title: Oxidative stress and mitochondrial damage in the pathogenesis of ALS: New perspectives.
abstract: This review attempts to reconcile the present dual view of the mechanisms operating in Amyotrophic Lateral Sclerosis (ALS). On one side, oxidative stress, mitochondrial damage and protein aggregation are considered as causative of the disease, as strongly supported by evidence obtained in models based on the expression of ALS-typical mutant SOD1. On the other hand, evidence from models expressing ALS-typical mutations in RNA-binding proteins such as FUS and TDP43 indicate that mRNA (dys)metabolism is a major pathway in this disease. A critical analysis of existing literature suggests that there may be more than one point of intersection.
authors.affiliation: Department of Biology, University of Rome Tor Vergata, 00133 Rome, Italy; Fondazione Santa Lucia IRCCS, c/o CERC, 00143 Rome, Italy.
authors.forename: F
authors.initials: F
authors.lastname: Bozzo
authors.affiliation: Department of Biology, University of Rome Tor Vergata, 00133 Rome, Italy; Fondazione Santa Lucia IRCCS, c/o CERC, 00143 Rome, Italy.
authors.forename: A
authors.initials: A
authors.lastname: Mirra
authors.affiliation: Department of Biology, University of Rome Tor Vergata, 00133 Rome, Italy; Fondazione Santa Lucia IRCCS, c/o CERC, 00143 Rome, Italy. Electronic address: carri@Bio.uniroma2.it.
authors.forename: M T
authors.initials: MT
authors.lastname: Carrì
mesh_terms: D000690:Amyotrophic Lateral Sclerosis / Q000378:metabolism*; D000818:Animals; D006801:Humans; D007501:Iron / Q000378:metabolism; D008928:Mitochondria / Q000378:metabolism*; D009154:Mutation; D018384:Oxidative Stress; D066263:Protein Aggregation, Pathological / Q000378:metabolism; D017510:Protein Folding; D012313:RNA / Q000378:metabolism; D016601:RNA-Binding Proteins / Q000235:genetics / Q000378:metabolism
chemical_list: D016601:RNA-Binding Proteins; D012313:RNA; D007501:Iron
keywords: ALS; FUS/TLS; Iron; Mitochondria; Oxidative stress; RNA metabolism; SOD1; TDP43