A Process Used by Cells to Ingest Misfolded Proteins Might be Enhanced to Treat Neurodegenerative Conditions

The aggregation of misfolded proteins is a feature of most neurodegenerative conditions: amyloid-β and tau in Alzheimer's disease, α-synuclein in Parkinson's disease, and so forth. These and a few more of the countless proteins present in the body can become altered, such as via misfolding, in ways that encourage other molecules of the same protein to also alter, forming structures of linked, harmful proteins that can spread through tissue or from cell to cell. Cells, particularly immune cells, are equipped with a range of mechanisms to identify and break down these problem proteins, but, for reasons that are not fully understood at the detail level, damage outpaces maintenance in the aging brain. Aggregates grow and spread, leaving a trail of cellular dysfunction and death in their wake. In today's research materials, scientists report on their exploration of a process by which cells ingest and break down misfolded extracellular proteins. Amyloid-β might be the most interesting example of such proteins, given its role in Alzheimer's disease. The researchers note evidence for upregulation of the operation of this maintenance process to reduce the impact of amyloid-β aggregation on brain tissue; we shall see whether this progresses to the point of producing therapies in the years ahead. Certainly researchers are quite interested in upregulating the operation of processes such as autophagy and proteasomal degradation of proteins that are focused on breaking down prob...
Source: Fight Aging! - Category: Research Authors: Tags: Medicine, Biotech, Research Source Type: blogs