New Relationship Discovery Between Prions and Infectious Brain Disease

Scientists are digging deeper into the causes and complications of dementia, Alzheimer’s and other diseases involving impaired brain function. Although prions are healthy proteins found inside the brain, they sometimes develop into pathogens that cause a variety of infections and abnormalities.

Decades of research is currently revealing that when prions are misfolded, they can become contagious pathogens that join with other prions that cross their path. They group together, damage other cells and eventually cause a break down of the brain itself. Prions that have mutated are not easily controlled using conventional heat or radiation and therefore they have the potential to spread easily between surgical patients. With no insight into how these natural proteins go rogue, related diseases have been considered fatal and untreatable.

Iowa State University researchers have now shown on a molecular level how copper ions can cause prions to misfold and then spread the mutation to other prions. The connection between copper ions and the misfolding of prions has been established but copper ions have not been linked to diseases related to prions at this point.

Scientists have never been able to explain the behavior of prions because proteins are not living organisms and should not be able to infect other proteins. Powerful imaging techniques were used to show that copper ions bind to the tail of prion proteins to cause the misfolding in the prions they attach to as well as others nearby. Researchers also discovered that misfolded prions stick together much more efficiently than healthy prions. Although there has not been sufficient research on how infectious prion diseases spread, the scientists have shown that changes made to the prions by copper ions are associated with inflammation and damage to nerve cells in the brains of mice.

Although, it has been proven that copper ions have the ability to trigger misfolding of prion proteins and the misfolding creates toxicity in the nerve cells, not all strains of the misfolded prion proteins are pathogenic. Researchers will now look into how the copper ions may be connected to actually causing diseases such as Cruetzfeldt-Jakob (‘mad cow’ disease.) This research could eventually lead to developing treatments for these untreatable diseases.

Alzheimer’s and Parkinson’s diseases are thought to be related to amyloid beta proteins misforming and clumping together in the brain and now evidence is surfacing that shows Alzheimer’s could be transmitted through surgical procedures, making it more similar to a prion disease than researchers previously thought. Scientists hope to learn more about prions and the role of metals in protein misfolding diseases in order to eventually make these types of diseases more manageable and much less terrifying.