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The Therapeutic Potential of Cold Temperature in Combating Neurodegenerative Disorders

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As we age, our risk of developing neurodegenerative disorders increases significantly due to the accumulation of misfolded proteins in the brain. These protein aggregations are associated with conditions such as Alzheimer's, Parkinson's, Huntington's, and amyotrophic lateral sclerosis (ALS). However, recent research suggests that there might be a surprising ally in the fight against these debilitating diseases: cold temperature.



In this blog post, we'll explore how the process of aging affects neurodegenerative disorders and how lowering body temperature could potentially offer a novel therapeutic approach. We'll delve into groundbreaking studies conducted in the model organism Caenorhabditis elegans and their relevance to human health. By the end, we hope to shed light on the exciting possibility of using cold-induced changes to combat age-related protein aggregation and neurodegeneration.



Aging and Neurodegenerative Disorders

As we grow older, our bodies undergo various changes, and our brain is no exception. Aging is a primary risk factor for neurodegenerative disorders, and one of the key mechanisms involved is the accumulation of misfolded and aggregated proteins in the brain cells. These protein clumps can interfere with cellular functions, disrupt communication between neurons, and lead to the characteristic symptoms of these diseases.

Cold Temperature: An Unexpected Anti-Aging Mechanism

Researchers have long been fascinated by the idea that lowering body temperature might extend lifespan and delay the onset of age-related diseases. This phenomenon has been observed in both cold-blooded organisms (poikilotherms) and warm-blooded animals (homeotherms), suggesting its broad evolutionary significance.

Understanding Cold-Induced Changes and Protein Aggregation

To better comprehend the relationship between cold temperature and neurodegenerative disorders, scientists turned to the tiny roundworm, Caenorhabditis elegans. This organism serves as an excellent model for studying various biological processes, including aging and disease.

In a groundbreaking study, scientists found that subjecting C. elegans to cold temperature (15°C) selectively induced the trypsin-like activity of the proteasome. The proteasome is a cellular complex responsible for breaking down and recycling proteins. Increased trypsin-like activity is associated with enhanced protein degradation, potentially clearing out misfolded proteins and reducing aggregation.

The Role of PSME-3 in Cold-Induced Longevity

Further investigation revealed that the protein PSME-3 plays a crucial role in the cold-induced trypsin-like activity of the proteasome in C. elegans. PSME-3 is the worm equivalent of a human protein called PA28γ/PSME3, known to activate the proteasome in mammals.

This proteasome activator, PSME-3, is essential for the cold-induced longevity observed in C. elegans. It not only promotes lifespan extension but also ameliorates age-related deficits in protein degradation, which are often linked to the onset and progression of neurodegenerative disorders.

Cold-Induced Reduction of Protein Aggregation

One of the most exciting findings from this research is that cold-induced PSME-3 also diminishes protein aggregation in C. elegans models of age-related diseases like Huntington's and ALS. By enhancing the clearance of misfolded proteins, cold temperature appears to act as a powerful modifier of pathological protein aggregation.

Extending the Findings to Human Cells

The implications of these findings stretch far beyond the realm of tiny worms. The researchers explored whether similar effects could be observed in human cells. Remarkably, they found that exposing human cells to moderate cold temperature (36°C) also activated trypsin-like activity through the human equivalent of PSME-3 (PA28γ/PSME3). This activation led to a reduction in disease-related protein aggregation and neurodegeneration.

Towards Multi-Disease Prevention



The discovery of cold-induced changes as potential modifiers of pathological protein aggregation opens up exciting possibilities for multi-disease prevention. By addressing the root cause of many neurodegenerative disorders—the accumulation of misfolded proteins—we might be able to develop novel therapies that have broad applications across different conditions.

Conclusion

Aging and neurodegenerative disorders have long been interconnected, but recent research into the effects of cold temperature on protein aggregation has provided a glimmer of hope. By studying the humble roundworm, C. elegans, scientists have uncovered the beneficial role of cold-induced changes, particularly through the activation of PSME-3, in promoting longevity and reducing protein aggregation.

These findings not only expand our understanding of the aging process but also offer potential implications for multi-disease prevention in humans. As research continues in this exciting field, we may be one step closer to unlocking a revolutionary approach to combat neurodegenerative disorders and improve the quality of life for millions of people worldwide.

From: https://www.nature.com/articles/s43587-023-00383-4

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