The Cohen Lab and NC State researchers team up to reverse TDP-43 protein aggregation, a hallmark of degenerative diseases.
Scientists have long known that a protein called TDP-43 clumps together in brain cells of people with amyotrophic lateral sclerosis (ALS), also known as Lou Gehrig’s Disease, and is associated with neuron death. This same protein is thought to cause muscle degeneration in patients with sporadic inclusion body myositis (sIBM), leading many researchers to think that TDP-43 is one of the causative factors in ALS and sIBM. Now, UNC School of Medicine and NC State researchers found that a specific chemical modification called acetylation promotes TDP-43 clumping in animals. Using a natural anti-clumping method in mouse models, the scientists reversed protein clumping in muscle cells and prevented the sIBM-related muscle weakness.
The discovery, published in Nature Communications, has important implications for understanding ALS and sIBM, and for the creation of potential treatments down the road.
The lead author of the study was UNC postdoctoral researcher Ping Wang, PhD. Other co-authors were UNC graduate student Connor M. Wander, UNC Faculty Member Todd Cohen, PhD, NC State Faculty Member Michael Bereman, PhD, and Chao-Xing Yuan, PhD, of the University of Pennsylvania.
To read the full article about the publication by UNC Healthcare News, click here.
To read the publication in Nature Communications, click here.