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My name is Ana Maria Cuervo,
and I am a professor
at the Albert Einstein
College of Medicine
and Co-Director
of the Aging Center.
I will be talking today
about Protein Homeostasis
and its importance in aging.
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As all of you know,
all proteins in the cells
are continuously exposed
to damaging agents
that can modify
their protein confirmation.
So when a protein is damaged,
it exposes regions
that are going to be particularly
hydrophobic or sticky,
and can abnormally interact
with other proteins
in the cell.
To avoid that,
cells count on systems
that take care
of protein misfolding.
The first ones are chaperones
that if possible
will refold these proteins
to return to their
normal conformation.
And the second system
are the proteases,
where chaperones deliver
the unfolded protein
to undergo degradation.
This is actually
a very conservative system
because when proteins
breakdown into amino acids,
they can be reutilized
to sustain protein synthesis.
So this quality control
mechanisms,
chaperones and proteases
are in place
and functioning in all the cells
when we are young.
However, as we get old
and in particular diseases,
these systems
do not work properly
and result in protein toxicity
or accumulation
of protein damage.
For example, if chaperones
cannot identify,
they unfold the protein
or if the proteolytic systems
are not ready to receive
this unfolded proteins,
they will accumulate
inside the cell
and they will organize
in higher molecular weight
as structures in the form of
protein aggregates
or oligomers
that are toxic for the cell.
So in this lecture,
I will give you some examples
of what is known about chaperone
and proteolytic
systems malfunctioning
during aging
and how can they contribute
to some of the characteristics
of the phenotype of ageing.
