Improved Quality Control of Protein Folding Extends Life in Nematode Worms

In the paper I'll point out today, researchers map an efficient form of protein quality control from stem cells and recreate it in somatic cells, producing extended life in nematode worms as a result. Proteins are large, complex molecules, and their correct function depends on the assumption of a precise three-dimensional arrangement after creation, a process known as protein folding. Proteins can and do misfold, however, and in doing so many become actively harmful rather than merely unwanted clutter. A baroque system of chaperone proteins assists in correct folding, as well as identification and removal of misfolded molecules. The presence of misfolded proteins is effectively a form of damage: some of the molecular waste that accumulates with age and contributes to the development of age-related disease consists of misfolded proteins, such as the various forms of amyloid, for example. The gradual failure of cellular recycling systems, such as declining lysosomal function caused by the presence of metabolic waste that is hard for the body to break down, or similar failures in the proteasome, also contribute to rising levels of damaged and dysfunctional proteins. Since aging is nothing more than the accumulation of damage and the reactions to that damage, more efficient operation of chaperone and other quality control systems in cells should slow aging: the less damage there is at any one time, the less of an opportunity that damage has to spread and cause secondary issues. I...
Source: Fight Aging! - Category: Research Authors: Tags: Medicine, Biotech, Research Source Type: blogs