The human protein prefoldin can reduce the neuronal toxicity of clumps of amyloid-β proteins that collect in the brains of Alzheimer’s patients.
“Our findings may also apply to various other neurological diseases caused by protein misfolding, such as prion disease, Huntington’s disease and Parkinson’s disease,” explains Tamotsu Zako from the research team.
Alzheimer’s disease is a progressive degenerative brain disease most commonly characterized by memory deficits. Loss of memory function, in particular, is known to be caused by neuronal damage arising from the misfolding of protein fragments in the brain.
Now, a group of researchers led by Mizuo Maeda of the RIKEN Bioengineering Laboratory, and including researchers from the Laboratory for Proteolytic Neuroscience at the RIKEN Brain Science Institute, has found that the human protein prefoldin can change the way these misfolded protein aggregates form and potentially reduce their toxic impact on the brains of Alzheimer’s patients…..
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