A study reported in Structure provides clues that stabilizing SOD1 could reverse harmful protein clumping in Amyotrophic Lateral Sclerosis (ALS). The study is from scientists at UNC School of Medicine. They have also found a method to mutate disease-associated SOD1 to prevent it from clumping. ALS is also referred to as motor neurone disease (MND), or Lou Gehrig's disease. It affects people's motor neurons found in the brain and spinal cord. As the disease progresses, it can lead to muscle weaknes, severe disability, and even death. Currently ALS is an incurable disease whose cause is unknown. The majority of patients with the fatal disorder die within 2-5 years of diagnosis. Familial ALS takes up approximately 10 percent of all disease cases. The new study was based on previous research in which scientists used cells to model the mechanics of ALS. SOD1 forms temporary clumps capable of destroying motor neuron-like cells in vitro. In this work, scientists continued to study why SOD1 clumps and whether it would be stopped by certain methods. According to study co-author Jimmy Fay, these studies might help us control the behavior of SOD1. The study showed that adding a phosphate group to SOD1 could stabilize it, allowing its normal clumping and dissipating to continue properly, instead clumps building up to cause disease. The scientists also identified a mutation to mimic the phosphorylation process. Previously, the scientists used cultured cells to explore the mechanics of ALS, and the SOD1 proteins form harmful clumps in these cells. In this study, they introduced a mutation that would mimic the addition of a phosphate group to SOD1 proteins in these cells, and found that these cells did not die. This mutation reversed the harmful clumps of SOD1. If you need Recombinant ITGB1, SOD1 and other proteins, please contact CusAb.
