Journal
JOURNAL OF THE NEUROLOGICAL SCIENCES
Volume 218, Issue 1-2, Pages 79-83Publisher
ELSEVIER
DOI: 10.1016/j.jns.2003.11.003
Keywords
amyotrophic lateral sclerosis (ALS); familial ALS (fALS); Cu/Zn superoxide dismutase (SOD1); missense mutation; genomic analysis; liquid chromatography-electrospray ionization-mass spectrometry (LC-ESI-MS)
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Amyotrophic lateral sclerosis (ALS) is a progressive neurodegenerative disorder affecting motor neurons. The majority of patients are sporadic cases, while 5-10% of the patients have a family history of ALS (fALS). Mutations in the gene that encodes cytoplasmic Cu/Zn superoxide dismutase (SOD1) have been identified in about 25% of fALS cases. Although the precise pathogenesis of ALS is still unknown, experimental studies including animal models suggest that fALS is caused by the toxic gain-of-function of the SOD1 mutant. We have analyzed not only SOD1 gene mutation by genomic sequencing, but also SOD1 mutant protein by liquid chromatography-electrospray ionization-mass spectrometry (LC-ESI-MS). We analyzed 33 fALS patients and found 10 mutations in SOD1 gene, in which two were novel: Asp101His substitution in exon 4 and Gly141Glu substitution in exon 5. Here, we present their mass spectrometric protein analyses and clinical features. (C) 2003 Elsevier B.V. All rights reserved.
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