Credit: EPFL / Galina Limorenko. Illustration depicting how exposingTDP-43 fibril core enhances pathology formation in cell.
Credit: EPFL / Galina Limorenko. Illustration depicting how exposingTDP-43 fibril core enhances pathology formation in cell. Scientists reproduce key features of pathological protein aggregates found in the brain of patients with Lou Gehrig's disease and other neurological diseases, providing insight into the underlying mechanism and offering promising avenues for new therapies. Several neurodegenerative diseases, such as Alzheimer's, Parkinson's, and Lou Gehrig's Disease aka Amyotrophic lateral sclerosis (ALS), are caused by proteins that go stray and start to aggregate into fibrils that accumulate in specific brain regions. Now, scientists have discovered a new mechanism that explains how the aggregates become pathological and spread to different regions of the brain. A main suspect is the highly unstable protein called TDP43. The scientists discovered that TDP43 aggregates that form in the brain are not implicitly pathogenic until they are processed to reveal their "sticky" core.
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