In the late-80’s through the 90’s, food and health agencies focused
on a mysterious fatal brain disease that infected thousands of cattle. Bovine
spongiform encephalitis—or “mad cow disease”—is caused by an infectious protein
called a prion. Despite fears that tainted meat would cause the disease to
spread to humans, mad cow disease never really made an impact on human health.
However, forms of the prion disease such as Creutzfeldt-Jakob disease do affect
In addition to Creutzfeldt-Jakob disease, many neurodegenerative diseases such as Alzheimer’s, Parkinson’s, Huntington’s and amyotrophic lateral sclerosis (ALS or Lou Gehrig’s disease) are now thought to be a result of prion-like activity. There is no cure for these diseases, however, new experimental treatment strategies might help slow the progression of neural degeneration.
Back in 2015 the Ice Bucket Challenge brought Amyotrophic Lateral Sclerosis (ALS) to public attention, initiating worldwide pleas for more funding of research toward a cure for this fatal disease, which is characterized by progressive degeneration of motor neurons. In spite of many efforts over the last few decades, the precise cause of ALS is still unknown.
The complexity of the problem of ALS pathogenesis is highlighted in the review “Decoding ALS: from genes to mechanism” published in Nature in November 2016. The review highlights a long list of genetic factors implicated in ALS, grouping them into genes affecting protein quality control, RNA stability/function, and the cytoskeletal structure of neuronal cells.
Mutations in the antioxidant enzyme superoxide dismutase (SOD1) were the first to be associated with ALS. According to the review, more than 170 SOD1 mutations causing ALS have since been identified. Many of these mutations are thought to result in misfolding of SOD1, contributing to toxicity when the misfolded protein accumulates within the cell.
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