Protein aggregation in neurodegenerative diseases.
10.1097/CM9.0000000000003802
- Author:
Jiannan WANG
1
;
Lijun DAI
2
;
Zhentao ZHANG
1
Author Information
1. Department of Neurology, Renmin Hospital of Wuhan University, Wuhan, Hubei 430060, China.
2. Center for Neurodegenerative Disease Research, Renmin Hospital of Wuhan University, Wuhan, Hubei 430060, China.
- Publication Type:Review
- Keywords:
Alzheimer’s disease;
Amyloid-β;
Amyotrophic lateral sclerosis;
Biomarker;
Huntington’s disease;
Parkinson’s disease;
Tau;
α-synuclein
- MeSH:
Humans;
Neurodegenerative Diseases/metabolism*;
alpha-Synuclein/metabolism*;
Amyloid beta-Peptides/metabolism*;
tau Proteins/metabolism*;
Protein Aggregation, Pathological/metabolism*;
DNA-Binding Proteins/metabolism*;
Animals;
Protein Aggregates/physiology*
- From:
Chinese Medical Journal
2025;138(21):2753-2768
- CountryChina
- Language:English
-
Abstract:
Neurodegenerative diseases constitute a group of chronic disorders characterized by the progressive loss of neurons. Major neurodegenerative conditions include Alzheimer's disease, Parkinson's disease, Huntington's disease, frontotemporal lobar degeneration, and amyotrophic lateral sclerosis. Pathologically, these diseases are marked by the accumulation of aggregates formed by pathological proteins such as amyloid-β, tau, α-synuclein, and TAR DNA-binding protein 43. These proteins assemble into amyloid fibrils that undergo prion-like propagation and dissemination, ultimately inducing neurodegeneration. Understanding the biology of these protein aggregates is fundamental to elucidating the pathophysiology of neurodegenerative disorders. In this review, we summarize the molecular mechanisms underlying the aggregation and transmission of pathological proteins, the processes through which these protein aggregates trigger neurodegeneration, and the interactions between different pathological proteins. We also provide an overview of the current diagnostic approaches and therapeutic strategies targeting pathological protein aggregates.