title: Prion Properties of SOD1 in Amyotrophic Lateral Sclerosis and Potential Therapy.
abstract: Amyotrophic lateral sclerosis (ALS) is a devastating and rapidly progressive neurodegenerative disease caused by the deterioration of motor neurons. The first symptoms of ALS always begin at a focal but variable site and consistently spread to neighboring regions, suggesting that neurodegeneration in ALS is an orderly and propagating process. Like other neurodegenerative diseases, misfolding of a specific protein is central to ALS. SOD1, the major constituent of the protein deposits in some familial and sporadic forms of ALS, propagates its misfolded conformation like prions, providing a plausible molecular basis for the focality and spreading of muscle weakness in ALS. Because protein misfolding is a common cause of diverse neurodegenerative diseases, strategies aimed at boosting a cell's ability to cope with misfolded proteins could lead to therapeutics to combat these devastating age-related proteinopathies.
authors.affiliation: MRC Laboratory of Molecular Biology, Cambridge CB2 0QH, United Kingdom.
authors.forename: Caroline
authors.initials: C
authors.lastname: Sibilla
authors.affiliation: MRC Laboratory of Molecular Biology, Cambridge CB2 0QH, United Kingdom.
authors.forename: Anne
authors.initials: A
authors.lastname: Bertolotti
mesh_terms: D000690:Amyotrophic Lateral Sclerosis / Q000378:metabolism* / Q000628:therapy; D006801:Humans; D011328:Prions / Q000378:metabolism*; D000072105:Superoxide Dismutase-1 / Q000378:metabolism*
chemical_list: D011328:Prions; C000606290:SOD1 protein, human; D000072105:Superoxide Dismutase-1