casemed.case.edu
Study
sheds light on age-related changes of prions
A new study sheds light on why normal prion proteins may experience age-related mutations in
inherited diseases. Researchers at the Case Western Reserve University School
of Medicine studied a previously discovered mutation in the prion
protein in members of an extended family in
In a laboratory study of the mutation
that causes GSS in this family, the mutant protein was found to assume its
normal shape in the cell, but after it was unfolded it failed to return to its normal
shape. This may explain why the disease is age-related, because the healthy
young cell can properly fold and maintain the mutant protein but the deficits
in the cellular machinery associated with aging might promote accumulation of
the aberrant form of the prion protein resulting in
disease.
Several questions remain, according to
Robert Petersen, Ph.D., associate professor of pathology and neuroscience at
Case and senior author of the study. “The most important question is,” he said,
“what is the exact nature of the improperly refolded form of the mutant
protein. In addition, it will be important to address what features of the
aging cell are most involved in defective protein folding, the understanding of
which may result in novel therapeutic strategies for halting these devastating
diseases.”
The study appears in the April 2005 issue
of the Journal of Alzheimer’s Disease
(http://www.j-alz.com), published by IOS
Press.
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