ALS Latest News And Discovery: Scientists Reversed Clumping Of Protein Involved In Death Of Neurons That Causes ALS

Amyotrophic Lateral Sclerosis or most popularly known as ALS is a progressive neurodegenerative disease that affects nerve cells in the brain and the spinal cord. There is still no known cure for the debilitating disease, but a new research at the University of North Carolina has revealed that stabilizing a protein in the brain may help in reversing or preventing ALS.

According to Medical Xpress, in the efforts to understand what causes the neurodegenerative diseases, researchers in the past have pointed out that clumps of proteins that doesn't function well kill neurons in the brain and spinal cord by congesting their cellular machinery.

In the new study, published in the journal Structure, researchers at the UNC School of Medicine revealed that stabilizing a protein called SOD1 can help reverse the jamming process in the types of neurons by affected by the life-threatening Lou Gehrig's disease. The disease, also known popularly as ALS, still has no known cure and its causes remain to be a mystery.

As many may have already known, ALS causes gradual paralysis brought about by the death of motor neurons in the brain mainly responsible for moving, speaking, swallowing and breathing. This is one of the main reasons why the disease is thought to be a death sentence for people diagnosed with it. UPI reported that the new research followed up on cultured cells which were developed to model the mechanics of ALS. Researchers thought that finding a way to avoid SOD1 clumps from forming could potentially halt the disease from progressing.

"By slowly piecing together the larger story of how SOD1 acts, hopefully, that can be useful in drug studies to try to get a handle on how to affect the behavior of this protein in a planned way," Jimmy Fay, a graduate student at UNC, said in a press release. In a past study, researchers were able to learn that SOD1 forms temporary clumps which can kill motor neuron-like cells which were grown in the lab. The new study aims to figure out what makes SOD1 clump and if there are methods to prevent or reverse the clumping.

Bioscience Technology wrote that for researchers to test their hypothesis, they created a genetic mutation that would copy the addition of a phosphate group to the proteins in motor neuron-like cells in the lab. They found that the phosphate group, when added to the protein, stabilized it, which then allowed its normal clumping and dissolving to continue properly, instead of building up to cause the disease.

"When we transfected this new mutation into cells in concert with the disease mutation, it actually rescued toxicity; it made the cells not die," according to Faye. Instead of being killed by toxic clumps of SOD1 the cells survived, thanks to the phosphorylation-mimicking mutation.

Meanwhile, researchers also said that future studies will focus their energy on identifying drug targets to cause the anti-clumping mutation. Also, the findings may also give clues about why some people get ALS while others do not. If phosphorylation of SOD1 is found to be common in people without ALS, it could indicate that defects leading to reduced phosphorylation play a role in destabilizing SOD1, even in people without detrimental SOD1 mutations.