The incorrect folding of proteins and their involvement with pathological processes

Abstract

During synthesis and the period in which they exert their cellular function, there is monitoring so that the proteins maintain a certain three-dimensional folding, where their energy levels are stabilized and their biological activity is maintained. Changes in cellular conditions can modify this structure, favoring its aggregation into insoluble complexes, called amyloidosis, depositing in the intra or extracellular environment. Recent data indicate that several types of proteins are involved in some type of amyloidosis, presenting a systemic character, or depositing in a specific tissue. The classification used for these cases considers the amyloid source, the pathology, and the organ affected. Protein fragments derived from immunoglobulin light and heavy chains are responsible for primary systemic amyloidosis. In secondary amyloidosis, there is the participation of circulating plasma protein, acting in inflammatory processes in different organs. Dialysis-related amyloidosis, on the other hand, is characterized by damage to bone tissues and joints in patients with chronic kidney disease. Most studies related to localized amyloidosis involve neurodegenerative diseases such as Alzheimer's and Parkinson's diseases. These heterogeneous pathologies associated with the incorrect folding of proteins are subject to genetic influence, which is increasingly evidenced, despite their multifactorial character. Deficiencies in the cellular proteostasis processes, i.e., in the surveillance that confers the quality control of these proteins, leading to their recovery or sending them for recycling, tend to increase with age. For this reason, most of the time these amyloidoses are related to the individual's aging processes.

DOI:https://doi.org/10.56238/innovhealthknow-033