A team of researchers from the University of British Columbia and the Vancouver Coastal Health Research Institute have found a key link between prions and the neurodegenerative disease ALS. The discovery may result in new approaches to the treatment of ALS.
The researchers demonstrate that the SOD1 protein (superoxide dismutase 1), which has been shown to be implicated in the ALS disease process, exhibits prion-like properties. The researchers found that SOD1 participates in a process called template-directed misfolding. This refers to the coercion of one protein by another to change shape and accumulate in large complexes in a fashion similar to the process underlying prion diseases.
These findings provide a molecular explanation for the progressive spread of ALS through the nervous system, and highlight the central role of the propagation of misfolded proteins in the pathogenesis of neurodegenerative diseases, including ALS, Alzheimer disease, and Parkinson disease.
Researchers say that this discovery is the first step toward the development of targeted treatments that may stop progression of ALS.
The work was completed by Dr Neil Cashman’s lab at the Brain Research Centre based at the University of British Columbia and the Vancouver Coastal Health Research Institute, in collaboration with researchers at the University of Alberta.
The team published its findings in Proceedings of the National Academy of Science in September.
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