TY - JOUR

T1 - Interaction of Proteins Involved in Neuronal Proteinopathies

AU - Kulichikhin, Konstantin Yu.

AU - Malikova, Oksana A.

AU - Zobnina, Anastasia E.

AU - Zalutskaya, Natalia M.

AU - Rubel, Aleksandr A.

PY - 2023/9/23

Y1 - 2023/9/23

N2 - Proteinopathy is characterized by the accumulation of aggregates of a specific protein in a target organ, tissue, or cell. The aggregation of the same protein can cause different pathologies as single protein can adopt various amyloidogenic, disease-specific conformations. The conformation governs the interaction of amyloid aggregates with other proteins that are prone to misfolding and, thus, determines disease-specific spectrum of concomitant pathologies. In this regard, a detailed description of amyloid protein conformation as well as spectrum of its interaction with other proteins become a key point for drafting of precise description of the disease. The majority of clinical cases of neuronal proteinopathies is caused by the aggregation of rather limited range of amyloidogenic proteins. Here, we provided the characterization of pathologies, related to the aggregation of amyloid β peptide, tau protein, α-synuclein, TDP-43, and amylin, giving a short description of pathologies themselves, recent advances in elucidation of misfolded protein conformation, with emphasis on those protein aggregates extracted from biological samples, what is known about the interaction of this proteins, and the influence of this interaction on the progression of underlying disease and comorbidities.

AB - Proteinopathy is characterized by the accumulation of aggregates of a specific protein in a target organ, tissue, or cell. The aggregation of the same protein can cause different pathologies as single protein can adopt various amyloidogenic, disease-specific conformations. The conformation governs the interaction of amyloid aggregates with other proteins that are prone to misfolding and, thus, determines disease-specific spectrum of concomitant pathologies. In this regard, a detailed description of amyloid protein conformation as well as spectrum of its interaction with other proteins become a key point for drafting of precise description of the disease. The majority of clinical cases of neuronal proteinopathies is caused by the aggregation of rather limited range of amyloidogenic proteins. Here, we provided the characterization of pathologies, related to the aggregation of amyloid β peptide, tau protein, α-synuclein, TDP-43, and amylin, giving a short description of pathologies themselves, recent advances in elucidation of misfolded protein conformation, with emphasis on those protein aggregates extracted from biological samples, what is known about the interaction of this proteins, and the influence of this interaction on the progression of underlying disease and comorbidities.

KW - amyloid β peptide

KW - tau protein

KW - α-synuclein

KW - TDP-43

KW - amylin

KW - protein misfolding

KW - proteinopathy

KW - disease-specific conformation

KW - protein interaction

UR - https://www.mdpi.com/2075-1729/13/10/1954/xml

UR - https://www.mendeley.com/catalogue/41e533d2-0d27-3b7e-8712-1a700857ddfe/

U2 - 10.3390/life13101954

DO - 10.3390/life13101954

M3 - Review article

VL - 13

JO - Life

JF - Life

SN - 0024-3019

IS - 10

M1 - 1954

ER -