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Molecular Basis Of ALS Found

Northwestern University researchers have discovered the molecular basis of the neurodegenerative disease amyotrophic lateral sclerosis (ALS).// Two separate teams including neurologists and biochemists worked on how the mutated form of superoxide dismutase (SOD1) protein renders people vulnerable to formation of intermolecular aggregates. This mutated protein is associated with a familial form of ALS.

The findings, which have implications for new therapeutics for the devastating disease, were published online this week in two related papers by the Proceedings of the National Academy of Sciences (PNAS).

ALS is a progressive paralytic disorder caused by degeneration of motor neurons in the brain and spinal cord. The cause and development (pathogenesis) of the fatal disease are not known, and there is no effective treatment. Fifteen years ago, an international consortium led by Teepu Siddique, M.D., Les Turner ALS Foundation/Herbert C. Wenske Foundation Professor at Northwestern's Feinberg School of Medicine, mapped the first ALS gene to chromosome 21. Subsequently, they found that mutations in the SOD1 gene are responsible for 20 percent of familial (inherited) ALS cases. Siddique and his colleagues also made the first ALS transgenic mouse models.

Although more than 100 types of a single mutation in the SOD1 gene have been identified and multiple lines of the mouse models developed, a key question remains to be answered: How does the genetic mutation alter this incredibly stable protein to make it so toxic that it kills motor neurons and causes neurodegenerative disease? The presence of aggregated proteins is common to many neurodegenerative disorders, including ALS and Alzheimer's, Parkinson's and prion diseases, but the relevance of these aggregates to the diseases is not well understood. In ALS patients with SOD1 mutations and mouse models overexpressing mutant SOD1, SOD1-positive aggregates were identified in neurons. Researchers do
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