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Nanoparticulate air pollution disrupts proteostasis in Caenorhabditis elegans

The proteostasis network comprises the biochemical pathways that together maintain and regulate proper protein synthesis, transport, folding, and degradation. Many progressive neurodegenerative diseases, such as Huntington’s disease (HD) and Alzheimer’s disease (AD), are characterized by an age-depe...

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Autores principales: Garcia Manriquez, Bailey A., Papapanagiotou, Julia A., Strysick, Claire A., Green, Emily H., Kikis, Elise A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9949623/
https://www.ncbi.nlm.nih.gov/pubmed/36821635
http://dx.doi.org/10.1371/journal.pone.0275137
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author Garcia Manriquez, Bailey A.
Papapanagiotou, Julia A.
Strysick, Claire A.
Green, Emily H.
Kikis, Elise A.
author_facet Garcia Manriquez, Bailey A.
Papapanagiotou, Julia A.
Strysick, Claire A.
Green, Emily H.
Kikis, Elise A.
author_sort Garcia Manriquez, Bailey A.
collection PubMed
description The proteostasis network comprises the biochemical pathways that together maintain and regulate proper protein synthesis, transport, folding, and degradation. Many progressive neurodegenerative diseases, such as Huntington’s disease (HD) and Alzheimer’s disease (AD), are characterized by an age-dependent failure of the proteostasis network to sustain the health of the proteome, resulting in protein misfolding, aggregation, and, often, neurotoxicity. Although important advances have been made in recent years to identify genetic risk factors for neurodegenerative diseases, we still know relatively little about environmental risk factors such as air pollution. Exposure to nano-sized particulate air pollution, referred to herein as nanoparticulate matter (nPM), has been shown to trigger the accumulation of misfolded and oligomerized amyloid beta (Aβ) in mice. Likewise, air pollution is known to exacerbate symptoms of AD in people. We asked whether nPM contributes to the misfolded protein load, thereby overwhelming the proteostasis network and triggering proteostasis decline. To address this, we utilized C. elegans that express reporter proteins that are sensitive to changes in the protein folding environment and respond by misfolding and displaying readily scorable phenotypes, such as localized YFP fluorescence or paralysis. We found that nPM exacerbated protein aggregation in body wall muscle cells, increasing the number of large visible protein aggregates, the amount of high molecular weight protein species, and proteotoxicity. Taken together, the data point to nPM negatively impacting proteostasis. Therefore, it seems plausible that nPM exposure may exacerbate symptoms of AD and age-related dementia in a manner that is at least partially dependent on proteostasis decline.
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spelling pubmed-99496232023-02-24 Nanoparticulate air pollution disrupts proteostasis in Caenorhabditis elegans Garcia Manriquez, Bailey A. Papapanagiotou, Julia A. Strysick, Claire A. Green, Emily H. Kikis, Elise A. PLoS One Research Article The proteostasis network comprises the biochemical pathways that together maintain and regulate proper protein synthesis, transport, folding, and degradation. Many progressive neurodegenerative diseases, such as Huntington’s disease (HD) and Alzheimer’s disease (AD), are characterized by an age-dependent failure of the proteostasis network to sustain the health of the proteome, resulting in protein misfolding, aggregation, and, often, neurotoxicity. Although important advances have been made in recent years to identify genetic risk factors for neurodegenerative diseases, we still know relatively little about environmental risk factors such as air pollution. Exposure to nano-sized particulate air pollution, referred to herein as nanoparticulate matter (nPM), has been shown to trigger the accumulation of misfolded and oligomerized amyloid beta (Aβ) in mice. Likewise, air pollution is known to exacerbate symptoms of AD in people. We asked whether nPM contributes to the misfolded protein load, thereby overwhelming the proteostasis network and triggering proteostasis decline. To address this, we utilized C. elegans that express reporter proteins that are sensitive to changes in the protein folding environment and respond by misfolding and displaying readily scorable phenotypes, such as localized YFP fluorescence or paralysis. We found that nPM exacerbated protein aggregation in body wall muscle cells, increasing the number of large visible protein aggregates, the amount of high molecular weight protein species, and proteotoxicity. Taken together, the data point to nPM negatively impacting proteostasis. Therefore, it seems plausible that nPM exposure may exacerbate symptoms of AD and age-related dementia in a manner that is at least partially dependent on proteostasis decline. Public Library of Science 2023-02-23 /pmc/articles/PMC9949623/ /pubmed/36821635 http://dx.doi.org/10.1371/journal.pone.0275137 Text en © 2023 Garcia Manriquez et al https://creativecommons.org/licenses/by/4.0/This is an open access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
spellingShingle Research Article
Garcia Manriquez, Bailey A.
Papapanagiotou, Julia A.
Strysick, Claire A.
Green, Emily H.
Kikis, Elise A.
Nanoparticulate air pollution disrupts proteostasis in Caenorhabditis elegans
title Nanoparticulate air pollution disrupts proteostasis in Caenorhabditis elegans
title_full Nanoparticulate air pollution disrupts proteostasis in Caenorhabditis elegans
title_fullStr Nanoparticulate air pollution disrupts proteostasis in Caenorhabditis elegans
title_full_unstemmed Nanoparticulate air pollution disrupts proteostasis in Caenorhabditis elegans
title_short Nanoparticulate air pollution disrupts proteostasis in Caenorhabditis elegans
title_sort nanoparticulate air pollution disrupts proteostasis in caenorhabditis elegans
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9949623/
https://www.ncbi.nlm.nih.gov/pubmed/36821635
http://dx.doi.org/10.1371/journal.pone.0275137
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