期刊
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
卷 22, 期 22, 页码 -出版社
MDPI
DOI: 10.3390/ijms222212193
关键词
neurodegeneration; proteinopathy; metallopathy; protein aggregation; amyloid; metal exposure; metal-protein binding
资金
- Kamprad Research Foundation
- Magnus Bergvall Foundation
- Ulla-Carin Lindquist Foundation for ALS Research
- Karolinska Institutet IMM strategic grants
ALS, Alzheimer's disease, Parkinson's disease and other neurodegenerative disorders have a significant impact on patients, caregivers, and society due to the aggregation of proteins in nerve cells. TDP-43 seems to play a specific role in ALS pathogenesis, and further research is needed on the role of metals in TDP-43 aggregation.
Amyotrophic lateral sclerosis (ALS), Alzheimer's disease, Parkinson's disease and similar neurodegenerative disorders take their toll on patients, caregivers and society. A common denominator for these disorders is the accumulation of aggregated proteins in nerve cells, yet the triggers for these aggregation processes are currently unknown. In ALS, protein aggregation has been described for the SOD1, C9orf72, FUS and TDP-43 proteins. The latter is a nuclear protein normally binding to both DNA and RNA, contributing to gene expression and mRNA life cycle regulation. TDP-43 seems to have a specific role in ALS pathogenesis, and ubiquitinated and hyperphosphorylated cytoplasmic inclusions of aggregated TDP-43 are present in nerve cells in almost all sporadic ALS cases. ALS pathology appears to include metal imbalances, and environmental metal exposure is a known risk factor in ALS. However, studies on metal-to-TDP-43 interactions are scarce, even though this protein seems to have the capacity to bind to metals. This review discusses the possible role of metals in TDP-43 aggregation, with respect to ALS pathology.
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