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Magnetite-Amyloid-β deteriorates activity and functional organization in an in vitro model for Alzheimer’s disease
The understanding of the key mechanisms behind human brain deterioration in Alzheimer’ disease (AD) is a highly active field of research. The most widespread hypothesis considers a cascade of events initiated by amyloid-β peptide fibrils that ultimately lead to the formation of the lethal amyloid pl...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4660300/ https://www.ncbi.nlm.nih.gov/pubmed/26608215 http://dx.doi.org/10.1038/srep17261 |
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author | Teller, Sara Tahirbegi, Islam Bogachan Mir, Mònica Samitier, Josep Soriano, Jordi |
author_facet | Teller, Sara Tahirbegi, Islam Bogachan Mir, Mònica Samitier, Josep Soriano, Jordi |
author_sort | Teller, Sara |
collection | PubMed |
description | The understanding of the key mechanisms behind human brain deterioration in Alzheimer’ disease (AD) is a highly active field of research. The most widespread hypothesis considers a cascade of events initiated by amyloid-β peptide fibrils that ultimately lead to the formation of the lethal amyloid plaques. Recent studies have shown that other agents, in particular magnetite, can also play a pivotal role. To shed light on the action of magnetite and amyloid-β in the deterioration of neuronal circuits, we investigated their capacity to alter spontaneous activity patterns in cultured neuronal networks. Using a versatile experimental platform that allows the parallel monitoring of several cultures, the activity in controls was compared with the one in cultures dosed with magnetite, amyloid-β and magnetite-amyloid-β complex. A prominent degradation in spontaneous activity was observed solely when amyloid-β and magnetite acted together. Our work suggests that magnetite nanoparticles have a more prominent role in AD than previously thought, and may bring new insights in the understanding of the damaging action of magnetite-amyloid-β complex. Our experimental system also offers new interesting perspectives to explore key biochemical players in neurological disorders through a controlled, model system manner. |
format | Online Article Text |
id | pubmed-4660300 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | Nature Publishing Group |
record_format | MEDLINE/PubMed |
spelling | pubmed-46603002015-11-30 Magnetite-Amyloid-β deteriorates activity and functional organization in an in vitro model for Alzheimer’s disease Teller, Sara Tahirbegi, Islam Bogachan Mir, Mònica Samitier, Josep Soriano, Jordi Sci Rep Article The understanding of the key mechanisms behind human brain deterioration in Alzheimer’ disease (AD) is a highly active field of research. The most widespread hypothesis considers a cascade of events initiated by amyloid-β peptide fibrils that ultimately lead to the formation of the lethal amyloid plaques. Recent studies have shown that other agents, in particular magnetite, can also play a pivotal role. To shed light on the action of magnetite and amyloid-β in the deterioration of neuronal circuits, we investigated their capacity to alter spontaneous activity patterns in cultured neuronal networks. Using a versatile experimental platform that allows the parallel monitoring of several cultures, the activity in controls was compared with the one in cultures dosed with magnetite, amyloid-β and magnetite-amyloid-β complex. A prominent degradation in spontaneous activity was observed solely when amyloid-β and magnetite acted together. Our work suggests that magnetite nanoparticles have a more prominent role in AD than previously thought, and may bring new insights in the understanding of the damaging action of magnetite-amyloid-β complex. Our experimental system also offers new interesting perspectives to explore key biochemical players in neurological disorders through a controlled, model system manner. Nature Publishing Group 2015-11-26 /pmc/articles/PMC4660300/ /pubmed/26608215 http://dx.doi.org/10.1038/srep17261 Text en Copyright © 2015, Macmillan Publishers Limited http://creativecommons.org/licenses/by/4.0/ This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ |
spellingShingle | Article Teller, Sara Tahirbegi, Islam Bogachan Mir, Mònica Samitier, Josep Soriano, Jordi Magnetite-Amyloid-β deteriorates activity and functional organization in an in vitro model for Alzheimer’s disease |
title | Magnetite-Amyloid-β deteriorates activity and functional organization in an in vitro model for Alzheimer’s disease |
title_full | Magnetite-Amyloid-β deteriorates activity and functional organization in an in vitro model for Alzheimer’s disease |
title_fullStr | Magnetite-Amyloid-β deteriorates activity and functional organization in an in vitro model for Alzheimer’s disease |
title_full_unstemmed | Magnetite-Amyloid-β deteriorates activity and functional organization in an in vitro model for Alzheimer’s disease |
title_short | Magnetite-Amyloid-β deteriorates activity and functional organization in an in vitro model for Alzheimer’s disease |
title_sort | magnetite-amyloid-β deteriorates activity and functional organization in an in vitro model for alzheimer’s disease |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4660300/ https://www.ncbi.nlm.nih.gov/pubmed/26608215 http://dx.doi.org/10.1038/srep17261 |
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