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Molecular Basis Of ALS Found

ed up with Siddique and Deng. As reported in the second PNAS paper, they show that increased oxidative stress leads to the mutant SOD1 protein forming incorrect disulfide bonds early in its life. The researchers isolated and examined aggregates from the spinal cord of several ALS-model mice. In the diseased mice the scientists found intermolecular disulfide bonds that cross-linked SOD1 molecules together, resulting in the formation of insoluble aggregates. The SOD1 aggregates were specific to the spinal cord, the part of the body most damaged in ALS. Tissues unaffected by the disease, such as the brain and liver, had no aggregates.

Oxidation and protein aggregation have been suspected to play an important role in the pathogenesis of neurodegenerative disorders as well as in the normal aging process. However, the relationship between protein oxidation, protein aggregation and neurodegeneration remains unclear. The oxidative intermolecular disulfide cross-linking paradigm established by the Northwestern researchers provides direct links between protein oxidation, protein aggregation and neurodegeneration in SOD1-mediated ALS. This mechanism may play an important role not only in SOD1-mediated ALS but also in some other neurodegenerative disorders.

"For some time researchers have been thinking that copper, which causes the protein to be bluish-green in color, was the bad guy in this disease," said O'Halloran. "But the data has been building up to say that something else may be responsible for the toxicity. Our results suggest that the status of the disulfide bond, a long overlooked part of the SOD1 protein, plays a pivotal role. The ALS mutations appear to predispose SOD1 to form incorrect disulfide bonds that lead to aggregation of the protein and perhaps initiation of the disease. If these ideas are borne out, our next step is to look for therapeutic approaches that could prevent formation of the disulfide cross-linked aggregates." Source: Eur
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