Research led by Catalan scientists reveals new information about cell aging

Barcelona (ACN).- A group of researchers led by the Institute of Biotechnology and Biomedicine (IBB) at the Universitat Autònoma de Barcelona (UAB), together with the UAB Department of Biochemistry and Molecular Biology, have discovered how to precisely quantify the effects of protein aggregation on cell aging. The team used the Escherichia Coli bacterium and the Alzheimer’s trigger molecule as models. Protein aggregation is related to numerous diseases such as neurodegenerative disorders. With this research, the scientists have proven that it can be predicted in advance, and thus this discovery might lead to the early detection of Alzheimer ’s disease, among other illnesses.

Apart from the IBB and the UAB’s Department of Biochemistry and Molecular Biology, scientists from the Biophysics Unit (CSIC-UPV) at the University of the Basque Country, the Institute for Bioengineering of Catalonia and the Barcelona Centre for International Health Research are also part of the research team.

Published in the ‘Journal of Molecular Biology’

The research, recently published in the ‘Journal of Molecular Biology’, provides a very reliable system for modelling and quantifying the effects that protein aggregation has on cell viability, division and aging and it helps researchers to understand the natural evolution of proteins.

Although it is widely accepted that the misfolding and aggregation of proteins reduce the cell’s reproduction and survival capacity, the damage caused had not been measured in an experimental and accurate way until this recent discovery.

In the words of Salvador Ventura, the IBB researcher that led the team, the investigation “must develop computational approaches in order to predict the effects aggregation has on cell aging, as well as a way of finding molecules that act as natural chaperones, a type of protein highly preserved in evolution and also found in humans, that reduces their impact on the bacterium”.

The early detection of Alzheimer

Research had proved in former investigations that the expression of the peptide linked to Alzheimer AB42 in bacteria triggered a process of protein aggregation. Now they have proven that this effect is encoded in the aggregated protein sequence and it depends on its intrinsic properties and not on the answer it causes in cells. This allows the early prediction of the phenomenon. They have also stated that inside the bacteria, the damage caused is modulated by molecular chaperones, which reduce the aggregating tendency of the protein and favour the cell’s survival.