Researchers from The Buck Institute for Research in Novato, CA, have found that other proteins in addition to beta-amyloid and tau, which have previously been identified, play a role in the development of Alzheimer’s disease. The accumulation of insoluble proteins in the brain is a key factor in the disease, and researchers used a worm model to study how aging and beta-amyloid contribute to this process. By boosting the quality of mitochondrial health, researchers were able to delay the toxic effects of beta-amyloid on these insoluble proteins.
Proteins are essential for proper cellular function, but they can become misshapen and aggregated, leading to insoluble protein clumps. In Alzheimer’s disease, the brain struggles to dispose of these misshapen proteins, leading to the formation of plaques associated with neuronal death and inflammation. The research team at The Buck Institute discovered that insoluble proteins accumulate in the brain during normal aging, as well as in neurodegenerative diseases like Alzheimer’s, Parkinson’s, and Huntington’s. They found that beta-amyloid drives other proteins to become insoluble, creating a destructive cycle that accelerates protein insolubility in Alzheimer’s disease.
The researchers focused on the electron transport chain, a group of proteins responsible for producing energy in cells, located in mitochondria. Beta-amyloid was found to drive these proteins to become insoluble, impacting mitochondrial health. By using a compound called urolithin A, found in certain foods like pomegranates and nuts, researchers were able to boost mitophagy, a process that recycles damaged mitochondria, leading to improved mitochondrial health. This approach helped to reverse some of the negative effects of beta-amyloid on insoluble proteins.
Dr. Verna R. Porter, a neurologist not involved in the research, commented on the study’s findings, highlighting the importance of targeting mitochondrial health to address Alzheimer’s disease. Improving mitochondrial function may offer a novel approach to mitigating the effects of beta-amyloid toxicity in the brain. Porter suggested that clinical trials exploring the efficacy of mitochondrial health-boosting compounds such as urolithin A could lead to potential interventions for Alzheimer’s patients. Exploring how beta-amyloid disrupts mitochondrial function and leads to protein insolubility may reveal new therapeutic targets for the disease.
In conclusion, the study from The Buck Institute for Research sheds light on the role of insoluble proteins in Alzheimer’s disease and points to the importance of maintaining mitochondrial health to counteract the toxic effects of beta-amyloid. By targeting mitochondrial function through compounds like urolithin A, researchers were able to reverse some of the negative impacts of beta-amyloid on cellular proteins. This research opens the door to potential interventions for Alzheimer’s patients and suggests that further exploration of mitochondrial health could lead to innovative treatments for the disease.
