Metals in ALS TDP-43 Pathology

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 ag...

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Autores principales:	Lassi Koski, Cecilia Ronnevi, Elina Berntsson, Sebastian K. T. S. Wärmländer, Per M. Roos
Formato:	article
Lenguaje:	EN
Publicado:	MDPI AG 2021
Materias:	neurodegeneration proteinopathy metallopathy protein aggregation amyloid metal exposure Biology (General) QH301-705.5 Chemistry QD1-999
Acceso en línea:	https://doaj.org/article/b34c068f4f6f42bf92d1c0a0cf70c15e
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spelling	oai:doaj.org-article:b34c068f4f6f42bf92d1c0a0cf70c15e2021-11-25T17:54:11ZMetals in ALS TDP-43 Pathology10.3390/ijms2222121931422-00671661-6596https://doaj.org/article/b34c068f4f6f42bf92d1c0a0cf70c15e2021-11-01T00:00:00Zhttps://www.mdpi.com/1422-0067/22/22/12193https://doaj.org/toc/1661-6596https://doaj.org/toc/1422-0067Amyotrophic 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.Lassi KoskiCecilia RonneviElina BerntssonSebastian K. T. S. WärmländerPer M. RoosMDPI AGarticleneurodegenerationproteinopathymetallopathyprotein aggregationamyloidmetal exposureBiology (General)QH301-705.5ChemistryQD1-999ENInternational Journal of Molecular Sciences, Vol 22, Iss 12193, p 12193 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	neurodegeneration proteinopathy metallopathy protein aggregation amyloid metal exposure Biology (General) QH301-705.5 Chemistry QD1-999
spellingShingle	neurodegeneration proteinopathy metallopathy protein aggregation amyloid metal exposure Biology (General) QH301-705.5 Chemistry QD1-999 Lassi Koski Cecilia Ronnevi Elina Berntsson Sebastian K. T. S. Wärmländer Per M. Roos Metals in ALS TDP-43 Pathology
description	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.
format	article
author	Lassi Koski Cecilia Ronnevi Elina Berntsson Sebastian K. T. S. Wärmländer Per M. Roos
author_facet	Lassi Koski Cecilia Ronnevi Elina Berntsson Sebastian K. T. S. Wärmländer Per M. Roos
author_sort	Lassi Koski
title	Metals in ALS TDP-43 Pathology
title_short	Metals in ALS TDP-43 Pathology
title_full	Metals in ALS TDP-43 Pathology
title_fullStr	Metals in ALS TDP-43 Pathology
title_full_unstemmed	Metals in ALS TDP-43 Pathology
title_sort	metals in als tdp-43 pathology
publisher	MDPI AG
publishDate	2021
url	https://doaj.org/article/b34c068f4f6f42bf92d1c0a0cf70c15e
work_keys_str_mv	AT lassikoski metalsinalstdp43pathology AT ceciliaronnevi metalsinalstdp43pathology AT elinaberntsson metalsinalstdp43pathology AT sebastianktswarmlander metalsinalstdp43pathology AT permroos metalsinalstdp43pathology
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Metals in ALS TDP-43 Pathology

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