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Volumn 17, Issue 15, 2008, Pages 2265-2273

Iron-dependent regulation of frataxin expression: Implications for treatment of Friedreich ataxia

Author keywords

[No Author keywords available]

Indexed keywords

DEFEROXAMINE MESYLATE; FERRIC AMMONIUM CITRATE; FRATAXIN; IRON; IRON CHELATING AGENT; IRON REGULATORY PROTEIN 1; IRON REGULATORY PROTEIN 2; MESSENGER RNA; SULFUR;

EID: 47249127786     PISSN: 09646906     EISSN: 14602083     Source Type: Journal    
DOI: 10.1093/hmg/ddn127     Document Type: Article
Times cited : (125)

References (43)
  • 4
    • 0035138072 scopus 로고    scopus 로고
    • Mouse models for Friedreich ataxia exhibit cardiomyopathy, sensory nerve defect and Fe-S enzyme deficiency followed by intramitochondrial iron deposits
    • Puccio, H., Simon, D., Cosscc, M., Criqui-Filipe, P., Tiziano, F., Melki, J., Hindelang, C., Matyas, R., Rustin, P. and Koenig, M. (2001) Mouse models for Friedreich ataxia exhibit cardiomyopathy, sensory nerve defect and Fe-S enzyme deficiency followed by intramitochondrial iron deposits. Nat. Genet., 27, 181-186.
    • (2001) Nat. Genet , vol.27 , pp. 181-186
    • Puccio, H.1    Simon, D.2    Cosscc, M.3    Criqui-Filipe, P.4    Tiziano, F.5    Melki, J.6    Hindelang, C.7    Matyas, R.8    Rustin, P.9    Koenig, M.10
  • 7
    • 0033054177 scopus 로고    scopus 로고
    • The Friedreich's ataxia mutation confers cellular sensitivity to oxidant stress which is rescued by chelators of iron and calcium and inhibitors of apoptosis
    • Wong, A., Yang, J., Cavadini, P., Genera, C., Lonnerdal, B., Taroni, F. and Cortopassi, G. (1999) The Friedreich's ataxia mutation confers cellular sensitivity to oxidant stress which is rescued by chelators of iron and calcium and inhibitors of apoptosis. Hum. Mol. Genet., 8, 425-430.
    • (1999) Hum. Mol. Genet , vol.8 , pp. 425-430
    • Wong, A.1    Yang, J.2    Cavadini, P.3    Genera, C.4    Lonnerdal, B.5    Taroni, F.6    Cortopassi, G.7
  • 8
    • 0035978474 scopus 로고    scopus 로고
    • Development of potential iron chelators for the treatment of Friedreich's ataxia: Ligands that mobilize mitochondrial iron
    • Richardson, D.R., Mouralian, C., Ponka, P. and Becker, E. (2001) Development of potential iron chelators for the treatment of Friedreich's ataxia: Ligands that mobilize mitochondrial iron. Biochim. Biophys. Acta., 1536, 133-140.
    • (2001) Biochim. Biophys. Acta , vol.1536 , pp. 133-140
    • Richardson, D.R.1    Mouralian, C.2    Ponka, P.3    Becker, E.4
  • 9
    • 0037317490 scopus 로고    scopus 로고
    • Friedreich's ataxia: Iron chelators that target the mitochondrion as a therapeutic strategy?
    • Richardson, D.R. (2003) Friedreich's ataxia: Iron chelators that target the mitochondrion as a therapeutic strategy? Expert Opin. Investig. Drugs, 12, 235-245.
    • (2003) Expert Opin. Investig. Drugs , vol.12 , pp. 235-245
    • Richardson, D.R.1
  • 11
    • 17144378216 scopus 로고    scopus 로고
    • Opinion: Iron-sulphur cluster biogenesis and mitochondrial iron homeostasis
    • Rouault, T.A. and Tong, W.H. (2005) Opinion: Iron-sulphur cluster biogenesis and mitochondrial iron homeostasis. Nat. Rev. Mol. Cell Biol., 6, 345-351.
    • (2005) Nat. Rev. Mol. Cell Biol , vol.6 , pp. 345-351
    • Rouault, T.A.1    Tong, W.H.2
  • 12
    • 0001853405 scopus 로고    scopus 로고
    • The role of the mitochondrion in cellular iron homeostasis
    • Schueck, N.D., Woontner, M. and Koeller, D.M. (2001) The role of the mitochondrion in cellular iron homeostasis. Mitochondrion, 1 51-60.
    • (2001) Mitochondrion , vol.1 , pp. 51-60
    • Schueck, N.D.1    Woontner, M.2    Koeller, D.M.3
  • 13
    • 0032540929 scopus 로고    scopus 로고
    • Mt-Hsp70 homolog, Ssc2p, required for maturation of yeast frataxin and mitochondrial iron horneostasis
    • Knight S.A., Sepuri, N.B., Pain, D. and Dancis, A. (1998) Mt-Hsp70 homolog, Ssc2p, required for maturation of yeast frataxin and mitochondrial iron horneostasis. J. Biol. Chem., 273, 18389-18393.
    • (1998) J. Biol. Chem , vol.273 , pp. 18389-18393
    • Knight, S.A.1    Sepuri, N.B.2    Pain, D.3    Dancis, A.4
  • 14
    • 33644623262 scopus 로고    scopus 로고
    • Functions of mitochondrial ISCU and cytosolic ISCU in mammalian iron-sulftir cluster biogenesis and iron homeostasis
    • Tong, W.H. and Rouault, T.A. (2006) Functions of mitochondrial ISCU and cytosolic ISCU in mammalian iron-sulftir cluster biogenesis and iron homeostasis. Cell Metab., 3, 199-210.
    • (2006) Cell Metab , vol.3 , pp. 199-210
    • Tong, W.H.1    Rouault, T.A.2
  • 16
    • 12844275023 scopus 로고    scopus 로고
    • Ancient repeated DNA elements and the regulation of the human frataxin promoter
    • Greene, E., Entezam, A., Kumari, D. and Usdin, K. (2005) Ancient repeated DNA elements and the regulation of the human frataxin promoter. Genomics, 85, 221-230.
    • (2005) Genomics , vol.85 , pp. 221-230
    • Greene, E.1    Entezam, A.2    Kumari, D.3    Usdin, K.4
  • 17
    • 34250830900 scopus 로고    scopus 로고
    • Repeat-induced epigenetic changes in intron 1 of the frataxin gene and its consequences in Friedreich ataxia
    • Greene, E., Mahishi, L., Entezam, A., Kumari, D. and Usdin, K. (2007) Repeat-induced epigenetic changes in intron 1 of the frataxin gene and its consequences in Friedreich ataxia. Nucleic Acids Res., 35 3383-3390.
    • (2007) Nucleic Acids Res , vol.35 , pp. 3383-3390
    • Greene, E.1    Mahishi, L.2    Entezam, A.3    Kumari, D.4    Usdin, K.5
  • 18
    • 33745222541 scopus 로고    scopus 로고
    • A pool of extramitochondrial frataxin that promotes cell survival
    • Condo, I., Ventura, N., Malisan, F., Tomassini, B. and Testi, R. (2006) A pool of extramitochondrial frataxin that promotes cell survival. J. Biol. Chem., 281, 16750-16756.
    • (2006) J. Biol. Chem , vol.281 , pp. 16750-16756
    • Condo, I.1    Ventura, N.2    Malisan, F.3    Tomassini, B.4    Testi, R.5
  • 19
    • 0034731447 scopus 로고    scopus 로고
    • Two-step processing of human frataxin by mitochondrial processing peptidase. Precursor and intermediate forms are cleaved at different rates
    • Cavadini, P., Adamec, J., Taroni, F., Gakh, O. and Isaya, G. (2000) Two-step processing of human frataxin by mitochondrial processing peptidase. Precursor and intermediate forms are cleaved at different rates. J. Biol. Chem., 275, 41469-41475.
    • (2000) J. Biol. Chem , vol.275 , pp. 41469-41475
    • Cavadini, P.1    Adamec, J.2    Taroni, F.3    Gakh, O.4    Isaya, G.5
  • 21
    • 0141890273 scopus 로고    scopus 로고
    • Oxygen and iron regulation of iron regulatory protein 2
    • Hanson, E.S., Rawlins, M.L. and Leibold, E.A. (2003) Oxygen and iron regulation of iron regulatory protein 2. J. Biol. Chem., 278 40337-40342.
    • (2003) J. Biol. Chem , vol.278 , pp. 40337-40342
    • Hanson, E.S.1    Rawlins, M.L.2    Leibold, E.A.3
  • 22
    • 33746361251 scopus 로고    scopus 로고
    • The role of iron regulatory proteins in mammalian iron homeostasis and disease
    • Rouault, T.A. (2006) The role of iron regulatory proteins in mammalian iron homeostasis and disease. Nat. Chem. Biol., 2, 406-414.
    • (2006) Nat. Chem. Biol , vol.2 , pp. 406-414
    • Rouault, T.A.1
  • 23
    • 23644444604 scopus 로고    scopus 로고
    • Increased IRP1 activity in Friedreich ataxia
    • Lobmayr, L., Brooks, D.G. and Wilson, R.B. (2005) Increased IRP1 activity in Friedreich ataxia. Gene, 354, 157-161.
    • (2005) Gene , vol.354 , pp. 157-161
    • Lobmayr, L.1    Brooks, D.G.2    Wilson, R.B.3
  • 24
    • 9744248303 scopus 로고    scopus 로고
    • Iron-sulfur protein maturation in human cells: Evidence for a function of frataxin
    • Stehling, O., Elsasser, H.P., Bruckel, B., Muhlenhoff, U. and Lill, R. (2004) Iron-sulfur protein maturation in human cells: Evidence for a function of frataxin. Hum. Mol. Genet., 13, 3007-3015.
    • (2004) Hum. Mol. Genet , vol.13 , pp. 3007-3015
    • Stehling, O.1    Elsasser, H.P.2    Bruckel, B.3    Muhlenhoff, U.4    Lill, R.5
  • 26
    • 33746864096 scopus 로고    scopus 로고
    • Molecular control of vertebrate iron homeostasis by iron regulatory proteins
    • Wallander, M.L., Leibold, E.A. and Eisenstein, R.S. (2006) Molecular control of vertebrate iron homeostasis by iron regulatory proteins. Biochim. Biophys. Acta, 1763, 668-689.
    • (2006) Biochim. Biophys. Acta , vol.1763 , pp. 668-689
    • Wallander, M.L.1    Leibold, E.A.2    Eisenstein, R.S.3
  • 27
    • 2042546096 scopus 로고    scopus 로고
    • Balancing acts: Molecular control of mammalian iron metabolism
    • Hentze, M.W., Muckenthaler, M.U. and Andrews, N.C. (2004) Balancing acts: Molecular control of mammalian iron metabolism. Cell, 117 285-297.
    • (2004) Cell , vol.117 , pp. 285-297
    • Hentze, M.W.1    Muckenthaler, M.U.2    Andrews, N.C.3
  • 29
    • 10844282789 scopus 로고    scopus 로고
    • Mammalian tissue oxygen levels modulate iron-regulatory protein activities in vivo
    • Meyron-Holtz, E.G., Ghosh, M.C. and Rouault, T.A. (2004) Mammalian tissue oxygen levels modulate iron-regulatory protein activities in vivo. Science, 306, 2087-2090.
    • (2004) Science , vol.306 , pp. 2087-2090
    • Meyron-Holtz, E.G.1    Ghosh, M.C.2    Rouault, T.A.3
  • 32
    • 2542556601 scopus 로고    scopus 로고
    • Idebenone delays the onset of cardiac functional alteration without correction of Fe-S enzymes deficit in a mouse model for Friedreich ataxia
    • Seznec, H., Simon, D., Monassier, L., Criqui-Filipe, P., Gansmuller, A., Rustin, P., Koenig, M. and Puccio, H. (2004) Idebenone delays the onset of cardiac functional alteration without correction of Fe-S enzymes deficit in a mouse model for Friedreich ataxia. Hum. Mol. Genet., 13, 1017-1024.
    • (2004) Hum. Mol. Genet , vol.13 , pp. 1017-1024
    • Seznec, H.1    Simon, D.2    Monassier, L.3    Criqui-Filipe, P.4    Gansmuller, A.5    Rustin, P.6    Koenig, M.7    Puccio, H.8
  • 33
    • 33746795976 scopus 로고    scopus 로고
    • DNA sequence-specific polyamides alleviate transcription inhibition associated with long GAA.TTC repeats in Friedreich's ataxia
    • Burnett, R., Melander, C., Puckett, J.W., Son, L.S., Wells, R.D., Dervan, P.B. and Gottesfeld, J.M. (2006) DNA sequence-specific polyamides alleviate transcription inhibition associated with long GAA.TTC repeats in Friedreich's ataxia. Proc. Natl. Acad. Sci. USA 103, 11497-11502.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 11497-11502
    • Burnett, R.1    Melander, C.2    Puckett, J.W.3    Son, L.S.4    Wells, R.D.5    Dervan, P.B.6    Gottesfeld, J.M.7
  • 34
    • 33748778745 scopus 로고    scopus 로고
    • Herman, D., Jenssen, K., Burnett, R., Soragni, E., Perlman, S.L. and Gottesfeld, J.M. (2006) Histone deacetylase inhibitors reverse gene silencing in Friedreich's ataxia. Nat, Chem, Biol., 2, 551-558.
    • Herman, D., Jenssen, K., Burnett, R., Soragni, E., Perlman, S.L. and Gottesfeld, J.M. (2006) Histone deacetylase inhibitors reverse gene silencing in Friedreich's ataxia. Nat, Chem, Biol., 2, 551-558.
  • 35
    • 34748841015 scopus 로고    scopus 로고
    • Small molecules affecting transcription in Friedreich ataxia
    • Gottesfeld, J.M. (2007) Small molecules affecting transcription in Friedreich ataxia. Pharmacol. Ther., 116, 236-248.
    • (2007) Pharmacol. Ther , vol.116 , pp. 236-248
    • Gottesfeld, J.M.1
  • 37
    • 38649103446 scopus 로고    scopus 로고
    • Hydrogen peroxide scavenging rescues frataxin deficiency in a Drosophila model of Friedreich's ataxia
    • Anderson, P.R., Kirby, K., Orr, W.C., Hilliker, A.J. and Phillips, J.P. (2008) Hydrogen peroxide scavenging rescues frataxin deficiency in a Drosophila model of Friedreich's ataxia. Proc. Natl. Acad. Sci. USA, 105, 611-616.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 611-616
    • Anderson, P.R.1    Kirby, K.2    Orr, W.C.3    Hilliker, A.J.4    Phillips, J.P.5
  • 38
    • 0038448961 scopus 로고    scopus 로고
    • Upregulation of expression from the FRDA genomic locus for the therapy of Friedreich ataxia
    • Sarsero, J.P., Li, L., Wardan, H., Sitte, K., Williamson, R. and Ioannou, P.A. (2003) Upregulation of expression from the FRDA genomic locus for the therapy of Friedreich ataxia. J. Gene Med., 5, 72-81.
    • (2003) J. Gene Med , vol.5 , pp. 72-81
    • Sarsero, J.P.1    Li, L.2    Wardan, H.3    Sitte, K.4    Williamson, R.5    Ioannou, P.A.6
  • 39
    • 34250223092 scopus 로고    scopus 로고
    • Hemin rescues adrenodoxin, heme a and cytochrome oxidase activity in frataxin-deficient oligodendroglioma cells
    • Napoli, E., Morin, D., Bernhardt, R., Buckpitt, A. and Cortopassi, G. (2007) Hemin rescues adrenodoxin, heme a and cytochrome oxidase activity in frataxin-deficient oligodendroglioma cells. Biochim. Biophys. Acta 1772, 773-780.
    • (2007) Biochim. Biophys. Acta , vol.1772 , pp. 773-780
    • Napoli, E.1    Morin, D.2    Bernhardt, R.3    Buckpitt, A.4    Cortopassi, G.5
  • 40
    • 38949197818 scopus 로고    scopus 로고
    • Redistribution of accumulated cell iron: A modality of chelation with therapeutic implications
    • Sohn, Y.S., Breuer, W., Munnich, A. and Cabantchik, Z.I. (2008) Redistribution of accumulated cell iron: A modality of chelation with therapeutic implications. Blood, 111, 1690-1699.
    • (2008) Blood , vol.111 , pp. 1690-1699
    • Sohn, Y.S.1    Breuer, W.2    Munnich, A.3    Cabantchik, Z.I.4
  • 41
    • 0034331239 scopus 로고    scopus 로고
    • Distinct iron-sulfur cluster assembly complexes exist in the cytosol and mitochondria of human cells
    • Tong, W.H. and Rouault T. (2000) Distinct iron-sulfur cluster assembly complexes exist in the cytosol and mitochondria of human cells. EMBO J., 19, 5692-5700.
    • (2000) EMBO J , vol.19 , pp. 5692-5700
    • Tong, W.H.1    Rouault, T.2
  • 42
    • 33744956665 scopus 로고    scopus 로고
    • Roles of the mammalian cytosolic cysteine desulfurase, ISCS, and scaffold protein, ISCU, in iron-sulfur cluster assembly
    • Li, K., Tong, W.H., Hughes, R.M. and Rouault T.A. (2006) Roles of the mammalian cytosolic cysteine desulfurase, ISCS, and scaffold protein, ISCU, in iron-sulfur cluster assembly. J. Biol. Chem., 281, 12344-12351.
    • (2006) J. Biol. Chem , vol.281 , pp. 12344-12351
    • Li, K.1    Tong, W.H.2    Hughes, R.M.3    Rouault, T.A.4
  • 43
    • 0033529554 scopus 로고    scopus 로고
    • Yeast and human frataxin are processed to mature form in two sequential steps by the mitochondrial processing peptidase
    • Branda, S.S., Cavadini, P., Adamec, J., Kalousek, F., Taroni, F. and Isaya, G. (1999) Yeast and human frataxin are processed to mature form in two sequential steps by the mitochondrial processing peptidase. J. Biol. Chem., 274, 22763-22769.
    • (1999) J. Biol. Chem , vol.274 , pp. 22763-22769
    • Branda, S.S.1    Cavadini, P.2    Adamec, J.3    Kalousek, F.4    Taroni, F.5    Isaya, G.6


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