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Volumn 7, Issue 5, 2016, Pages

Mitochondrial energy imbalance and lipid peroxidation cause cell death in friedreich’s ataxia

Author keywords

[No Author keywords available]

Indexed keywords

FRATAXIN; GLUTATHIONE; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); SUCCINATE DEHYDROGENASE (UBIQUINONE); IRON; IRON BINDING PROTEIN; UBIQUINOL CYTOCHROME C REDUCTASE;

EID: 85017618880     PISSN: None     EISSN: 20414889     Source Type: Journal    
DOI: 10.1038/cddis.2016.111     Document Type: Article
Times cited : (101)

References (53)
  • 1
    • 0019782799 scopus 로고
    • Friedreich's ataxia: A clinical and genetic study of 90 families with an analysis of early diagnostic criteria and intrafamilial clustering of clinical features
    • Harding AE. Friedreich's ataxia: a clinical and genetic study of 90 families with an analysis of early diagnostic criteria and intrafamilial clustering of clinical features. Brain 1981; 104: 589–620.
    • (1981) Brain , vol.104 , pp. 589-620
    • Harding, A.E.1
  • 2
    • 84880341003 scopus 로고    scopus 로고
    • Clinical features of Friedreich's ataxia: Classical and atypical phenotypes
    • Parkinson MH, Boesch S, Nachbauer W, Mariotti C, Giunti P. Clinical features of Friedreich's ataxia: classical and atypical phenotypes. J Neurochem 2013; 126: 103–117.
    • (2013) J Neurochem , vol.126 , pp. 103-117
    • Parkinson, M.H.1    Boesch, S.2    Nachbauer, W.3    Mariotti, C.4    Giunti, P.5
  • 3
    • 13344270899 scopus 로고    scopus 로고
    • Friedreich's ataxia: Autosomal recessive disease caused by an intronic GAA triplet repeat expansion
    • Campuzano V, Montermini L, Molto MD, Pianese L, Cossee M, Cavalcanti F et al. Friedreich's ataxia: autosomal recessive disease caused by an intronic GAA triplet repeat expansion. Science 1996; 271: 1423–1427.
    • (1996) Science , vol.271 , pp. 1423-1427
    • Campuzano, V.1    Montermini, L.2    Molto, M.D.3    Pianese, L.4    Cossee, M.5    Cavalcanti, F.6
  • 4
    • 62549093116 scopus 로고    scopus 로고
    • The pathogenesis of Friedreich ataxia and the structure and function of frataxin
    • Pandolfo M, Pastore A. The pathogenesis of Friedreich ataxia and the structure and function of frataxin. J Neurol 2009; 256: 9–17.
    • (2009) J Neurol , vol.256 , pp. 9-17
    • Pandolfo, M.1    Pastore, A.2
  • 5
    • 84880857530 scopus 로고    scopus 로고
    • Neurodegeneration in Friedreich's ataxia: From defective frataxin to oxidative stress
    • Gomes CM, Santos R. Neurodegeneration in Friedreich's ataxia: from defective frataxin to oxidative stress. Oxid Med Cell Longev 2013; 2013: 487534.
    • (2013) Oxid Med Cell Longev , vol.2013
    • Gomes, C.M.1    Santos, R.2
  • 6
    • 0014253874 scopus 로고
    • Histologic and teased-fiber measurements of sural nerve in disorders of lower motor and primary sensory neurons
    • Dyck PJ, Gutrecht JA, Bastron JA, Karnes WE, Dale AJ. Histologic and teased-fiber measurements of sural nerve in disorders of lower motor and primary sensory neurons. Mayo Clin Proc 1968; 43: 81–123.
    • (1968) Mayo Clin Proc , vol.43 , pp. 81-123
    • Dyck, P.J.1    Gutrecht, J.A.2    Bastron, J.A.3    Karnes, W.E.4    Dale, A.J.5
  • 8
    • 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, Cossee M, Criqui-Filipe P, Tiziano F, Melki J et al. Mouse models for Friedreich ataxia exhibit cardiomyopathy, sensory nerve defect and Fe-S enzyme deficiency followed by intramitochondrial iron deposits. Nat Genet 2001; 27: 181–186.
    • (2001) Nat Genet , vol.27 , pp. 181-186
    • Puccio, H.1    Simon, D.2    Cossee, M.3    Criqui-Filipe, P.4    Tiziano, F.5    Melki, J.6
  • 10
    • 33845652267 scopus 로고    scopus 로고
    • The GAA triplet-repeat is unstable in the context of the human FXN locus and displays age-dependent expansions in cerebellum and DRG in a transgenic mouse model
    • Clark RM, De B I, Malykhina AP, Al-Mahdawi S, Pook M, Bidichandani SI. The GAA triplet-repeat is unstable in the context of the human FXN locus and displays age-dependent expansions in cerebellum and DRG in a transgenic mouse model. Hum Genet 2007; 120: 633–640.
    • (2007) Hum Genet , vol.120 , pp. 633-640
    • Clark, R.M.1    De, B.I.2    Malykhina, A.P.3    Al-Mahdawi, S.4    Pook, M.5    Bidichandani, S.I.6
  • 12
    • 34249988198 scopus 로고    scopus 로고
    • Somatic instability of the expanded GAA triplet-repeat sequence in Friedreich ataxia progresses throughout life
    • De BI, Rasmussen A, Monticelli A, Al-Mahdawi S, Pook M, Cocozza S et al. Somatic instability of the expanded GAA triplet-repeat sequence in Friedreich ataxia progresses throughout life. Genomics 2007; 90: 1–5.
    • (2007) Genomics , vol.90 , pp. 1-5
    • De, B.I.1    Rasmussen, A.2    Monticelli, A.3    Al-Mahdawi, S.4    Pook, M.5    Cocozza, S.6
  • 14
    • 33749638768 scopus 로고    scopus 로고
    • GAA repeat expansion mutation mouse models of Friedreich ataxia exhibit oxidative stress leading to progressive neuronal and cardiac pathology
    • Al-Mahdawi S, Pinto RM, Varshney D, Lawrence L, Lowrie MB, Hughes S et al. GAA repeat expansion mutation mouse models of Friedreich ataxia exhibit oxidative stress leading to progressive neuronal and cardiac pathology. Genomics 2006; 88: 580–590.
    • (2006) Genomics , vol.88 , pp. 580-590
    • Al-Mahdawi, S.1    Pinto, R.M.2    Varshney, D.3    Lawrence, L.4    Lowrie, M.B.5    Hughes, S.6
  • 15
    • 39749136603 scopus 로고    scopus 로고
    • The Friedreich ataxia GAA repeat expansion mutation induces comparable epigenetic changes in human and transgenic mouse brain and heart tissues
    • Al-Mahdawi S, Pinto RM, Ismail O, Varshney D, Lymperi S, Sandi C et al. The Friedreich ataxia GAA repeat expansion mutation induces comparable epigenetic changes in human and transgenic mouse brain and heart tissues. Hum Mol Genet 2008; 17: 735–746.
    • (2008) Hum Mol Genet , vol.17 , pp. 735-746
    • Al-Mahdawi, S.1    Pinto, R.M.2    Ismail, O.3    Varshney, D.4    Lymperi, S.5    Sandi, C.6
  • 16
    • 80054692642 scopus 로고    scopus 로고
    • The cerebellar component of Friedreich's ataxia
    • Koeppen AH, Davis AN, Morral JA. The cerebellar component of Friedreich's ataxia. Acta Neuropathol 2011; 122: 323–330.
    • (2011) Acta Neuropathol , vol.122 , pp. 323-330
    • Koeppen, A.H.1    Davis, A.N.2    Morral, J.A.3
  • 19
    • 1442324707 scopus 로고    scopus 로고
    • Friedreich ataxia mouse models with progressive cerebellar and sensory ataxia reveal autophagic neurodegeneration in dorsal root ganglia
    • Simon D, Seznec H, Gansmuller A, Carelle N, Weber P, Metzger D et al. Friedreich ataxia mouse models with progressive cerebellar and sensory ataxia reveal autophagic neurodegeneration in dorsal root ganglia. J Neurosci 2004; 24: 1987–1995.
    • (2004) J Neurosci , vol.24 , pp. 1987-1995
    • Simon, D.1    Seznec, H.2    Gansmuller, A.3    Carelle, N.4    Weber, P.5    Metzger, D.6
  • 20
    • 0036472291 scopus 로고    scopus 로고
    • Assembly and iron-binding properties of human frataxin, the protein deficient in Friedreich ataxia
    • Cavadini P, O'Neill HA, Benada O, Isaya G. Assembly and iron-binding properties of human frataxin, the protein deficient in Friedreich ataxia. Hum Mol Genet 2002; 11: 217–227.
    • (2002) Hum Mol Genet , vol.11 , pp. 217-227
    • Cavadini, P.1    O'neill, H.A.2    Benada, O.3    Isaya, G.4
  • 22
    • 0031253821 scopus 로고    scopus 로고
    • Aconitase and mitochondrial iron-sulphur protein deficiency in Friedreich ataxia
    • Rotig A, de LP, Chretien D, Foury F, Koenig M, Sidi D et al. Aconitase and mitochondrial iron-sulphur protein deficiency in Friedreich ataxia. Nat Genet 1997; 17: 215–217.
    • (1997) Nat Genet , vol.17 , pp. 215-217
    • Rotig, A.1    De, L.P.2    Chretien, D.3    Foury, F.4    Koenig, M.5    Sidi, D.6
  • 23
    • 45549108453 scopus 로고    scopus 로고
    • Regulation of mitochondrial structure and function by the F1Fo-ATPase inhibitor protein, IF1
    • Campanella M, Casswell E, Chong S, Farah Z, Wieckowski MR, Abramov AY et al. Regulation of mitochondrial structure and function by the F1Fo-ATPase inhibitor protein, IF1. Cell Metab 2008; 8: 13–25.
    • (2008) Cell Metab , vol.8 , pp. 13-25
    • Campanella, M.1    Casswell, E.2    Chong, S.3    Farah, Z.4    Wieckowski, M.R.5    Abramov, A.Y.6
  • 24
    • 0030059871 scopus 로고    scopus 로고
    • Energy metabolism of adult astrocytes in vitro
    • Peuchen S, Duchen MR, Clark JB. Energy metabolism of adult astrocytes in vitro. Neuroscience 1996; 71: 855–870.
    • (1996) Neuroscience , vol.71 , pp. 855-870
    • Peuchen, S.1    Duchen, M.R.2    Clark, J.B.3
  • 25
    • 79955598457 scopus 로고    scopus 로고
    • Mitochondrial H2O2 generated from electron transport chain complex I stimulates muscle differentiation
    • Lee S, Tak E, Lee J, Rashid MA, Murphy MP, Ha J et al. Mitochondrial H2O2 generated from electron transport chain complex I stimulates muscle differentiation. Cell Res 2011; 21: 817–834.
    • (2011) Cell Res , vol.21 , pp. 817-834
    • Lee, S.1    Tak, E.2    Lee, J.3    Rashid, M.A.4    Murphy, M.P.5    Ha, J.6
  • 26
    • 58249093939 scopus 로고    scopus 로고
    • How mitochondria produce reactive oxygen species
    • Murphy MP. How mitochondria produce reactive oxygen species. Biochem J 2009; 417: 1–13.
    • (2009) Biochem J , vol.417 , pp. 1-13
    • Murphy, M.P.1
  • 28
    • 84864423521 scopus 로고    scopus 로고
    • Small amounts of isotope-reinforced polyunsaturated fatty acids suppress lipid autoxidation
    • Hill S, Lamberson CR, Xu L, To R, Tsui HS, Shmanai VV et al. Small amounts of isotope-reinforced polyunsaturated fatty acids suppress lipid autoxidation. Free Radic Biol Med 2012; 53: 893–906.
    • (2012) Free Radic Biol Med , vol.53 , pp. 893-906
    • Hill, S.1    Lamberson, C.R.2    Xu, L.3    To, R.4    Tsui, H.S.5    Shmanai, V.V.6
  • 31
    • 79957871035 scopus 로고    scopus 로고
    • Beta-amyloid activates PARP causing astrocytic metabolic failure and neuronal death
    • Abeti R, Abramov AY, Duchen MR. Beta-amyloid activates PARP causing astrocytic metabolic failure and neuronal death. Brain 2011; 134: 1658–1672.
    • (2011) Brain , vol.134 , pp. 1658-1672
    • Abeti, R.1    Abramov, A.Y.2    Duchen, M.R.3
  • 32
    • 84877795435 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase-1-induced NAD(+) depletion promotes nuclear factor-kappaB transcriptional activity by preventing p65 deacetylation
    • Kauppinen TM, Gan L, Swanson RA. Poly(ADP-ribose) polymerase-1-induced NAD(+) depletion promotes nuclear factor-kappaB transcriptional activity by preventing p65 deacetylation. Biochim Biophys Acta 2013; 1833: 1985–1991.
    • (2013) Biochim Biophys Acta , vol.1833 , pp. 1985-1991
    • Kauppinen, T.M.1    Gan, L.2    Swanson, R.A.3
  • 33
    • 84860003699 scopus 로고    scopus 로고
    • Friedreich's ataxia reveals a mechanism for coordinate regulation of oxidative metabolism via feedback inhibition of the SIRT3 deacetylase
    • Wagner GR, Pride PM, Babbey CM, Payne RM. Friedreich's ataxia reveals a mechanism for coordinate regulation of oxidative metabolism via feedback inhibition of the SIRT3 deacetylase. Hum Mol Genet 2012; 21: 2688–2697.
    • (2012) Hum Mol Genet , vol.21 , pp. 2688-2697
    • Wagner, G.R.1    Pride, P.M.2    Babbey, C.M.3    Payne, R.M.4
  • 34
    • 77949887506 scopus 로고    scopus 로고
    • Mammalian sirtuins: Biological insights and disease relevance
    • Haigis MC, Sinclair DA. Mammalian sirtuins: biological insights and disease relevance. Annu Rev Pathol 2010; 5: 253–295.
    • (2010) Annu Rev Pathol , vol.5 , pp. 253-295
    • Haigis, M.C.1    Sinclair, D.A.2
  • 36
    • 61449195068 scopus 로고    scopus 로고
    • Qualitative determination of superoxide release at both sides of the mitochondrial inner membrane by capillary electrophoretic analysis of the oxidation products of triphenylphosphonium hydroethidine
    • Xu X, Arriaga EA. Qualitative determination of superoxide release at both sides of the mitochondrial inner membrane by capillary electrophoretic analysis of the oxidation products of triphenylphosphonium hydroethidine. Free Radic Biol Med 2009; 46: 905–913.
    • (2009) Free Radic Biol Med , vol.46 , pp. 905-913
    • Xu, X.1    Arriaga, E.A.2
  • 37
    • 50849135137 scopus 로고    scopus 로고
    • Glutathione-dependent redox status of frataxin-deficient cells in a yeast model of Friedreich's ataxia
    • Auchere F, Santos R, Planamente S, Lesuisse E, Camadro JM. Glutathione-dependent redox status of frataxin-deficient cells in a yeast model of Friedreich's ataxia. Hum Mol Genet 2008; 17: 2790–2802.
    • (2008) Hum Mol Genet , vol.17 , pp. 2790-2802
    • Auchere, F.1    Santos, R.2    Planamente, S.3    Lesuisse, E.4    Camadro, J.M.5
  • 38
    • 83255165402 scopus 로고    scopus 로고
    • Changes in mitochondrial glutathione levels and protein thiol oxidation in yfh1 yeast cells and the lymphoblasts of patients with Friedreich's ataxia
    • Bulteau AL, Planamente S, Jornea L, Dur A, Lesuisse E, Camadro JM et al. Changes in mitochondrial glutathione levels and protein thiol oxidation in yfh1 yeast cells and the lymphoblasts of patients with Friedreich's ataxia. Biochim Biophys Acta 2012; 1822: 212–225.
    • (2012) Biochim Biophys Acta , vol.1822 , pp. 212-225
    • Bulteau, A.L.1    Planamente, S.2    Jornea, L.3    Dur, A.4    Lesuisse, E.5    Camadro, J.M.6
  • 39
    • 34848917624 scopus 로고    scopus 로고
    • Mitochondrial effects of lipid-derived neurotoxins
    • Picklo MJ Sr., Montine TJ. Mitochondrial effects of lipid-derived neurotoxins. J Alzheimers Dis 2007; 12: 185–193.
    • (2007) J Alzheimers Dis , vol.12 , pp. 185-193
    • Picklo, M.J.1    Montine, T.J.2
  • 41
    • 84938099619 scopus 로고    scopus 로고
    • Targeting lipid peroxidation and mitochondrial imbalance in Friedreich's ataxia
    • Abeti R, Uzun E, Renganathan I, Honda T, Pook MA, Giunti P. Targeting lipid peroxidation and mitochondrial imbalance in Friedreich's ataxia. Pharmacol Res 2015; 99: 344–350.
    • (2015) Pharmacol Res , vol.99 , pp. 344-350
    • Abeti, R.1    Uzun, E.2    Renganathan, I.3    Honda, T.4    Pook, M.A.5    Giunti, P.6
  • 42
    • 81855176066 scopus 로고    scopus 로고
    • Sulforaphane inhibits mitochondrial permeability transition and oxidative stress
    • Greco T, Shafer J, Fiskum G. Sulforaphane inhibits mitochondrial permeability transition and oxidative stress. Free Radic Biol Med 2011; 51: 2164–2171.
    • (2011) Free Radic Biol Med , vol.51 , pp. 2164-2171
    • Greco, T.1    Shafer, J.2    Fiskum, G.3
  • 43
    • 84964999321 scopus 로고    scopus 로고
    • Nrf2 impacts cellular bioenergetics by controlling substrate availability for mitochondrial respiration
    • Holmstrom KM, Baird L, Zhang Y, Hargreaves I, Chalasani A, Land JM et al. Nrf2 impacts cellular bioenergetics by controlling substrate availability for mitochondrial respiration. Biol Open 2013; 2: 761–770.
    • (2013) Biol Open , vol.2 , pp. 761-770
    • Holmstrom, K.M.1    Baird, L.2    Zhang, Y.3    Hargreaves, I.4    Chalasani, A.5    Land, J.M.6
  • 47
    • 0029888017 scopus 로고    scopus 로고
    • Beta 25-35 alters calcium homeostasis and induces neurotoxicity in cerebellar granule cells
    • Scorziello A, Meucci O, Florio T, Fattore M, Forloni G, Salmona M et al. Beta 25-35 alters calcium homeostasis and induces neurotoxicity in cerebellar granule cells. J Neurochem 1996; 66: 1995–2003.
    • (1996) J Neurochem , vol.66 , pp. 1995-2003
    • Scorziello, A.1    Meucci, O.2    Florio, T.3    Fattore, M.4    Forloni, G.5    Salmona, M.6
  • 48
    • 0037286364 scopus 로고    scopus 로고
    • Imaging mitochondrial function in intact cells
    • Duchen MR, Surin A, Jacobson J. Imaging mitochondrial function in intact cells. Methods Enzymol 2003; 361: 353–389.
    • (2003) Methods Enzymol , vol.361 , pp. 353-389
    • Duchen, M.R.1    Surin, A.2    Jacobson, J.3
  • 49
    • 0014578265 scopus 로고
    • The kinetic properties of citrate synthase from rat liver mitochondria
    • Shepherd D, Garland PB. The kinetic properties of citrate synthase from rat liver mitochondria. Biochem J 1969; 114: 597–610.
    • (1969) Biochem J , vol.114 , pp. 597-610
    • Shepherd, D.1    Garland, P.B.2
  • 50
    • 84872599257 scopus 로고    scopus 로고
    • Human neuronal coenzyme Q10 deficiency results in global loss of mitochondrial respiratory chain activity, increased mitochondrial oxidative stress and reversal of ATP synthase activity: Implications for pathogenesis and treatment
    • Duberley KE, Abramov AY, Chalasani A, Heales SJ, Rahman S, Hargreaves IP. Human neuronal coenzyme Q10 deficiency results in global loss of mitochondrial respiratory chain activity, increased mitochondrial oxidative stress and reversal of ATP synthase activity: implications for pathogenesis and treatment. J Inherit Metab Dis 2013; 36: 63–73.
    • (2013) J Inherit Metab Dis , vol.36 , pp. 63-73
    • Duberley, K.E.1    Abramov, A.Y.2    Chalasani, A.3    Heales, S.J.4    Rahman, S.5    Hargreaves, I.P.6
  • 51
    • 33846818524 scopus 로고    scopus 로고
    • Three distinct mechanisms generate oxygen free radicals in neurons and contribute to cell death during anoxia and reoxygenation
    • Abramov AY, Scorziello A, Duchen MR. Three distinct mechanisms generate oxygen free radicals in neurons and contribute to cell death during anoxia and reoxygenation. J Neurosci 2007; 27: 1129–1138.
    • (2007) J Neurosci , vol.27 , pp. 1129-1138
    • Abramov, A.Y.1    Scorziello, A.2    Duchen, M.R.3
  • 52
    • 0035577283 scopus 로고    scopus 로고
    • Quantitative imaging of glutathione in hippocampal neurons and glia in culture using monochlorobimane
    • Keelan J, Allen NJ, Antcliffe D, Pal S, Duchen MR. Quantitative imaging of glutathione in hippocampal neurons and glia in culture using monochlorobimane. J Neurosci Res 2001; 66: 873–884.
    • (2001) J Neurosci Res , vol.66 , pp. 873-884
    • Keelan, J.1    Allen, N.J.2    Antcliffe, D.3    Pal, S.4    Duchen, M.R.5
  • 53
    • 1642499152 scopus 로고    scopus 로고
    • Beta-amyloid peptides induce mitochondrial dysfunction and oxidative stress in astrocytes and death of neurons through activation of NADPH oxidase
    • Abramov AY, Canevari L, Duchen MR. Beta-amyloid peptides induce mitochondrial dysfunction and oxidative stress in astrocytes and death of neurons through activation of NADPH oxidase. J Neurosci 2004; 24: 565–575.
    • (2004) J Neurosci , vol.24 , pp. 565-575
    • Abramov, A.Y.1    Canevari, L.2    Duchen, M.R.3


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