disorders, is the presence of insoluble proteins. Previous treatments for Alzheimer’s disease have not taken into consideration the overall impact of insoluble proteins, instead focusing on specific proteins. However, a recent study conducted on worms has provided a comprehensive understanding of the relationship between insoluble proteins, neurodegenerative diseases, and aging. Additionally, the research has identified a potential intervention that can reverse the harmful effects of protein aggregates by improving mitochondrial health.
Alzheimer’s disease and other neurodegenerative disorders are characterized by the presence of insoluble proteins. Previous treatments have only targeted specific proteins, rather than addressing the overall impact of insoluble proteins. However, a recent study conducted on worms has shed light on the connection between insoluble proteins, neurodegenerative diseases, and aging. The study also revealed a potential intervention to counteract the harmful effects of protein aggregates by enhancing mitochondrial health.Protein aggregation, a common feature of neurodegenerative diseases, involves the clumping of insoluble proteins in the brain. Even in the absence of disease, insoluble proteins tend to accumulate during the aging process.
Current treatments for Alzheimer’s disease have largely overlooked the role of insoluble proteins as a widespread issue, instead focusing on specific proteins. However, researchers at Buck Institute have conducted a detailed study in worms, revealing the complex connections between insoluble proteins, neurodegenerative diseases, and aging. Additionally, their work has identified a potential intervention to reverse this phenomenon.the harmful impacts of the aggregates by enhancing mitochondrial well-being.
“According to our findings, targeting insoluble proteins may offer a method for preventing and treating various age-related illnesses,” stated Edward Anderton, PhD, a postdoctoral fellow in Gordon Lithgow’s lab and co-first author of a study published in the May 16th edition of the journal GeroScience.
“Our research demonstrates how maintaining healthy mitochondria can fight against protein clumping associated with both aging and Alzheimer’s,” noted Manish Chamoli, PhD, a research scientist in Gordon Lithgow’s and Julie Andersen’s lab, and co-first author of the study.The research found that by enhancing the health of mitochondria, it may be possible to slow down or even reverse the harmful effects of aging and age-related diseases. The results also provide evidence for the geroscience hypothesis, which suggests a common pathway to Alzheimer’s disease and aging itself. Professor Gordon Lithgow, PhD, Vice President of Academic Affairs and the seniorThe lead researcher stated that the development of the illness is due to aging, but the factors that lead to the illness actually occur very early in life. The discovery of a core insoluble proteome enriched with many proteins that were previously overlooked opens up new avenues for investigation. Lithgow, the lead researcher, suggests that this finding raises questions about whether we should be considering what Alzheimer’s disease looks like in very young individuals. This suggests that beyond amyloid and tau, the focus of most Alzheimer’s disease research thus far has been on targeting the build-up of two proteins.One: Amyloid beta and tau are well-known proteins in insoluble aggregations related to Alzheimer’s disease. However, according to Anderton, there are thousands of other proteins in these aggregations, and their role in Alzheimer’s disease is not yet understood. Furthermore, Anderton mentioned that his lab and others have noted the accumulation of insoluble proteins during the normal aging process without disease. They have also observed that insoluble proteins from aged animals, when combined with amyloid beta in a test tube, speed up the aggregation of the amyloid.
The team was curious about the connection between the accumulation of aggregates in Alzheimer’s disease and the natural aging process without disease. They decided to focus on the amyloid beta protein and used a strategy to study this protein.Caenorhabditis elegans, a type of microscopic worm commonly used in studies on aging, has been genetically modified to produce human amyloid protein. According to Anderton, the research team suspected that amyloid beta could be the reason for the insolubility of other proteins. Their findings revealed that amyloid beta significantly contributes to insolubility, even in very young worms. They identified a specific group of proteins that are particularly susceptible to becoming insoluble, either through the introduction of amyloid beta or as a result of the natural aging process, and termed this group the “core insoluble proteome.”The team discovered that the core insoluble proteome contains proteins that have been associated with various neurodegenerative diseases, including Alzheimer’s disease, Parkinson’s disease, Huntington’s disease, and prion disease. According to Anderton, the findings indicate that amyloid may be contributing to the aggregation seen in normal aging. It is possible that both aging and amyloid beta are causing insolubility in a similar manner, creating a potential vicious cycle.
Researchers discovered that amyloid protein is highly toxic to worms, and they aimed to reverse this toxicity. They found that by using Urolithin A, a natural gut metabolite found in raspberries, walnuts, and pomegranates, they were able to significantly delay the harmful effects of amyloid beta. This compound is known to improve mitochondrial function, and the team hypothesized that boosting mitochondrial protein quality could potentially reverse some of the negative effects of amyloid beta. Their findings supported this hypothesis, offering hope for potential treatments in the future.
oid beta.” “From our data, it’s clear that mitochondria are incredibly important,” Anderton stated. The authors emphasize the significance of maintaining healthy mitochondria for overall well-being. Anderton noted the strong connection between mitochondria and aging, as well as their association with amyloid beta. He also highlighted the study’s unique finding that the insolubility and aggregation of these proteins may serve as the link between the two. “Due to the central role of mitochondria in all of this, one potential solution to break the cycle of decline is to replace damaged mitochondria with new mitoc. Lithgow mentioned the importance of exercise and a healthy diet in preventing diseases like Alzheimer’s.
