Propagation of tau via extracellular vesicles

Extracellular vesicles (EVs), like exosomes, play a critical role in physiological processes, including synaptic transmission and nerve regeneration. However, exosomes in particular can also contribute to the development of neurodegenerative conditions such as Alzheimer’s disease (AD), Parkinson’s d...

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Bibliographic Details
Authors: Pérez, Mar, Ávila, Jesús, Hernández, Félix
Format: article
Status:Published version
Publication Date:2019
Country:España
Institution:Consejo Superior de Investigaciones Científicas (CSIC)
Repository:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/215267
Online Access:http://hdl.handle.net/10261/215267
Access Level:Open access
Keyword:Tau propagation
Extracellular vesicles
Neurodegenerative diseases
Tau protein
Alzheimer’s disease
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spelling Propagation of tau via extracellular vesiclesPérez, MarÁvila, JesúsHernández, FélixTau propagationExtracellular vesiclesNeurodegenerative diseasesTau proteinAlzheimer’s diseaseExtracellular vesicles (EVs), like exosomes, play a critical role in physiological processes, including synaptic transmission and nerve regeneration. However, exosomes in particular can also contribute to the development of neurodegenerative conditions such as Alzheimer’s disease (AD), Parkinson’s disease, and prion diseases. All of these disorders are characterized by protein aggregation and deposition in specific regions of the brain. Several lines of evidence indicate that protein in exosomes is released from affected neurons and propagated along neuroanatomically connected regions of the brain, thus spreading the neurodegenerative disease. Also, different cell types contribute to the progression of tauopathy, such as microglia. Several groups have reported tau release via exosomes by cultured neurons or cells overexpressing human tau. Although the exact mechanisms underlying the propagation of protein aggregates are not fully understood, recent findings have implicated EVs in this process. The AD brain has two hallmarks, namely the presence of amyloid-β-containing plaques and neurofibrillary tangles, the latter formed by hyperphosphorylated tau protein. Both amyloid peptide and tau protein are present in specific exosomes. This review summarizes recent advances in our understanding of exosomes in the pathology of AD, with a special focus on tau protein.Spanish Ministry of Science, Innovation and Universities (BFU2016-77885-P), the Comunidad de Madrid, through EU structural funds (S2017/BMD-3700 NEUROMETAD-CM), CIBERNED (ISCIII), and the Fundacion Ramon ArecesMinisterio de Ciencia, Innovación y Universidades (España)Comunidad de MadridEuropean CommissionCentro Investigación Biomédica en Red Enfermedades Neurodegenerativas (España)Fundación Ramón ArecesConsejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]2020202020192020info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Publisher's versioninfo:eu-repo/semantics/publishedVersionhttp://hdl.handle.net/10261/215267reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Ingléshttp://dx.doi.org/10.3389/fnins.2019.00698Síinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/2152672026-05-22T06:33:51Z
dc.title.none.fl_str_mv Propagation of tau via extracellular vesicles
title Propagation of tau via extracellular vesicles
spellingShingle Propagation of tau via extracellular vesicles
Pérez, Mar
Tau propagation
Extracellular vesicles
Neurodegenerative diseases
Tau protein
Alzheimer’s disease
title_short Propagation of tau via extracellular vesicles
title_full Propagation of tau via extracellular vesicles
title_fullStr Propagation of tau via extracellular vesicles
title_full_unstemmed Propagation of tau via extracellular vesicles
title_sort Propagation of tau via extracellular vesicles
dc.creator.none.fl_str_mv Pérez, Mar
Ávila, Jesús
Hernández, Félix
author Pérez, Mar
author_facet Pérez, Mar
Ávila, Jesús
Hernández, Félix
author_role author
author2 Ávila, Jesús
Hernández, Félix
author2_role author
author
dc.contributor.none.fl_str_mv Ministerio de Ciencia, Innovación y Universidades (España)
Comunidad de Madrid
European Commission
Centro Investigación Biomédica en Red Enfermedades Neurodegenerativas (España)
Fundación Ramón Areces
Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
dc.subject.none.fl_str_mv Tau propagation
Extracellular vesicles
Neurodegenerative diseases
Tau protein
Alzheimer’s disease
topic Tau propagation
Extracellular vesicles
Neurodegenerative diseases
Tau protein
Alzheimer’s disease
description Extracellular vesicles (EVs), like exosomes, play a critical role in physiological processes, including synaptic transmission and nerve regeneration. However, exosomes in particular can also contribute to the development of neurodegenerative conditions such as Alzheimer’s disease (AD), Parkinson’s disease, and prion diseases. All of these disorders are characterized by protein aggregation and deposition in specific regions of the brain. Several lines of evidence indicate that protein in exosomes is released from affected neurons and propagated along neuroanatomically connected regions of the brain, thus spreading the neurodegenerative disease. Also, different cell types contribute to the progression of tauopathy, such as microglia. Several groups have reported tau release via exosomes by cultured neurons or cells overexpressing human tau. Although the exact mechanisms underlying the propagation of protein aggregates are not fully understood, recent findings have implicated EVs in this process. The AD brain has two hallmarks, namely the presence of amyloid-β-containing plaques and neurofibrillary tangles, the latter formed by hyperphosphorylated tau protein. Both amyloid peptide and tau protein are present in specific exosomes. This review summarizes recent advances in our understanding of exosomes in the pathology of AD, with a special focus on tau protein.
publishDate 2019
dc.date.none.fl_str_mv 2019
2020
2020
2020
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
Publisher's version
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/215267
url http://hdl.handle.net/10261/215267
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv http://dx.doi.org/10.3389/fnins.2019.00698
Sí
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.source.none.fl_str_mv reponame:DIGITAL.CSIC. Repositorio Institucional del CSIC
instname:Consejo Superior de Investigaciones Científicas (CSIC)
instname_str Consejo Superior de Investigaciones Científicas (CSIC)
reponame_str DIGITAL.CSIC. Repositorio Institucional del CSIC
collection DIGITAL.CSIC. Repositorio Institucional del CSIC
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score 15,811543

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