Amyotrophic lateral sclerosis linked to a novel SOD1 mutation with muscle mitochondrial dysfunction

Stefania Corti, Chiara Donadoni, Dario Ronchi, Andreina Bordoni, Francesco Fortunato, Domenico Santoro, Roberto Del Bo, Valeria Lucchini, Veronica Crugnola, Dimitra Papadimitriou, Sabrina Salani, Maurizio Moggio, Nereo Bresolin, Giacomo P. Comi

Research output: Contribution to journalArticlepeer-review


Amyotrophic lateral sclerosis (ALS) is a fatal neurodegenerative motor neuron disorder. Mutations in Cu,Zn superoxide dismutase (SOD1) cause approximately 20% of familial ALS. One of the possible mechanisms whereby they induce disease is mitochondrial dysfunction in motor neurons. Here we describe a patient with ALS and muscle mitochondrial oxidative defect associated with a novel SOD1 mutation. Direct sequencing of SOD1 gene revealed a heterozygous mutation in codon 22 substituting a highly conserved amino acid, from glutamine to arginine (Q22R). Muscle biopsy showed a neurogenic pattern associated with cytochrome c oxidase (COX) deficiency in several muscle fibers. Western blot analysis demonstrated a reduction in SOD1 content in the cytoplasmic and mitochondrial fractions. These results suggest that a minute quantity of mutant SOD1 protein contributes to a mitochondrial toxicity also in muscle tissue.

Original languageEnglish
Pages (from-to)170-174
Number of pages5
JournalJournal of the Neurological Sciences
Issue number1-2
Publication statusPublished - Jan 15 2009


  • Amyotrophic lateral sclerosis
  • Mitochondria
  • Motor neuron
  • SOD1

ASJC Scopus subject areas

  • Clinical Neurology
  • Neurology


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