Enhancing mitochondrial proteostasis (protein-folding quality-control processes) can reduce protein aggregation in animal models of amyloid-beta diseases, such as Alzheimer’s disease, reports a paper published in Nature. The study suggests that harmful amyloid-beta accumulation disrupts mitochondrial function, inducing a mitochondrial stress response. Boosting this response is shown to be beneficial in human cells, roundworms and in a mouse model of Alzheimer’s disease.
Alzheimer’s disease is a common and devastating disease characterized by the aggregation of the amyloid-beta peptide. However, the underlying molecular mechanisms remain uncertain and to date, there is no disease-altering therapy for Alzheimer’s disease available.
Johan Auwerx and colleagues find that mitochondrial proteostasis is implicated in a mitochondrial stress response signature present in amyloid-beta disease in humans, mice and Caenorhabditis elegans roundworms. They show that inducing this response is essential for maintaining mitochondrial proteostasis and health in a worm model of amyloid-beta disease. Moreover, enhancing the response increases the fitness and lifespan of worms, and reduces amyloid aggregation in human cells, worms and transgenic mice with Alzheimer’s disease. The findings support the relevance of enhancing mitochondrial proteostasis to delay amyloid-beta diseases, such as Alzheimer’s.
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