The prion-like transmission of tau oligomers via exosomes

Noel A. Jackson, Marcos J. Guerrero-Muñoz, Diana L. Castillo-Carranza*

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review

8 Citations (Scopus)


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.

Original languageEnglish
Article number974414
Pages (from-to)974414
JournalFrontiers in Aging Neuroscience
Publication statusPublished - 18 Aug 2022

Bibliographical note

Funding Information:
This work was supported by the UIN21517 School of Medicine, University of Monterrey.

Publisher Copyright:
Copyright © 2022 Jackson, Guerrero-Muñoz and Castillo-Carranza.

All Science Journal Classification (ASJC) codes

  • Ageing
  • Cognitive Neuroscience


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