In a new study published in Nature Genetics, University of Pennsylvania researchers and colleagues have made inroads into the mechanism by which ALS acts. Working with a powerful fruit fly model of the disease, they found a way of reducing disease toxicity that slows the dysfunction of neurons and showing that a parallel mechanism can reduce toxicity in mammalian cells. Their discoveries offer the possibility of a new strategy for treating ALS.
Recognition that the mutations adversely impact regulation of RNA could lead to targeted therapy to correct the problem. The mutation’s location in the prion-like domain might also prove significant. Although the mutations in hnRNPA2B1 or hnRNPA1 appear to be rare, hundreds of other RNA-binding proteins have prion-like domains. Taylor said patients with unexplained neurodegenerative diseases may have mutations in these proteins.