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SOD1 mutation is assosiated with accumulation of neurofilaments in amyotrophic lateral scelaries
Author(s) -
Rouleau Guy A.,
Clark Arthur W.,
Rooke Karen,
Pramatarova Albena,
Krizus Aldis,
Suchowersky Oksana,
Julien JeanPierre,
Figlewicz Denise
Publication year - 1996
Publication title -
annals of neurology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.764
H-Index - 296
eISSN - 1531-8249
pISSN - 0364-5134
DOI - 10.1002/ana.410390119
Subject(s) - amyotrophic lateral sclerosis , sod1 , neurofilament , exon , pathogenesis , mutation , superoxide dismutase , genetically modified mouse , gene , biology , microbiology and biotechnology , genetics , medicine , transgene , disease , pathology , immunology , immunohistochemistry , endocrinology , oxidative stress
Mutations in the Cu/Zn superoxide dismutase (SODl) gene are found in 15 to 20% of patients with familial amyotrophic lateral sclerosis (FALS). Increased levels of neurofilament subunits in transgenic mouse models of ALS also suggests a key role for these proteins in the pathogenesis of the disease. We report the coexistence of an Ile 113 → Thr substitution in exon 4 of the SOD1 gene and marked neurofilamentous pathology in the same FALS patient. These observations suggest that two mechanisms, SOD 1‐induced toxicity and neurofilament disruption, are acting together.