In two ground-breaking studies, published in the journals PLOS ONE and Nature Communications, Prof. Lederkremer and his team demonstrated that protein clusters are not the cause of toxicity in Huntington's disease.
On the contrary, these aggregates actually serve as a defense mechanism
for "stressed" brain cells. Conducted on tissue cultures using
cutting-edge microscopic technology, their studies identified a
different causative agent—the "stress response" of affected brain cells.
Prof. Lederkremer and his team chose to examine the effect of protein
aggregates in the pathology of Huntington's disease because its genetic
cause is well-known, unlike those of other neurodegenerative diseases,
such as Parkinson's, whose origins remain less clear.
"What we found in this study—a surprise, although we suspected it—was
that damage to the cells, the cell 'stress' that leads to death of
cells, appeared well before the protein aggregates did," said Prof.
Lederkremer. "And even more surprising, when the aggregates finally
appeared, the stress was reduced, in some cases even stopping. The
actual process of forming an aggregate was protective, isolating and
segregating the problematic proteins. This explains why in autopsies of
people who died of Huntington's and other diseases like Alzheimer's or
old age, the protein aggregates in the brains were all quite similar,
reflecting no specific disease link."
On the contrary, these aggregates actually serve as a defense mechanism
for "stressed" brain cells. Conducted on tissue cultures using
cutting-edge microscopic technology, their studies identified a
different causative agent—the "stress response" of affected brain cells.
Prof. Lederkremer and his team chose to examine the effect of protein
aggregates in the pathology of Huntington's disease because its genetic
cause is well-known, unlike those of other neurodegenerative diseases,
such as Parkinson's, whose origins remain less clear.
"What we found in this study—a surprise, although we suspected it—was
that damage to the cells, the cell 'stress' that leads to death of
cells, appeared well before the protein aggregates did," said Prof.
Lederkremer. "And even more surprising, when the aggregates finally
appeared, the stress was reduced, in some cases even stopping. The
actual process of forming an aggregate was protective, isolating and
segregating the problematic proteins. This explains why in autopsies of
people who died of Huntington's and other diseases like Alzheimer's or
old age, the protein aggregates in the brains were all quite similar,
reflecting no specific disease link."
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