New research has uncovered a quality-control mechanism in brain cells that may help keep deadly neurological diseases in check for months or years.

The findings, published in The Journal of Clinical Investigation, “present a breakthrough in understanding the secret life of prion molecules in the brain and may offer a new way to treat prion diseases,” said David Westaway, director of the Center for Prions and Protein Folding Diseases at the University of Alberta.

Prion diseases lead to incurable neurodegenerative disorders such as Creutzfeldt-Jakob disease in humans, mad cow disease (Bovine Spongiform Encephalopathy) and chronic wasting disease in deer and elk. The diseases are caused by the conversion of normal cellular prion proteins into the diseased form.

For years, scientists have been perplexed by two unexplained characteristics of prion infections: vastly differing asymptomatic periods lasting up to five decades, and when symptoms do arise, greatly varying accumulation of the diseased proteins. In striking contrast, test tube prions replicate rapidly, and in a matter of days reach levels found in brains in the final stage of the disease.

“Our study investigated the molecular mechanism of this intriguing puzzle,” said Jiri Safar, co-director of the National Prion Disease Pathology Surveillance Center.  In probing these mysteries, Westaway, Safar, their teams and other collaborating researchers in the U.S., Italy and the Netherlands studied a molecule called the ‘shadow of the prion protein.’

“Dramatic changes in this shadow protein led us to expand our view to include the normal prion protein itself,” said Westaway. “This is a crucial molecule in brain cells because it is pirated as the raw material to make diseased prion proteins.”

From:  Case Western Reserve University