A new approach to assessing aging and disease risk: The protein aggregation clock

Protein Clumps in Cells May Reveal Risk of Age-Related Diseases, Scientists Propose
Researchers from Johannes Gutenberg University Mainz (JGU) and the Institute of Molecular Biology (IMB) in Mainz have proposed a new concept called a “protein aggregation clock” to measure aging and health. In a perspective article published in Nature Cell Biology, Professor Dorothee Dormann and Professor Edward Lemke suggest that measuring protein clumps in our cells could help determine our risk of developing age-related diseases.

Protein Misfolding and Aggregation Linked to Aging and Disease

As we age, the DNA and proteins in our bodies undergo changes that cause our bodies to function less effectively, making us more susceptible to age-related diseases like cardiovascular disease, cancer, and Alzheimer’s. One crucial change is the misfolding and clumping together of proteins to form aggregates, known as amyloids. This process can happen to any protein, but a group of proteins called intrinsically disordered proteins (IDPs) are particularly prone to forming amyloids.

IDPs, which make up around 30 percent of the proteins in our cells, are flexible and dynamic, lacking a fixed structure. Scientists have observed that aggregates formed from IDPs tend to accumulate in many long-lived cells, such as neurons or muscle cells, as we age. These aggregates can cause many age-related diseases, particularly neurodegenerative diseases like Alzheimer’s and Parkinson’s.

Potential Benefits of a Protein Aggregation Clock

Dormann and Lemke propose that IDP aggregation could be used as a biological “clock” to measure a person’s health and age. If developed into a sensitive diagnostic test, a protein aggregation clock could help doctors diagnose age-related diseases at very early stages or identify people with a higher risk of developing these diseases as they age. This would allow for preventative treatments before severe disease develops. Additionally, scientists could use the clock to assess the effects of new experimental treatments aimed at reducing protein aggregation to prevent or delay age-related diseases.

“In practice, we are still far away from a routine diagnostic test, and it is important that we improve our understanding of the fundamental mechanisms leading to IDP aggregation”, said Dormann. “However, we want to stimulate thinking and research in the direction of studying protein aggregates to measure biological ageing processes,” Lemke added.

While other “clocks” exist to measure aging and health, most are based on nucleic acids like DNA. Dormann and Lemke believe that a protein-based biological clock would complement these existing clocks, as proteins are among the most abundant molecules in cells and are essential for all cellular functions. With further research and technological advancements, they hope that a protein aggregation clock can help scientists and doctors move closer to promoting healthy aging and preventing age-related diseases.

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