Disaggregases as the Basis for Therapies to Remove Amyloids

A few proteins in the body are capable of misfolding or becoming otherwise altered in ways that encourage other molecules of the same protein to do the same. They can spread throughout a tissue and the body, given time, forming aggregates that precipitate into solid clumps and fibrils, surrounded by a halo of toxic biochemistry that harms cells. This is an age-related problem, likely because the systems of maintenance and recycling responsible for clearing aggregates falter with age, a victim of rising levels of molecular damage and the maladaptive reactions to that damage. Amyloid-β, associated with Alzheimer's disease, is likely the most well studied of the amyloids, with transthyretin amyloid a close second. In the case of amyloid-β, immunotherapies have proven themselves capable of clearing this molecular waste, though without achieving patient benefits as a result. For transthyretin amyloid, existing therapies slow the aggregation process. A few other approaches that clear existing aggregates are in development but either stalled (CPHPC) or not moving forward as fast as we'd like (catabodies). In today's open access paper, researchers discuss disaggregases as a basis for the clearance of amyloids. Disaggregases are a broad class of molecules capable of breaking apart amyloid aggregates. Some exist in the human body, well known parts of cellular stress response systems, some might be mined from other species. It is an interesting topic, and not that well e...
Source: Fight Aging! - Category: Research Authors: Tags: Medicine, Biotech, Research Source Type: blogs