Researchers at Buck Institute have identified the role of insoluble proteins in aging and Alzheimer’s disease, uncovering their widespread presence beyond just amyloid and tau proteins. Their study in worms demonstrates that boosting mitochondrial health can reverse the detrimental effects of these protein aggregates, suggesting new treatment strategies for neurodegenerative diseases and aging by targeting mitochondrial health and overall protein insolubility.
“Based on our discoveries, targeting insoluble proteins could provide a strategy for the prevention and treatment of a variety of age-related diseases,” said Edward Anderton, PhD, a postdoctoral fellow in Gordon Lithgow’s lab and co-first author of a study that appears in the May 16 issue of the journal“Our study shows how maintaining healthy mitochondria can combat protein clumping linked to both aging and Alzheimer’s,” said Manish Chamoli, PhD, a research scientist in Gordon Lithgow’s and...
Anderton said the team suspected they might see that amyloid beta is driving some level of insolubility in other proteins. “What we found is that amyloid beta causes a massive amount of insolubility, even in a very young animal,” said Anderton. They found that there is a subset of proteins that seem to be very vulnerable to becoming insoluble, either by adding amyloid beta or during the normal aging process. They called that vulnerable subset the “core insoluble proteome”.
The amyloid protein is very toxic to the worms and the team wanted to find a way to reverse that toxicity. “Since hundreds of mitochondrial proteins become insoluble both during aging and after expressing amyloid beta, we thought if we can boost the mitochondrial protein quality using a compound, then maybe we can reverse some of the negative effects of amyloid beta,” said Anderton.
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