Can Existing Mechanisms be Enhanced to Clear Age-Related Protein Aggregates?

Human biochemistry does include systems capable of breaking down or otherwise removing the hyperphosphorylated tau protein deposits observed to be associated with the neurodegenerative conditions known as tauopathies, a class that includes Alzheimer's disease. Obviously, these mechanisms are far from adequate in the normal operation of aged metabolism, but could they be boosted to effectively clear out deposits of broken proteins? That is essentially what is taking place in the development of immunotherapies to clear out β-amyloid and tau in Alzheimer's patients, harnessing the immune system to the task. But are there other, more fundamental approaches that may just involve enhancing the amounts or activities of specific proteins? The research here suggests that this might be the case. Inside the cell, proteins need to be folded to be functional and active. Molecular chaperones are key enzymes that assist in folding proteins by stabilizing nascent polypeptide chains and by facilitating interactions that help stabilize a final structure. These chaperones also prevent the aggregation of newly formed proteins and can shunt misfolded proteins toward degradation pathways. In addition to interacting with newly synthesized proteins, chaperones also help to maintain cellular homeostasis by triaging toxic protein aggregates, which are responsible for causing neurodegenerative diseases. Two proteins that can form these toxic aggregates are tau and α-synuclein, which f...
Source: Fight Aging! - Category: Research Authors: Tags: Daily News Source Type: blogs