The prion-like transmission of tau oligomers via exosomes

The conversion and transmission of misfolded proteins established the basis for the prion concept. Neurodegenerative diseases are considered “prion-like” disorders that lack infectivity. Among them, tauopathies are characterized by the conversion of native tau protein into an abnormally folded aggre...

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Main Authors: Noel A. Jackson, Marcos J. Guerrero-Muñoz, Diana L. Castillo-Carranza
Format: Article
Language:English
Published: Frontiers Media S.A. 2022-08-01
Series:Frontiers in Aging Neuroscience
Subjects:
Online Access:https://www.frontiersin.org/articles/10.3389/fnagi.2022.974414/full
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author Noel A. Jackson
Marcos J. Guerrero-Muñoz
Diana L. Castillo-Carranza
author_facet Noel A. Jackson
Marcos J. Guerrero-Muñoz
Diana L. Castillo-Carranza
author_sort Noel A. Jackson
collection DOAJ
description The conversion and transmission of misfolded proteins established the basis for the prion concept. Neurodegenerative diseases are considered “prion-like” disorders that lack infectivity. Among them, tauopathies are characterized by the conversion of native tau protein into an abnormally folded aggregate. During the progression of the disease, misfolded tau polymerizes into oligomers and intracellular neurofibrillary tangles (NFTs). While the toxicity of NFTs is an ongoing debate, the contribution of tau oligomers to early onset neurodegenerative pathogenesis is accepted. Tau oligomers are readily transferred from neuron to neuron propagating through the brain inducing neurodegeneration. Recently, transmission of tau oligomers via exosomes is now proposed. There is still too much to uncover about tau misfolding and propagation. Here we summarize novel findings of tau oligomers transmission and propagation via exosomes.
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spelling doaj.art-72d7ffaa19c54038a2398e1c629fd6a42022-12-22T01:43:08ZengFrontiers Media S.A.Frontiers in Aging Neuroscience1663-43652022-08-011410.3389/fnagi.2022.974414974414The prion-like transmission of tau oligomers via exosomesNoel A. Jackson0Marcos J. Guerrero-Muñoz1Diana L. Castillo-Carranza2School of Public Health, Harvard University, Boston, MA, United StatesSchool of Medicine, University of Monterrey, San Pedro Garza García, MexicoSchool of Medicine, University of Monterrey, San Pedro Garza García, MexicoThe conversion and transmission of misfolded proteins established the basis for the prion concept. Neurodegenerative diseases are considered “prion-like” disorders that lack infectivity. Among them, tauopathies are characterized by the conversion of native tau protein into an abnormally folded aggregate. During the progression of the disease, misfolded tau polymerizes into oligomers and intracellular neurofibrillary tangles (NFTs). While the toxicity of NFTs is an ongoing debate, the contribution of tau oligomers to early onset neurodegenerative pathogenesis is accepted. Tau oligomers are readily transferred from neuron to neuron propagating through the brain inducing neurodegeneration. Recently, transmission of tau oligomers via exosomes is now proposed. There is still too much to uncover about tau misfolding and propagation. Here we summarize novel findings of tau oligomers transmission and propagation via exosomes.https://www.frontiersin.org/articles/10.3389/fnagi.2022.974414/fulltau oligomersexosomesvesiclesmisfoldingspreadingprion
spellingShingle Noel A. Jackson
Marcos J. Guerrero-Muñoz
Diana L. Castillo-Carranza
The prion-like transmission of tau oligomers via exosomes
Frontiers in Aging Neuroscience
tau oligomers
exosomes
vesicles
misfolding
spreading
prion
title The prion-like transmission of tau oligomers via exosomes
title_full The prion-like transmission of tau oligomers via exosomes
title_fullStr The prion-like transmission of tau oligomers via exosomes
title_full_unstemmed The prion-like transmission of tau oligomers via exosomes
title_short The prion-like transmission of tau oligomers via exosomes
title_sort prion like transmission of tau oligomers via exosomes
topic tau oligomers
exosomes
vesicles
misfolding
spreading
prion
url https://www.frontiersin.org/articles/10.3389/fnagi.2022.974414/full
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