Lab findings may point to potential therapies for Lou Gehrig’s disease, dementia.
By imitating a natural process of cells, scientists prevented the formation of protein clumps associated with amyotrophic lateral sclerosis (ALS) and frontotemporal dementia.
In lab cultures of human and yeast cells, the researchers stopped the harmful clumping of FUS proteins by exposing them to phosphorylation, a process that makes precise changes to the amino acid building blocks of proteins, increasing their negative electric charge. Their study shows that the increase in charge causes the proteins to repel when they normally might aggregate.
The findings, published in the EMBO Journal, could eventually have positive implications for the treatment of ALS—commonly called Lou Gehrig’s disease—and dementia.
“No one has shown that you can use charge, and phosphorylation as a way to get charge, to disrupt these ALS-associated protein aggregates,” says co-corresponding author Nicolas Fawzi, PhD, assistant professor of medical science.
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