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- Title
Pathological Roles of Wild-Type Cu, Zn-Superoxide Dismutase in Amyotrophic Lateral Sclerosis.
- Authors
Furukawa, Yoshiaki
- Abstract
Dominant mutations in a Cu, Zn-superoxide dismutase (SOD1) gene cause a familial form of amyotrophic lateral sclerosis (ALS). While it remains controversial how SOD1 mutations lead to onset and progression of the disease, many in vitro and in vivo studies have supported a gain-of-toxicity mechanism where pathogenic mutations contribute to destabilizing a native structure of SOD1 and thus facilitate misfolding and aggregation. Indeed, abnormal accumulation of SOD1-positive inclusions in spinal motor neurons is a pathological hallmark in SOD1-related familial ALS. Furthermore, similarities in clinical phenotypes and neuropathology of ALS cases with and withoutmutations in sod1 gene have implied a diseasemechanism involving SOD1 common to all ALS cases. Although pathogenic roles of wild-type SOD1 in sporadic ALS remain controversial, recent developments of novel SOD1 antibodies have made it possible to characterize wild-type SOD1 under pathological conditions of ALS. Here, I have briefly reviewed recent progress on biochemical and immunohistochemical characterization of wild-type SOD1 in sporadic ALS cases and discussed possible involvement of wild-type SOD1 in a pathomechanism of ALS.
- Subjects
PATHOLOGICAL psychology; SUPEROXIDE dismutase; GENETICS of amyotrophic lateral sclerosis; IN vitro studies; NEUROLOGICAL disorders; GENETIC mutation; IN vitro toxicity testing; PROTEIN folding
- Publication
Neurology Research International, 2012, p1
- ISSN
2090-1852
- Publication type
Article
- DOI
10.1155/2012/323261