Pandolfo M. Friedreich ataxia: the clinical picture. J Neurol. 2009;256 Suppl 1:3–8. ArticlePubMed Google Scholar
Rufini A, Fortuni S, Arcuri G, Condo I, Serio D, Incani O, et al. Preventing the ubiquitin–proteasome-dependent degradation of frataxin, the protein defective in Friedreich’s ataxia. Hum Mol Genet. 2011;20:1253–61. ArticlePubMedCAS Google Scholar
Pandolfo M, Pastore A. The pathogenesis of Friedreich ataxia and the structure and function of frataxin. J Neurol. 2009;256 Suppl 1:9–17. ArticlePubMedCAS Google Scholar
Calabrese V, Lodi R, Tonon C, D’Agata V, Sapienza M, Scapagnini G, et al. Oxidative stress, mitochondrial dysfunction and cellular stress response in Friedreich’s ataxia. J Neurol Sci. 2005;233:145–62. ArticlePubMedCAS Google Scholar
Koeppen AH, Davis AN, Morral JA. The cerebellar component of Friedreich’s ataxia. Acta Neuropathol. 2011;122:323–30. ArticlePubMed Google Scholar
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;11:217–27. ArticlePubMedCAS Google Scholar
Santos R, Lefevre S, Sliwa D, Seguin A, Camadro JM, Lesuisse E. Friedreich ataxia: molecular mechanisms, redox considerations, and therapeutic opportunities. Antioxid Redox Signal. 2010;13:651–90. ArticlePubMedCAS Google Scholar
Hausse AO, Aggoun Y, Bonnet D, Sidi D, Munnich A, Rotig A, et al. Idebenone and reduced cardiac hypertrophy in Friedreich’s ataxia. Heart. 2002;87:346–9. ArticlePubMedCAS Google Scholar
Kemp K, Mallam E, Hares K, Witherick J, Scolding N, Wilkins A. Mesenchymal stem cells restore frataxin expression and increase hydrogen peroxide scavenging enzymes in Friedreich ataxia fibroblasts. PLoS One. 2011;6:e26098. ArticlePubMedCAS Google Scholar
Kemp K, Gordon D, Wraith DC, Mallam E, Hartfield E, Uney J, et al. Fusion between human mesenchymal stem cells and rodent cerebellar Purkinje cells. Neuropathol Appl Neurobiol 2010;37:166–78. Google Scholar
Kemp K, Gray E, Mallam E, Scolding N, Wilkins A. Inflammatory cytokine induced regulation of superoxide dismutase 3 expression by human mesenchymal stem cells. Stem Cell Rev 2010;6:548–59. Google Scholar
Mallam E, Kemp K, Wilkins A, Rice C, Scolding N. Characterization of in vitro expanded bone marrow-derived mesenchymal stem cells from patients with multiple sclerosis. Mult Scler 2010;16:909–18. Google Scholar
Wilkins A, Kemp K, Ginty M, Hares K, Mallam E, Scolding N. Human bone marrow-derived mesenchymal stem cells secrete brain-derived neurotrophic factor which promotes neuronal survival in vitro. Stem Cell Res 2009;3:63–70. Google Scholar
Kemp K, Hares K, Mallam E, Heesom KJ, Scolding N, Wilkins A. Mesenchymal stem cell-secreted superoxide dismutase promotes cerebellar neuronal survival. J Neurochem. 2010;114:1569–80. ArticlePubMedCAS Google Scholar
Zelko IN, Mariani TJ, Folz RJ. Superoxide dismutase multigene family: a comparison of the CuZn-SOD (SOD1), Mn-SOD (SOD2), and EC-SOD (SOD3) gene structures, evolution, and expression. Free Radic Biol Med. 2002;33:337–49. ArticlePubMedCAS Google Scholar
Wilkins A, Compston A. Trophic factors attenuate nitric oxide mediated neuronal and axonal injury in vitro: roles and interactions of mitogen-activated protein kinase signalling pathways. J Neurochem. 2005;92:1487–96. ArticlePubMedCAS Google Scholar
Campuzano V, Montermini L, Lutz Y, Cova L, Hindelang C, Jiralerspong S, et al. Frataxin is reduced in Friedreich ataxia patients and is associated with mitochondrial membranes. Hum Mol Genet. 1997;6:1771–80. ArticlePubMedCAS Google Scholar
Koeppen AH. Friedreich’s ataxia: pathology, pathogenesis, and molecular genetics. J Neurol Sci. 2011;303:1–12. ArticlePubMedCAS Google Scholar
Pianese L, Turano M, Lo Casale MS, De Biase I, Giacchetti M, Monticelli A, et al. Real time PCR quantification of frataxin mRNA in the peripheral blood leucocytes of Friedreich ataxia patients and carriers. J Neurol Neurosurg Psychiatry. 2004;75:1061–3. ArticlePubMedCAS Google Scholar
Acquaviva F, Castaldo I, Filla A, Giacchetti M, Marmolino D, Monticelli A, et al. Recombinant human erythropoietin increases frataxin protein expression without increasing mRNA expression. Cerebellum. 2008;7:360–5. ArticlePubMedCAS Google Scholar
Herman D, Jenssen K, Burnett R, Soragni E, Perlman SL, Gottesfeld JM. Histone deacetylase inhibitors reverse gene silencing in Friedreich’s ataxia. Nat Chem Biol. 2006;2:551–8. ArticlePubMedCAS Google Scholar
Pook MA, Al-Mahdawi S, Carroll CJ, Cossee M, Puccio H, Lawrence L, et al. Rescue of the Friedreich’s ataxia knockout mouse by human YAC transgenesis. Neurogenetics. 2001;3:185–93. PubMedCAS Google Scholar
Kontoghiorghes GJ. Prospects for introducing deferiprone as potent pharmaceutical antioxidant. Front Biosci (Elite Ed). 2009;1:161–78. Google Scholar
Velasco-Sanchez D, Aracil A, Montero R, Mas A, Jimenez L, O’Callaghan M, et al. Combined therapy with idebenone and deferiprone in patients with Friedreich’s ataxia. Cerebellum. 2011;10:1–8. ArticlePubMedCAS Google Scholar
Sparaco M, Gaeta LM, Santorelli FM, Passarelli C, Tozzi G, Bertini E, et al. Friedreich’s ataxia: oxidative stress and cytoskeletal abnormalities. J Neurol Sci. 2009;287:111–8. ArticlePubMedCAS Google Scholar
Busi MV, Gomez-Casati DF. Exploring frataxin function. IUBMB Life 2012;64:56–63.
Armstrong JS, Khdour O, Hecht SM. Does oxidative stress contribute to the pathology of Friedreich’s ataxia? A radical question. FASEB J. 2010;24:2152–63. ArticlePubMedCAS Google Scholar
Michiels C, Raes M, Toussaint O, Remacle J. Importance of Se-glutathione peroxidase, catalase, and Cu/Zn-SOD for cell survival against oxidative stress. Free Radic Biol Med. 1994;17:235–48. ArticlePubMedCAS Google Scholar
Esposito LA, Kokoszka JE, Waymire KG, Cottrell B, MacGregor GR, Wallace DC. Mitochondrial oxidative stress in mice lacking the glutathione peroxidase-1 gene. Free Radic Biol Med. 2000;28:754–66. ArticlePubMedCAS Google Scholar
Beckman JS, Beckman TW, Chen J, Marshall PA, Freeman BA. Apparent hydroxyl radical production by peroxynitrite: implications for endothelial injury from nitric oxide and superoxide. Proc Natl Acad Sci USA. 1990;87:1620–4. ArticlePubMedCAS Google Scholar
Schulz JB, Dehmer T, Schols L, Mende H, Hardt C, Vorgerd M, et al. Oxidative stress in patients with Friedreich ataxia. Neurology. 2000;55:1719–21. ArticlePubMedCAS Google Scholar
Garcia-Gimenez JL, Gimeno A, Gonzalez-Cabo P, Dasi F, Bolinches-Amoros A, Molla B, et al. Differential expression of PGC-1alpha and metabolic sensors suggest age-dependent induction of mitochondrial biogenesis in Friedreich ataxia fibroblasts. PLoS One. 2011;6:e20666. ArticlePubMedCAS Google Scholar
Chantrel-Groussard K, Geromel V, Puccio H, Koenig M, Munnich A, Rotig A, et al. Disabled early recruitment of antioxidant defenses in Friedreich’s ataxia. Hum Mol Genet. 2001;10:2061–7. ArticlePubMedCAS Google Scholar
Seznec H, Simon D, Bouton C, Reutenauer L, Hertzog A, Golik P, et al. Friedreich ataxia: the oxidative stress paradox. Hum Mol Genet. 2005;14:463–74. ArticlePubMedCAS Google Scholar
Irazusta V, Obis E, Moreno-Cermeno A, Cabiscol E, Ros J, Tamarit J. Yeast frataxin mutants display decreased superoxide dismutase activity crucial to promote protein oxidative damage. Free Radic Biol Med. 2010;48:411–20. ArticlePubMedCAS Google Scholar
Paupe V, Dassa EP, Goncalves S, Auchere F, Lonn M, Holmgren A, et al. Impaired nuclear Nrf2 translocation undermines the oxidative stress response in Friedreich ataxia. PLoS One. 2009;4:e4253. ArticlePubMed Google Scholar
Irazusta V, Cabiscol E, Reverter-Branchat G, Ros J, Tamarit J. Manganese is the link between frataxin and iron-sulfur deficiency in the yeast model of Friedreich ataxia. J Biol Chem. 2006;281:12227–32. ArticlePubMedCAS Google Scholar
Foury F, Cazzalini O. Deletion of the yeast homologue of the human gene associated with Friedreich’s ataxia elicits iron accumulation in mitochondria. FEBS Lett. 1997;411:373–7. ArticlePubMedCAS Google Scholar
Wong A, Yang J, Cavadini P, Gellera C, Lonnerdal B, Taroni F, et al. 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. 1999;8:425–30. ArticlePubMedCAS Google Scholar
Finocchietto PV, Franco MC, Holod S, Gonzalez AS, Converso DP, Antico Arciuch VG, et al. Mitochondrial nitric oxide synthase: a masterpiece of metabolic adaptation, cell growth, transformation, and death. Exp Biol Med (Maywood). 2009;234:1020–8. ArticleCAS Google Scholar
Bayot A, Santos R, Camadro JM, Rustin P. Friedreich’s ataxia: the vicious circle hypothesis revisited. BMC Med. 2011;9:112. ArticlePubMedCAS Google Scholar
Napoli E, Taroni F, Cortopassi GA. Frataxin, iron–sulfur clusters, heme, ROS, and aging. Antioxid Redox Signal. 2006;8:506–16. ArticlePubMedCAS Google Scholar
Kaplan DR, Miller FD. Neurotrophin signal transduction in the nervous system. Curr Opin Neurobiol. 2000;10:381–91. ArticlePubMedCAS Google Scholar
Goldberg JL, Barres BA. The relationship between neuronal survival and regeneration. Annu Rev Neurosci. 2000;23:579–612. ArticlePubMedCAS Google Scholar
Song G, Ouyang G, Bao S. The activation of Akt/PKB signaling pathway and cell survival. J Cell Mol Med. 2005;9:59–71. ArticlePubMedCAS Google Scholar
Klesse LJ, Parada LF. p21 ras and phosphatidylinositol-3 kinase are required for survival of wild-type and NF1 mutant sensory neurons. J Neurosci. 1998;18:10420–8. PubMedCAS Google Scholar
Diem R, Meyer R, Weishaupt JH, Bahr M. Reduction of potassium currents and phosphatidylinositol 3-kinase-dependent AKT phosphorylation by tumor necrosis factor-(alpha) rescues axotomized retinal ganglion cells from retrograde cell death in vivo. J Neurosci. 2001;21:2058–66. PubMedCAS Google Scholar
Encinas M, Tansey MG, Tsui-Pierchala BA, Comella JX, Milbrandt J, Johnson Jr EM. c-Src is required for glial cell line-derived neurotrophic factor (GDNF) family ligand-mediated neuronal survival via a phosphatidylinositol-3 kinase (PI-3K)-dependent pathway. J Neurosci. 2001;21:1464–72. PubMedCAS Google Scholar
Crowder RJ, Freeman RS. Phosphatidylinositol 3-kinase and Akt protein kinase are necessary and sufficient for the survival of nerve growth factor-dependent sympathetic neurons. J Neurosci. 1998;18:2933–43. PubMedCAS Google Scholar
Vaillant AR, Mazzoni I, Tudan C, Boudreau M, Kaplan DR, Miller FD. Depolarization and neurotrophins converge on the phosphatidylinositol 3-kinase-Akt pathway to synergistically regulate neuronal survival. J Cell Biol. 1999;146:955–66. ArticlePubMedCAS Google Scholar
Asada S, Daitoku H, Matsuzaki H, Saito T, Sudo T, Mukai H, et al. Mitogen-activated protein kinases, Erk and p38, phosphorylate and regulate Foxo1. Cell Signal. 2007;19:519–27. ArticlePubMedCAS Google Scholar
Chen RW, Lu XC, Yao C, Liao Z, Jiang ZG, Wei H, et al. PAN-811 provides neuroprotection against glutamate toxicity by suppressing activation of JNK and p38 MAPK. Neurosci Lett. 2007;422:64–7. ArticlePubMedCAS Google Scholar
Yamagishi S, Matsumoto T, Yokomaku D, Hatanaka H, Shimoke K, Yamada M, et al. Comparison of inhibitory effects of brain-derived neurotrophic factor and insulin-like growth factor on low potassium-induced apoptosis and activation of p38 MAPK and c-Jun in cultured cerebellar granule neurons. Brain Res Mol Brain Res. 2003;119:184–91. ArticlePubMedCAS Google Scholar