Abstract
Amyloidoses are a group of diseases associated with the formation of pathological protein fibrils with cross-β structures. Approximately 5–10% of the cases of these diseases are determined by amyloidogenic mutations, as well as by transmission of infectious amyloids (prions) between organisms. The most common group of so-called sporadic amyloidoses is associated with abnormal aggregation of wild-type proteins. Some sporadic amyloidoses are known to be induced only against the background of certain pathologies, but in some cases the cause of amyloidosis is unclear. It is assumed that these diseases often occur by accident. Here we present facts and hypotheses about the association of sporadic amyloidoses with vascular pathologies, trauma, oxidative stress, cancer, metabolic diseases, chronic infections and COVID-19. Generalization of current data shows that all sporadic amyloidoses can be regarded as a secondary event occurring against the background of diseases provoking a cellular stress response. Various factors causing the stress response provoke protein overproduction, a local increase in the concentration or modifications, which contributes to amyloidogenesis. Progress in the treatment of vascular, metabolic and infectious diseases, as well as cancers, should lead to a significant reduction in the risk of sporadic amyloidoses.
Highlights
90% of all cases of amyloid diseases belong to the group of sporadic amyloidoses
In the case of genetically determined amyloidoses, the pathology is associated with the occurrence of mutations that provoke amyloidogenesis
The data presented in this review indicate that sporadic amyloidoses can be regarded as a secondary event occurring against the background of diseases provoking a cellular stress response (Table 1) For the majority of proteins included in this group, it was shown that certain factors cause their overproduction, which promotes amyloidogenesis (Table 1)
Summary
Publisher’s Note: MDPI stays neutral with regard to jurisdictional claims in published maps and institutional affiliations. Pathological amyloid fibrils are formed as a result of protein misfolding, which can be provoked by various factors. Certain infectious properties have been shown for some other amyloid proteins, such as α-synuclein and tau [9,10,11,12], but the natural foodborne transmission is indicated only for PrPSc. The group of amyloidoses associated with mutations that promote protein aggregation is extensive. Mutations in several genes have been shown to contribute to the accumulation and aggregation of amyloid peptide beta (Aβ), which causes neurotoxicity in Alzheimer’s disease [14]. Some sporadic amyloidoses are known to be induced only against the background of certain pathologies, but in some cases the cause of amyloidosis is not so obvious.
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