It looks like you're using an Ad Blocker.
Please white-list or disable AboveTopSecret.com in your ad-blocking tool.
Some features of ATS will be disabled while you continue to use an ad-blocker.
Breakthrough in Understanding Secret Life of Prion Molecules
New research from David Westaway, PhD, of the University of Alberta and Jiri Safar, MD, Case Western Reserve University School of Medicine 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 Westaway, Director of the Centre for Prions and Protein Folding Diseases and Professor of Neurology in the Faculty of Medicine and Dentistry 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.
Researchers at the University of Alberta closer to stopping brain diseases
"These are slow, unstoppable, deadly degenerative diseases of the brain," said project lead David Westaway of the Centre for Prions and Protein Folding Diseases and the Faculty of Medicine and Dentistry.
"We think we have stumbled upon something unexpected, that the cells have a protective mechanism. And we are quite confident that finding is very solid, very robust, because we looked at six different types of prion disease and they all had the same effect."
The research team found the number of cellular prion protein molecules in animal models dropped months or years before they showed symptoms of illness, indicating the infected cells are "smarter than we once thought," Westaway said.
The team is looking at ways to augment the natural protective response and bring the diseases to a standstill in their pre-clinical phase.
Evolving proteins – no DNA required
Prions are the infective agents that cause transmissible spongiform encephalopathies such as Mad Cow Disease in humans. All prions affect the brain or neural tissues and are currently untreatable. What makes them particularly fascinating is that unlike other infective agents such as bacteria, protozoa, and viruses, they don’t contain any genetic material. No DNA or RNA. Prions are just misfolded proteins but they are capable of spreading, causing disease, and evolving.
Prions spread disease a little like zombies. The prions themselves are misfolded proteins, and when they come into contact with correctly folded versions of the protein they cause them to misfold as well. Once these proteins become misfolded they can go on and convert further proteins to the misfolded form. This misfolded protein accumulates in neural cells and tissues causing damage to the brain. In mammals, all prion diseases are caused by a protein known as PrP (prion protein). The correctly folded form is referred to as PrPC and the misfolded form as PrPSc.
Not only do the prions spread they also change and evolve as they go. There are various different theories as to how a prion, a piece of folded protein with no associated DNA, can evolve. The ‘cloud hypothesis’ is that different variants of PrPSc are present within the organism. Depending on outside environmental pressures, one form may be able to spread quicker or more effectively than others and therefore will be selected for.