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Item
#12
Misshapen
Proteins Tied to Type 2 Diabetes
Type
2 diabetes may be the result of protein folding gone awry.
Changes
in structure, not chemistry, cause problems.
Illnesses from Alzheimer's disease, Type II diabetes and
Creutzfeldt-Jakob disease may be the result of protein folding
gone awry.
Two
new studies in the journal Nature report that misfolded
proteins that clump together are harmful because of their abnormal
shape, not because their chemistry has become toxic.
The
findings suggest future therapies designed to prevent or target
the misfolded proteins may help treat seemingly unrelated
diseases. Christopher M. Dobson, a professor of chemistry and
structural biology at the University of Cambridge in England, was
a co-investigator on the first study.
Proteins
need to collapse into one another to determine what their ultimate
function will be.
For
the last decade, Dobson's research has focused on how proteins go
from their disordered state after they are first made inside a
cell into their folded, functional state.
"As
we were very much involved in understanding the folding process,
we were able to focus on a different angle, which is what makes
the protein misfold," he says.
Dobson
says the deposits that form in the 20 or so protein misfolding
conditions -- including Alzheimer's disease, the prion diseases
(such as Creutzfeldt-Jakob disease), and even Type II diabetes --
are made up of thread-like structures.
However,
he found that aside from the proteins linked to those diseases,
other proteins in the laboratory could be "persuaded" to
take these thread-like forms.
"We
could form these thread-like structures in the test tube from
virtually any protein that we wanted to if we got it under the
right conditions," Dobson says. Moreover, "if you take
any protein and misfold it into these aggregates [an abnormal
collection of proteins], they will be damaging to the cells."
He
explains this misfolding appears to happen when the normal process
of protein folding goes awry, and the protein bonds incorrectly to
itself. Dobson suspects that when this happens, "sticky"
parts of the early aggregate protein that are normally hidden
inside the properly folded protein are exposed, interfering with
other parts of the cell.
As
the more mature protein threads form, says Dobson, "a lot of
the sticky regions of the protein get covered up and you end up
with a rather innocuous type of material."
Other
proteins called "molecular chaperones" normally protect
folding proteins and destroy those that have misfolded. Dobson
suspects that since most of the misfolding-related diseases are
linked to aging, perhaps these cellular housekeeping functions
become less efficient with time.
"We
tend to accumulate these aggregates under some
circumstances," he says. "Once these aggregates start to
form, they actually seed the formation of other aggregates, and
one can end up with large quantities of them."
He
says that understanding the fundamental structural mechanisms of
this misfolding may lead to new therapies for illnesses like
Alzheimer's disease. In particular, he says, "if one wants an
effective therapy, one should either try and stop the aggregates
forming at all … or else try and get rid of these early
aggregates."
"This
is an entirely new way of thinking about what causes a whole
variety of diseases of old age," Walker says. "The good
news is that people are thinking in this way, and this is going to
lead to -- more or less -- a revolution in the way we think about
these [proteins] and a revolution in the way we think about
treating the diseases."
Walker
says that scientists are now on the threshold of new discoveries.
"Hopefully … we'll be able to use what we learn to treat a
variety of diseases that have always been thought of as being
completely unrelated."
================================
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