Accumulation of aggregated alpha-synuclein in neural tissue structures in neurodegenerative diseases

Abstract

A critical analysis of the literature on the structure and properties of alpha-synuclein under physiological and pathological conditions is presented, when the conformation of this protein changes, which contributes to its aggregation and changes in localization features in brain structures in such neurodegenerative diseases as Parkinson’s disease, dementia with Lewy bodies, multiple systemic atrophy and Alzheimer’s disease. It has been shown that the toxic effect of conformationally altered alpha-synuclein can indirectly affect the functions of neurons due to its interaction with neuroglial cells, primarily microglia and astrocytes, and can also modulate the aggregation and expression of other proteins that are functionally important for the development of neurodegeneration. Further study of the mechanisms of interaction of conformationally altered alphasynuclein with other proteins and clarification of the relationship between its accumulation in brain structures and neuronal dysfunction remains relevant for modern neurology. Literature search was carried out in the “PubMed” and “eLIBRARY” databases.