Mental Health
Alzheimer's Disease Associated to Prion-Like Proteins, Research Finds
Proteins that act like prions - copies of a normal protein that have been corrupted in ways that cause diseases - might be responsible for disorders that attack the brain and spinal column, according to a new research.
Earlier it was thought that only one particular protein could be corrupted in this fashion, but the new research is suggesting that another protein linked to Alzheimer's disease and many other neurodegenerative conditions also behaves very much like a prion.
According to the research, protein, known as tau, could be corrupted in different ways, and that these different forms of corruption-known as strains-are linked to distinct forms of damage to the brain.
"If we think of these different tau strains as different pathogens, then we can begin to describe many human disorders linked to tau based on the strains that underlie them," said senior author Diamond, the David Clayson Professor of Neurology, in the press release. "This may mean that certain antibodies or drugs, for example, will work better against certain disorders than others."
Prions are made of normal proteins that have folded into an abnormal shape but aren't alive. However their effects can be similar to infectious microbes such as bacteria or viruses.
"When we infected a cell with one of these misshapen copies of tau and allowed the cell to reproduce, the daughter cells contained copies of tau misfolded in the same fashion as the parent cell," Diamond added in the press release. "Further, if we extracted the tau from an affected cell, we could reintroduce it to a naïve cell, where it would recreate the same aggregate shape. This proves that each of these differently shaped copies of the tau protein can form stable prion strains, like a virus or a bacteria, that can be passed on indefinitely."
Researchers said they are now working to find a way to isolate tau prions non-invasively from individuals for diagnostic purposes.
The findings of the study will be published in Neuron.
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