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The role of TDP-43 propagation in neurodegenerative diseases: integrating insights from clinical and experimental studies

Experimental & Molecular Medicine 2020년 52권 10호 p.4 ~ 4
조명진, Lee Shin-Rye, 전유미, 김세연, Kwon Young-Hwi, 김형준,
소속 상세정보
조명진 ( Jo Myung-Jin ) - Korea Brain Research Institute Dementia Research Group
 ( Lee Shin-Rye ) - Korea Brain Research Institute Dementia Research Group
전유미 ( Jeon Yu-Mi ) - Korea Brain Research Institute Dementia Research Group
김세연 ( Kim Se-Yeon ) - Korea Brain Research Institute Dementia Research Group
 ( Kwon Young-Hwi ) - Korea Brain Research Institute Dementia Research Group
김형준 ( Kim Hyung-Jun ) - Korea Brain Research Institute Dementia Research Group

Abstract


TAR DNA-binding protein 43 (TDP-43) is a highly conserved nuclear RNA/DNA-binding protein involved in the regulation of RNA processing. The accumulation of TDP-43 aggregates in the central nervous system is a common feature of many neurodegenerative diseases, such as amyotrophic lateral sclerosis (ALS), frontotemporal dementia (FTD), Alzheimer’s disease (AD), and limbic predominant age-related TDP-43 encephalopathy (LATE). Accumulating evidence suggests that prion-like spreading of aberrant protein aggregates composed of tau, amyloid-β, and α-synuclein is involved in the progression of neurodegenerative diseases such as AD and PD. Similar to those of prion-like proteins, pathological aggregates of TDP-43 can be transferred from cell-to-cell in a seed-dependent and self-templating manner. Here, we review clinical and experimental studies supporting the prion-like spreading of misfolded TDP-43 and discuss the molecular mechanisms underlying the propagation of these pathological aggregated proteins. The idea that misfolded TDP-43 spreads in a prion-like manner between cells may guide novel therapeutic strategies for TDP-43-associated neurodegenerative diseases.

키워드

Neurodegeneration; Neurodegenerative diseases

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