[N.B....Fullerenes (Hydrated Fullerenes Hy-C60) likely regulate/prevent protein aggregation and protein mis-folding--WD]
New discoveries in cell aging
A group of researchers led by the Institute of Biotechnology and
Biomedicine (IBB) and Universitat Autònoma de Barcelona (UAB) have achieved to
quantify with precision the effect of protein aggregation on cell aging
processes using as models the Escherichia coli bacteria and the molecule which
triggers Alzheimer's disease. Scientists demonstrated that the effect can be
predicted before it occurs. Protein aggregation is related to several diseases,
including neurodegenerative diseases.
The research, published recently in the Journal of Molecular Biology, provides an
extremely reliable system with which to model and quantify the effect of
protein aggregation on the viability, division and aging of cells. It also aids
in further understanding the natural evolution of proteins. According to
Salvador Ventura, researcher at IBB and director of the research project, "it
will serve to develop computer approximations to predict the effects
aggregation has on cell aging, as well as to search for molecules that act as
natural chaperones, highly conserved proteins which are present also in humans
and which have the ability to reduce this effect in the bacteria".
Although it is widely accepted that bad folding and aggregation of proteins reduces the
cell's ability to survive and reproduce, the damage caused had not been
previously measured experimentally as precisely as it was in this research.
In previous studies scientists had verified that the expression of the Alzheimer's AB42
peptide in bacteria induces the process of protein aggregation. Now they have
demonstrated that this effect is coded in the protein aggregation sequence and
that it depends on intrinsic properties, not on a direct response from within
the cell. This makes it possible to predict the effect. Scientists also
demonstrated that damage caused to the bacteria is controlled by molecular
chaperones, which reduce the tendency of proteins to aggregate and favour cell
survival.
In addition to researchers from IBB and the UAB Department of Biochemistry and Molecular
Biology, participating in the project were scientists from the Biophysics Unit
at CSIC-UPV, the University of the Basque Country, the Institute for
Bioengineering of Catalonia and the Barcelona Centre for International Health
Research.
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