Dr. Neil Cashman,    MD
Professor and Canada Research Chair,
Brain Research Centre, Department of Medicine (Neurology), University of British Columbia
Academic Director, ALS Centre, GF Strong Hospital, Vancouver, British Columbia

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The term ‘prion’ is a combination of the words protein and infection used to represent the concept of misfolding of prion proteins naturally present in neural tissue. This disruption in protein structure leads to a cascade effect resulting in the formation of conformational copies of the misfolded prion protein. This propagated protein misfolding process, discovered by the 1997 Nobel Laureate Stanley Prusiner, can lead to neurodegenerative diseases such as Creutzfeld Jacob disease (CJD) in humans, bovine spongiform encephalopathy (BSE) in cattle, and chronic wasting disease (CWD) in cervids. Prion diseases can be transmitted both within and between species: the human version of BSE, variant Creutzfeld Jacob disease (vJCD), is caused by the consumption of beef contaminated with the BSE agent. Recent research has suggested a role for template-directed protein misfolding in the etiology of other important neurological conditions, including Alzheimer’s disease, Parkinson’s disease, and amyotrophic lateral sclerosis (ALS). This presentation provides an overview of the current knowledge of protein misfolding in important neurological conditions, and opportunities for addressing prion disease risks.