Zhao G, Bou-Abdallah F, Yang X et al (2001) Is hydrogen peroxide produced during iron(II) oxidation in mammalian apoferritins. īehera RK, Theil EC (2014) Moving Fe2+from ferritin ion channels to catalytic OH centers depends on conserved protein cage carboxylates. Levi S, Santambrogio P, Cozzi A, Rovida E, Corsi B, Tamborini E, Spada S, Albertini A, Arosio P (1994) The Role of the L-chain in ferritin iron incorporation. Santambrogio P, Levi S, Arosio P, Palagi L, Vecchio G, Lawson DM, Yewdall SJ, Artymiuk PJ et al (1992) Evidence that a salt bridge in the light chain contributes to the physical stability difference between heavy and light human ferritins. Sun S, Chasteen ND, Arosio P, Levi S (1993) Ferroxidase kinetics of human liver apoferritin, recombinant H-chain apoferritin, and site-directed mutants. Lawson DM, Treffry A, Artymiuk PJ et al (1989) Identification of the ferroxidase centre in ferritin. Wade VJ, Levi S, Arosio P et al (1991) Influence of site-directed modifications on the formation of iron cores in ferritin. Levi S, Luzzago A, Cesareni G, Cozzi A, Franceschinelli F, Albertini A, Arosio P (1988) Mechanism of ferritin iron uptake: activity of the H-chain and deletion mapping of the ferro-oxidase site. Levi S, Arosio P (2004) Mitochondrial ferritin. Santambrogio P, Biasiotto G, Sanvito F, Olivieri S, Arosio P, Levi S (2007) Mitochondrial ferritin expression in adult mouse tissues. Levi S, Corsi B, Bosisio M, Invernizzi R, Volz A, Sanford D, Arosio P, Drysdale J (2001) A human mitochondrial ferritin encoded by an intronless gene. Harrison PM, Arosio P (1996) The ferritins: molecular properties, iron storage function and cellular regulation. Biochim Biophys Acta Gen Subj 1800:783–792. Īrosio P, Levi S (2010) Cytosolic and mitochondrial ferritins in the regulation of cellular iron homeostasis and oxidative damage.
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McNeill A, Chinnery PF (2012) Neuroferritinopathy: update on clinical features and pathogenesis. Levi S, Tiranti V (2019) Neurodegeneration with brain iron accumulation disorders: valuable models aimed at understanding the pathogenesis of Iron deposition. ĭi Meo I, Tiranti V (2018) Classification and molecular pathogenesis of NBIA syndromes. ĭusek P, Schneider SA (2012) Neurodegeneration with brain iron accumulation. Kruer MC, Boddaert N, Schneider A, Houlden H, Bhatia KP, Gregory A, Anderson JC, Rooney WD, Hogarth P, Hayflick SJ (2012) Neuroimaging features of neurodegeneration with brain iron accumulation. Gregory A, Hayflick SJ (2011) Genetics of neurodegeneration with brain iron accumulation.
Levi S, Rovida E (2015) Neuroferritinopathy: From ferritin structure modification to pathogenetic mechanism. Levi S, Girelli D, Perrone F, Pasti M, Beaumont C, Corrocher R, Albertini A, Arosio P (1998) Analysis of ferritins in lymphoblastoid cell lines and in the lens of subjects with hereditary hyperferritinemia-cataract syndrome. Here, we will review the clinical and neurological features of neuroferritinopathy and summarize biochemical studies and data from cellular and animal models to propose a pathogenic mechanism of the disorder.Ĭurtis ARJ, Fey C, Morris CM, Bindoff LA, Ince PG, Chinnery PF, Coulthard A, Jackson MJ et al (2001) Mutation in the gene encoding ferritin light polypeptide causes dominant adult-onset basal ganglia disease. Second, neuroferritinopathy shows the characteristic signs of an accelerated process of aging thus, it can be considered an interesting model to study the progress of aging. First, neuroferritinopathy displays features also found in a larger group of disorders named Neurodegeneration with Brain Iron Accumulation (NBIA), such as iron deposition in the basal ganglia and extrapyramidal symptoms thus, the elucidation of its pathogenic mechanism may contribute to clarifying the incompletely understood aspects of NBIA. Although very rare, the disorder is notable for two reasons. This form of iron has detrimental effects on cells, particularly severe for neuronal cells, which are highly sensitive to oxidative stress.
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Neuroferritinopathy is a rare autosomal dominant inherited movement disorder caused by alteration of the L-ferritin gene that results in the production of a ferritin molecule that is unable to properly manage iron, leading to the presence of free redox-active iron in the cytosol.
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