Canadian Study Discovers How Lou Gehrig's Disease Spreads
February 19, 2014

Canadian Study Discovers How Lou Gehrig’s Disease Spreads

Rebekah Eliason for – Your Universe Online

A new study from the University of British Columbia and Vancouver Coastal Health Research Institute has discovered how amyotrophic lateral sclerosis (ALS), commonly known as Lou Gehrig’s disease, spreads. This fatal neurodegenerative disease is transmitted from one cell to another, which provides hope that the disease can be blocked.

ALS damages nerve cells located in the brain and the spinal cord. This causes the motor neurons to progressively degenerate and die. When the motor neurons are attacked by the disease, the brain loses its ability to initiate and control muscle movement. Once the disease has progressed to a late stage, patients often become totally paralyzed. Approximately 140,000 new cases are diagnosed throughout the world each year.

Dr. Neil Cashman, UBC’s Canada Research Chair in Neurodegeneration and Protein Misfolding and lead investigator of this study, said, “This work identifies an important piece of the puzzle in determining how the disease is transmitted throughout the nervous system. By understanding how this occurs, we can devise the best ways to stop the progressive neurological damage seen in ALS.”

According to the new research, misfolded non-mutant SOD1 protein can spread throughout the nervous system from region to region. This provides a molecular explanation for how ALS progressively spreads.

The exciting study also demonstrated how antibodies can be used to block the protein from spreading. Researchers raised antibodies to specifically bind to areas of SOD1 that become exposed when they are misfolded and once attached they can block the protein from spreading. The researchers say that if the non-mutant SOD1 misfolding causes ALS, this study suggests that the new treatment could halt ALS progression.

This new research builds on earlier research from Cashman’s lab. ALS was previously shown to be linked to mutant SOD1 protein (superoxide dismutase 1). The initial research discovered that the mutant SOD1 associated with the disease was capable of inducing a shape change in other proteins by misfolding inside of living cells. Similar to other rare, fatal, degenerative brain disorders, known as prion diseases, which are seen in both humans and animals, the attacked and deformed proteins accumulate in the brain.

Other prion diseases similar to ALS include Alzheimer’s disease, Parkinson’s disease and Creutzfeldt-Jakob disease. In animals, common prion diseases are Bovine Spongiform Encehalopathy (mad cow disease), scrapie and chronic wasting disease.

Dr. Cashman is Professor and Canada Research Chair in Neurodegeneration and Protein Misfolding at UBC, and Academic Director of the Vancouver Coastal Health ALS Centre. He is also a member of the Brain Research Centre, a partnership between UBC and Vancouver Coastal Health Research Institute. This study was published in the journal Proceedings of the National Academy of Sciences.