Research from Cologne: Protein EPS8 could be the key against neurodegeneration!

Transparenz: Redaktionell erstellt und geprüft.
Veröffentlicht am

Research at the University of Cologne is investigating how the protein EPS8 is related to aging and neurodegeneration. Study by Prof. Vilchez.

Forschung an der Uni Köln untersucht, wie das Protein EPS8 mit Altern und Neurodegeneration zusammenhängt. Studie von Prof. Vilchez.
Research at the University of Cologne is investigating how the protein EPS8 is related to aging and neurodegeneration. Study by Prof. Vilchez.

Research from Cologne: Protein EPS8 could be the key against neurodegeneration!

A research team from University of Cologne, led by Professor Dr. David Vilchez, has made significant advances in understanding the links between aging and neurodegenerative diseases. The study, which was carried out as part of the Cluster of Excellence for Aging Research CECAD, used the nematodeCaenorhabditis elegansas a model organism. The focus is on the protein EPS8, which accumulates with age and triggers harmful stress responses.

The research shows that elevated levels of EPS8 and activation of its signaling pathways can lead to harmful protein aggregation and neurodegeneration, which are hallmarks of Huntington's disease and amyotrophic lateral sclerosis (ALS). Reduced EPS8 activity could therefore prevent the formation of toxic protein aggregates and maintain neuronal function in the worm models.

Mechanisms of neurodegeneration

The research results may open new perspectives on the molecular mechanisms that link aging and neurodegenerative diseases. EPS8 and its signaling partners are evolutionarily conserved and also occur in human cells. In human cell models of Huntington's disease and ALS, reducing EPS8 levels also resulted in the prevention of toxic protein aggregates. However, which specific mechanism the increased EPS8 activity stimulates toxic protein aggregation remains unclear.

A central aspect of neurodegenerative diseases is the harmful accumulation of proteins, which leads to the loss and death of nerve cells in the brain. This fits in with the findings that in Alzheimer's disease, amyloid beta proteins form plaques and the TAU protein causes tangles within the cells. Scisimple reported that aggregates in the brain can spread and stimulate other proteins to misfold, further exacerbating disease progression. Therefore, research into the formation and distribution of such aggregates is crucial for the development of future treatments.

Therapeutic approaches

Current therapies focus on reducing or removing these harmful aggregates, including through the use of antibodies against amyloid-beta and tau. However, not all treatment methods have proven successful in clinical studies. This leads to a reassessment of the underlying disease mechanisms and the approach of targeting smaller aggregates (oligomers) that have proven to be particularly toxic.

Mathematical models are helpful in simulating the dynamics of protein aggregation and identifying possible treatment strategies. Recent studies suggest that more frequent dosing may increase the effectiveness of treatments, although it is beneficial to maintain a balance to avoid side effects. These findings, together with the results of the Cologne study, could help develop more comprehensive strategies to combat toxic protein buildups.

In summary, the potential role of EPS8 and the mechanisms of protein aggregation are important topics that are of enormous importance not only for basic research but also for the development of therapies against age-related and neurodegenerative diseases.