For a while, researchers and scientists have known that the protein, TDP-43, is found in clumps in the brain cells of patients with amyotrophic lateral sclerosis (ALS). It has also been known that this protein is also related to neuron death.
Amyotrophic lateral sclerosis (ALS) is a rare progressive, neurological disease that kills nerve cells in the brain stem, spinal cord and brain.
Consequentially, muscles eventually weaken, causing loss of voluntary movement and control. To learn more about this debilitating rare disease, click here.
Additionally, the problem-causing TDP-43 protein is believed to promote the degeneration of muscles in people with another condition, called sporadic inclusion body myositis (sIBM). As a result, most scientists are led to believe that TDP-43 is a causative factor in ALS as well as sIBM.
Recently, researchers at NC State and the School of Medicine pinpointed that a unique chemical change, called acetylation, advances the TDP-43 clumping in animals. These scientists then used a natural method to reverse this clumping in the muscle cells of mouse models and stop the muscle weakness related to sIBM and ALS.
Senior author of this study, Todd J. Cohen, PhD, believes that in theory, this clumping reversal could be used as a potential treatment for ALS and sIBM in an oral or injectable therapy, but the actual practice of this type of medication is still a long time coming.
Here’s a little biology lesson on this notorious protein:
In a normal functioning body, TDP-43 works in the cell’s nucleus; it is a protein that typically binds to the molecules that are written from DNA. Like any other protein, TDP-43 has many vital bodily functions, as it regulates gene expression.
In patients with ALS (and sIBM as well as some other neuro-degenerative diseases), TDP-43 moves from the nucleus into the cytoplasm (main part of the cell) and clumps together there. This dysfunction, like most other protein dysfunction, causes the normal regulation of gene expression to fail, which is why the affected cells then die.
But how exactly do these affected proteins move out of the nucleus?
This is where acetylation comes into play. This method is actually commonly used by cells to switch protein activity on and off.
Scientists discovered that acetylation happens in two different areas on TDP-43, which causes the protein to detach itself from DNA molecules. This then prompts the protein to move to the cytoplasm and clump.
So now that we know all the science behind this protein which eventually may lead to ALS, it makes sense that scientists are excited about future ALS treatments.
Since it has worked in mouse models, researchers are optimistic for future human treatments soon, too.
To read more about this discovery and the science surrounding it, click this click here and head to Medical Xpress.
