 75
    • 0036798434 scopus 로고    scopus 로고
    • Lack of upregulation of ferritin is associated with sustained iron regulatory protein-1 binding activity in the substantia nigra of patients with Parkinson's disease
    • Faucheux B.A., Martin M.E., Beaumont C., Hunot S., Hauw J.J., Hirsch E.C. Lack of upregulation of ferritin is associated with sustained iron regulatory protein-1 binding activity in the substantia nigra of patients with Parkinson's disease. J Neurochem 2002, 83:320-330.
    • (2002) J Neurochem , vol.83 , pp. 320-330
    • Faucheux, B.A.1    Martin, M.E.2    Beaumont, C.3    Hunot, S.4    Hauw, J.J.5    Hirsch, E.C.6
  • 76
    • 0029092802 scopus 로고
    • A quantitative analysis of isoferritins in select regions of aged, parkinsonian, and Alzheimer's diseased brains
    • Connor J.R., Snyder B.S., Arosio P., Loeffler D.A., LeWitt P. A quantitative analysis of isoferritins in select regions of aged, parkinsonian, and Alzheimer's diseased brains. J Neurochem 1995, 65:717-724.
    • (1995) J Neurochem , vol.65 , pp. 717-724
    • Connor, J.R.1    Snyder, B.S.2    Arosio, P.3    Loeffler, D.A.4    LeWitt, P.5
  • 77
    • 0028350924 scopus 로고
    • Isoforms of ferritin have a specific cellular distribution in the brain
    • Connor J.R., Boeshore K.L., Benkovic S.A., Menzies S.L. Isoforms of ferritin have a specific cellular distribution in the brain. J Neurosci Res 1994, 37:461-465.
    • (1994) J Neurosci Res , vol.37 , pp. 461-465
    • Connor, J.R.1    Boeshore, K.L.2    Benkovic, S.A.3    Menzies, S.L.4
  • 78
    • 23844465238 scopus 로고    scopus 로고
    • Expression of 8-oxoguanine DNA glycosylase (OGG1) in Parkinson's disease and related neurodegenerative disorders
    • Fukae J., Takanashi M., Kubo S., Nishioka K., Nakabeppu K., Mori H., et al. Expression of 8-oxoguanine DNA glycosylase (OGG1) in Parkinson's disease and related neurodegenerative disorders. Acta Neuropathol 2005, 109:256-262.
    • (2005) Acta Neuropathol , vol.109 , pp. 256-262
    • Fukae, J.1    Takanashi, M.2    Kubo, S.3    Nishioka, K.4    Nakabeppu, K.5    Mori, H.6
  • 80
    • 0025821265 scopus 로고
    • Alterations in the level of iron, ferritin and other trace metals in Parkinson's disease and other neurodegenerative diseases affecting the basal ganglia
    • Dexter D.T., Carayon A., Javoy-Agid F., Agid Y., Wells F.R., Daniel S.E., et al. Alterations in the level of iron, ferritin and other trace metals in Parkinson's disease and other neurodegenerative diseases affecting the basal ganglia. Brain 1991, 114:1953-1975.
    • (1991) Brain , vol.114 , pp. 1953-1975
    • Dexter, D.T.1    Carayon, A.2    Javoy-Agid, F.3    Agid, Y.4    Wells, F.R.5    Daniel, S.E.6
  • 81
    • 2942549658 scopus 로고    scopus 로고
    • Electron nanodiffraction and high-resolution electron microscopy studies of the structure and composition of physiological and pathological ferritin
    • Quintana C., Cowley J.M., Marhic C. Electron nanodiffraction and high-resolution electron microscopy studies of the structure and composition of physiological and pathological ferritin. J Struct Biol 2004, 147:166-178.
    • (2004) J Struct Biol , vol.147 , pp. 166-178
    • Quintana, C.1    Cowley, J.M.2    Marhic, C.3
  • 83
    • 0030885482 scopus 로고    scopus 로고
    • Iron accumulation in Alzheimer disease is a source of redox generated free radicals
    • Smith M.A., Harris P.L.R., Sayre L.M., Perry G. Iron accumulation in Alzheimer disease is a source of redox generated free radicals. Proc Natl Acad Sci U S A 1997, 94:9866-9868.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 9866-9868
    • Smith, M.A.1    Harris, P.L.R.2    Sayre, L.M.3    Perry, G.4
  • 84
    • 84961042345 scopus 로고
    • The effect of age on non-haemin iron in human brain
    • Hallgren B., Sourander P. The effect of age on non-haemin iron in human brain. J Neurochem 1958, 3:41-51.
    • (1958) J Neurochem , vol.3 , pp. 41-51
    • Hallgren, B.1    Sourander, P.2
  • 85
    • 0027260711 scopus 로고
    • Total and paramagnetic metals in human substantia nigra and its neuromelanin
    • Zecca L., Swartz H.M. Total and paramagnetic metals in human substantia nigra and its neuromelanin. J Neural Transm Park Dis Dement Sect 1993, 5:203-213.
    • (1993) J Neural Transm Park Dis Dement Sect , vol.5 , pp. 203-213
    • Zecca, L.1    Swartz, H.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.