Discovery into how ALS spreads

Issue: BCMJ, vol. 56 , No. 3 , April 2014 , Pages 142 News

A study led by University of British Columbia and Vancouver Coastal Health Research Institute researchers has revealed how amyotrophic lateral sclerosis (ALS), also known as Lou Gehrig’s disease, is transmitted from cell to cell, and findings suggest the spread of the disease could be blocked. ALS is associated with the mutant SOD1 protein (superoxide dismutase 1) and earlier investigations found the disease-associated mutant SOD1 can induce a change in the shape of other proteins at the molecular level by misfolding inside living cells. The affected proteins then accumulate in ways similar to the process underlying prion diseases—rare, fatal, degenerative brain disorders seen in both humans and animals. The research shows that misfolded nonmutant SOD1 can be transmitted from region to region in the nervous system, offering a molecular explanation for the progressive spread of ALS.

The study also shows the spread can be blocked using antibodies. Antibodies were specifically raised to bind to regions of SOD1 exposed when it is misfolded, and block its spread. If nonmutant SOD1 misfolding is the cause of ALS, as the study suggests, researchers predict the antibodies could arrest ALS progression. 

Lead investigator Dr Neil Cashman, professor and Canada research chair in neurodegeneration and protein misfolding at UBC, and academic director of the Vancouver Coastal Health ALS Centre, suggests that by understanding how the disease is transmitted throughout the nervous system researchers can devise the best ways to stop progressive neurological damage. There are approximately 140 000 new cases diagnosed worldwide each year.

The study is published in the Proceedings of the National Academy of Sciences.

. Discovery into how ALS spreads. BCMJ, Vol. 56, No. 3, April, 2014, Page(s) 142 - News.



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