메뉴 건너뛰기




Volumn 109, Issue 4, 2009, Pages 1067-1078

Abnormal iron metabolism and oxidative stress in mice expressing a mutant form of the ferritin light polypeptide gene

Author keywords

Animal model; Hereditary ferritinopathy; Neuroferritinopathy

Indexed keywords

BRAIN EXTRACT; CARBONYL DERIVATIVE; CD71 ANTIGEN; COMPLEMENTARY DNA; FERRITIN; NITRONE; POLYPEPTIDE;

EID: 65649154118     PISSN: 00223042     EISSN: 14714159     Source Type: Journal    
DOI: 10.1111/j.1471-4159.2009.06028.x     Document Type: Article
Times cited : (66)

References (43)
  • 2
    • 57649133953 scopus 로고    scopus 로고
    • Iron-mediated aggregation and a localized structural change characterize ferritin from a mutant light chain polypeptide that causes neurodegeneration
    • Baraibar M. A., Barbeito A. G., Muhoberac B. B. Vidal R. (2008) Iron-mediated aggregation and a localized structural change characterize ferritin from a mutant light chain polypeptide that causes neurodegeneration. J. Biol. Chem. 283, 31679 31689.
    • (2008) J. Biol. Chem. , vol.283 , pp. 31679-31689
    • Baraibar, M.A.1    Barbeito, A.G.2    Muhoberac, B.B.3    Vidal, R.4
  • 3
    • 0041534373 scopus 로고    scopus 로고
    • Iron status and neural functioning
    • DOI 10.1146/annurev.nutr.23.020102.075739
    • Beard J. L. Connor J. R. (2003) Iron status and neural functioning. Annu. Rev. Nutr. 23, 41 58. (Pubitemid 37059715)
    • (2003) Annual Review of Nutrition , vol.23 , pp. 41-58
    • Beard, J.L.1    Connor, J.R.2
  • 4
    • 34247564692 scopus 로고    scopus 로고
    • Role of iron in neurodegenerative disorders
    • DOI 10.1097/01.rmr.0000245461.90406.ad, PII 0000214220060200000002
    • Berg D. Youdim M. B. (2006) Role of iron in neurodegenerative disorders. Top. Magn. Reson. Imaging 17, 5 17. (Pubitemid 46672929)
    • (2006) Topics in Magnetic Resonance Imaging , vol.17 , Issue.1 , pp. 5-17
    • Berg, D.1    Youdim, M.B.H.2
  • 5
    • 42949166848 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in SOD1G93A-bearing astrocytes promotes motor neuron degeneration: Prevention by mitochondrial-targeted antioxidants
    • Cassina P., Cassina A., Pehar M. et al. (2008) Mitochondrial dysfunction in SOD1G93A-bearing astrocytes promotes motor neuron degeneration: prevention by mitochondrial-targeted antioxidants. J. Neurosci. 28, 4115 4122.
    • (2008) J. Neurosci. , vol.28 , pp. 4115-4122
    • Cassina, P.1    Cassina, A.2    Pehar, M.3
  • 6
    • 0033947467 scopus 로고    scopus 로고
    • Sequestration of iron by Lewy bodies in Parkinson's disease
    • Castellani R. J., Siedlak S. L., Perry G. Smith M. A. (2000) Sequestration of iron by Lewy bodies in Parkinson's disease. Acta Neuropathol. 100, 111 114. (Pubitemid 30456131)
    • (2000) Acta Neuropathologica , vol.100 , Issue.2 , pp. 111-114
    • Castellani, R.J.1    Siedlak, S.L.2    Perry, G.3    Smith, M.A.4
  • 7
    • 0031605490 scopus 로고    scopus 로고
    • Ferritin. Uptake, storage, and release of iron
    • Chasteen N. D. (1998) Ferritin. Uptake, storage, and release of iron. Met. Ions Biol. Syst. 35, 479 514.
    • (1998) Met. Ions Biol. Syst. , vol.35 , pp. 479-514
    • Chasteen, N.D.1
  • 8
    • 0026513756 scopus 로고
    • A histochemical study of iron, transferrin, and ferritin in Alzheimer's diseased brains
    • Connor J. R., Menzies S. L., St Martin S. M. Mufson E. J. (1992) A histochemical study of iron, transferrin, and ferritin in Alzheimer's diseased brains. J. Neurosci. Res. 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
  • 10
    • 0032504563 scopus 로고    scopus 로고
    • Immunohistochemical analysis of transferrin receptor: Regional and cellular distribution in the hypotransferrinemic (hpx) mouse brain
    • DOI 10.1016/S0006-8993(98)00575-7, PII S0006899398005757
    • Dickinson T. K. Connor J. R. (1998) Immunohistochemical analysis of transferrin receptor: regional and cellular distribution in the hypotransferrinemic (hpx) mouse brain. Brain Res. 801, 171 181. (Pubitemid 28401661)
    • (1998) Brain Research , vol.801 , Issue.1-2 , pp. 171-181
    • Dickinson, T.K.1    Connor, J.R.2
  • 11
    • 0033826764 scopus 로고    scopus 로고
    • Iron regulatory proteins and the molecular control of mammalian iron metabolism
    • Eisenstein R. S. (2000) Iron regulatory proteins and the molecular control of mammalian iron metabolism. Annu. Rev. Nutr. 20, 627 662.
    • (2000) Annu. Rev. Nutr. , vol.20 , pp. 627-662
    • Eisenstein, R.S.1
  • 12
    • 30944449709 scopus 로고    scopus 로고
    • Generation of conditional alleles of the murine iron regulatory protein (IRP)-1 and -2 genes
    • DOI 10.1002/gene.20169
    • Galy B., Ferring D. Hentze M. W. (2005) Generation of conditional alleles of the murine iron regulatory protein (IRP)-1 and -2 genes. Genesis 43, 181 188. (Pubitemid 43117834)
    • (2005) Genesis , vol.43 , Issue.4 , pp. 181-188
    • Galy, B.1    Feering, D.2    Hentze, M.W.3
  • 13
    • 0030608152 scopus 로고    scopus 로고
    • The ferritins: Molecular properties, iron storage function and cellular regulation
    • DOI 10.1016/0005-2728(96)00022-9
    • Harrison P. M. Arosio P. (1996) The ferritins: molecular properties, iron storage function and cellular regulation. Biochim. Biophys. Acta 1275, 161 203. (Pubitemid 26248989)
    • (1996) Biochimica et Biophysica Acta - Bioenergetics , vol.1275 , Issue.3 , pp. 161-203
    • Harrison, P.M.1    Arosio, P.2
  • 14
    • 2042546096 scopus 로고    scopus 로고
    • Balancing acts: Molecular control of mammalian iron metabolism
    • DOI 10.1016/S0092-8674(04)00343-5, PII S0092867404003435
    • Hentze M. W., Muckenthaler M. U. Andrews N. C. (2004) Balancing acts: molecular control of mammalian iron metabolism. Cell 117, 285 297. (Pubitemid 38534536)
    • (2004) Cell , vol.117 , Issue.3 , pp. 285-297
    • Hentze, M.W.1    Muckenthaler, M.U.2    Andrews, N.C.3
  • 15
    • 33846258191 scopus 로고    scopus 로고
    • Validation of endogenous controls for quantitative gene expression analysis: Application on brain cortices of human chronic alcoholics
    • DOI 10.1016/j.brainres.2006.11.026, PII S000689930603321X
    • Johansson S., Fuchs A., Okvist A., Karimi M., Harper C., Garrick T., Sheedy D., Hurd Y., Bakalkin G. Ekström T. J. (2007) Validation of endogenous controls for quantitative gene expression analysis: application on brain cortices of human chronic alcoholics. Brain Res. 1132, 20 28. (Pubitemid 46096453)
    • (2007) Brain Research , vol.1132 , Issue.1 , pp. 20-28
    • Johansson, S.1    Fuchs, A.2    Okvist, A.3    Karimi, M.4    Harper, C.5    Garrick, T.6    Sheedy, D.7    Hurd, Y.8    Bakalkin, G.9    Ekstrom, T.J.10
  • 16
    • 0032746973 scopus 로고    scopus 로고
    • Control of transferrin receptor expression via nitric oxide-mediated modulation of iron-regulatory protein 2
    • Kim S. Ponka P. (1999) Control of transferrin receptor expression via nitric oxide-mediated modulation of iron-regulatory protein 2. J. Biol. Chem. 274, 33035 33042. (Pubitemid 129535344)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.46 , pp. 33035-33042
    • Kim, S.1    Ponka, P.2
  • 17
    • 0026673757 scopus 로고
    • Coordination of cellular iron metabolism by post-transcriptional gene regulation
    • Kühn L. C. Hentze M. W. (1992) Coordination of cellular iron metabolism by post-transcriptional gene regulation. J. Inorg. Biochem. 47, 183 195.
    • (1992) J. Inorg. Biochem. , vol.47 , pp. 183-195
    • Kühn, L.C.1    Hentze, M.W.2
  • 18
    • 34548665512 scopus 로고    scopus 로고
    • Localization and regulation of mouse pantothenate kinase 2
    • DOI 10.1016/j.febslet.2007.08.056, PII S0014579307009325
    • Leonardi R., Zhang Y. M., Lykidis A., Rock C. O. Jackowski S. (2007) Localization and regulation of mouse pantothenate kinase 2. FEBS Lett. 581, 4639 4644. (Pubitemid 47418790)
    • (2007) FEBS Letters , vol.581 , Issue.24 , pp. 4639-4644
    • Leonardi, R.1    Zhang, Y.-M.2    Lykidis, A.3    Rock, C.O.4    Jackowski, S.5
  • 19
    • 0026095312 scopus 로고
    • Oligodendrocytes and myelin sheaths in normal, quaking and shiverer brains are enriched in iron
    • LeVine S. M. (1991) Oligodendrocytes and myelin sheaths in normal, quaking and shiverer brains are enriched in iron. J. Neurosci. Res. 29, 413 419.
    • (1991) J. Neurosci. Res. , vol.29 , pp. 413-419
    • Levine, S.M.1
  • 21
    • 0036358643 scopus 로고    scopus 로고
    • Activation of iron regulatory protein- 1 by oxidative stress
    • DOI 10.1016/S0076-6879(02)48651-X, 32, Part B: Protein Sensors and Reactive Oxygen Species
    • Mueller S. Pantopoulos K. (2002) Activation of iron regulatory protein-1 (IRP1) by oxidative stress. Methods Enzymol. 348, 324 337. (Pubitemid 41103123)
    • (2002) Methods in Enzymology , vol.348 , pp. 324-337
    • Mueller, S.1    Pantopoulos, K.2
  • 22
    • 0024276911 scopus 로고
    • A stem-loop in the 3′ untranslated region mediates iron-dependent regulation of transferrin receptor mRNA stability in the cytoplasm
    • Müllner E. W. Kühn L. C. (1988) A stem-loop in the 3′ untranslated region mediates iron-dependent regulation of transferrin receptor mRNA stability in the cytoplasm. Cell 53, 815 825.
    • (1988) Cell , vol.53 , pp. 815-825
    • Müllner, E.W.1    Kühn, L.C.2
  • 23
    • 0021089933 scopus 로고
    • Iron uptake and utilization by mammalian cells. I: Cellular uptake of transferrin and iron
    • DOI 10.1016/0968-0004(83)90217-7
    • Octave J. N., Schneider Y. J., Trouet A. Crichton R. R. (1983) Iron uptake and utilization by mammalian cells. I. cellular uptake of transferrin and iron. Trends Biochem. Sci. 8, 217 221. (Pubitemid 14240729)
    • (1983) Trends in Biochemical Sciences , vol.8 , Issue.6 , pp. 217-220
    • Octave, J.N.1    Schneider, Y.J.2    Trouet, A.3    Crichton, R.R.4
  • 24
    • 0032694352 scopus 로고    scopus 로고
    • Adenovirus E1A blocks oxidant-dependent ferritin induction and sensitizes cells to pro-oxidant cytotoxicity
    • DOI 10.1016/S0014-5793(99)01443-X, PII S001457939901443X
    • Orino K., Tsuji Y., Torti F. M. Torti S. V. (1999) Adenovirus E1A blocks oxidant-dependent ferritin induction and sensitizes cells to pro-oxidant cytotoxicity. FEBS Lett. 461, 334 338. (Pubitemid 29533358)
    • (1999) FEBS Letters , vol.461 , Issue.3 , pp. 334-338
    • Orino, K.1    Tsuji, Y.2    Torti, F.M.3    Torti, S.V.4
  • 26
    • 0036113819 scopus 로고    scopus 로고
    • The role of iron and copper in the aetiology of neurodegenerative disorders: Therapeutic implications
    • Perry G., Sayre L. M., Atwood C. S., Castellani R. J., Cash A. D., Rottkamp C. A. Smith M. A. (2002) The role of iron and copper in the aetiology of neurodegenerative disorders: therapeutic implications. CNS Drugs 16, 339 352. (Pubitemid 34548201)
    • (2002) CNS Drugs , vol.16 , Issue.5 , pp. 339-352
    • Perry, G.1    Sayre, L.M.2    Atwood, C.S.3    Castellani, R.J.4    Cash, A.D.5    Rottkamp, C.A.6    Smith, M.A.7
  • 28
    • 0032546922 scopus 로고    scopus 로고
    • Role of ferritin in the control of the labile iron pool in murine erythroleukemia cells
    • DOI 10.1074/jbc.273.25.15382
    • Picard V., Epsztejn S., Santambrogio P., Cabantchik Z. I. Beaumont C. (1998) Role of ferritin in the control of the labile iron pool in murine erythroleukemia cells. J. Biol. Chem. 273, 15382 15386. (Pubitemid 28298142)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.25 , pp. 15382-15386
    • Picard, V.1    Epsztejn, S.2    Santambrogio, P.3    Cabantchik, Z.I.4    Beaumont, C.5
  • 29
    • 0342948905 scopus 로고    scopus 로고
    • Variations in dietary iron alter brain iron metabolism in developing rats
    • Pinero D. J. Connor J. R. (2000) Iron in the brain: an important contributor in normal and diseased states. Neuroscientist 6, 435 453. (Pubitemid 30073804)
    • (2000) Journal of Nutrition , vol.130 , Issue.2 , pp. 254-263
    • Pinero, D.J.1    Li, N.-Q.2    Connor, J.R.3    Beard, J.L.4
  • 31
    • 0030463223 scopus 로고    scopus 로고
    • Role of H and L subunits in mouse ferritin
    • DOI 10.1074/jbc.271.52.33352
    • Rucker P., Torti F. M. Torti S. V. (1996) Role of H and L subunits in mouse ferritin. J. Biol. Chem. 271, 33352 33357. (Pubitemid 27010145)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.52 , pp. 33352-33357
    • Rucker, P.1    Torti, F.M.2    Torti, S.V.3
  • 32
    • 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
    • DOI 10.1046/j.1471-4159.2000.0740270.x
    • Sayre L. M., Perry G., Harris P. L. R., Liu Y., Schubert K. A. Smith M. A. (2000) In situ oxidative catalysis by neurofibrillary tangles and senile plaques in Alzheimer's disease: a central role for bound transition metals. J. Neurochem. 74, 270 279. (Pubitemid 30012778)
    • (2000) Journal of Neurochemistry , vol.74 , Issue.1 , pp. 270-279
    • Sayre, L.M.1    Perry, G.2    Harris, P.L.R.3    Liu, Y.4    Schubert, K.A.5    Smith, M.A.6
  • 34
    • 0031776586 scopus 로고    scopus 로고
    • Cytochemical demonstration of oxidative damage in Alzheimer disease by immunochemical enhancement of the carbonyl reaction with 2,4- dinitrophenylhydrazine
    • Smith M. A., Sayre L. M., Anderson V. E., Harris P. L., Beal M. F., Kowall N. Perry G. (1998) Cytochemical demonstration of oxidative damage in Alzheimer disease by immunochemical enhancement of the carbonyl reaction with 2,4-dinitrophenylhydrazine. J. Histochem. Cytochem. 46, 731 735. (Pubitemid 28272207)
    • (1998) Journal of Histochemistry and Cytochemistry , vol.46 , Issue.6 , pp. 731-735
    • Smith, M.A.1    Sayre, L.M.2    Anderson, V.E.3    Harris, P.L.R.4    Beal, M.F.5    Kowall, N.6    Perry, G.7
  • 35
    • 0032819392 scopus 로고    scopus 로고
    • Effect of age and caloric restriction on bleomycin-chelatable and nonheme iron in different tissues of C57BL/6 mice
    • DOI 10.1016/S0891-5849(99)00052-0, PII S0891584999000520
    • Sohal R. S., Wennberg-Kirch E., Jaiswal K., Kwong L. K. Forster M. J. (1999) Effect of age and caloric restriction on bleomycin-chelatable and nonheme iron in different tissues of C57BL/6 mice. Free Radic. Biol. Med. 27, 287 293. (Pubitemid 29395420)
    • (1999) Free Radical Biology and Medicine , vol.27 , Issue.3-4 , pp. 287-293
    • Sohal, R.S.1    Wennberg-Kirch, E.2    Jaiswal, K.3    Kwong, L.K.4    Forster, M.J.5
  • 36
    • 0025112529 scopus 로고
    • The ferritin family of iron storage proteins
    • Theil E. C. (1990) The ferritin family of iron storage proteins. Adv. Enzymol. Relat. Areas Mol. Biol. 63, 421 449.
    • (1990) Adv. Enzymol. Relat. Areas Mol. Biol. , vol.63 , pp. 421-449
    • Theil, E.C.1
  • 37
    • 0037216723 scopus 로고    scopus 로고
    • Mouse brains deficient in H-ferritin have normal iron concentration but a protein profile of iron deficiency and increased evidence of oxidative stress
    • DOI 10.1002/jnr.10463
    • Thompson K., Menzies S., Muckenthaler M., Torti F. M., Wood T., Torti S. V., Hentze M. W., Beard J. Connor J. (2003) Mouse brains deficient in H-ferritin have normal iron concentration but a protein profile of iron deficiency and increased evidence of oxidative stress. J. Neurosci. Res. 71, 46 63. (Pubitemid 36008401)
    • (2003) Journal of Neuroscience Research , vol.71 , Issue.1 , pp. 46-63
    • Thompson, K.1    Menzies, S.2    Muckenthaler, M.3    Torti, F.M.4    Wood, T.5    Torti, S.V.6    Hentze, M.W.7    Beard, J.8    Connor, J.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.