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The prion-like transmission of tau oligomers via exosomes

*Corresponding author for this work
  • Harvard University
    ,
  • Universidad de Monterrey
    ,
  • ,
  • Vice-Presidency of Academic Affairs in Health Sciences
Research Output:
Contribution to journal
Review article
Peer-review

Open access

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SciVal
Citations
39
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FWCI
0.90
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Author count
3
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68
Scopus
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Abstract

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.

Publication Information

Output type

Research Output:
Contribution to journal
Review article
Peer-review

Original language

English

Article number

974414

Pages from-to (Number of pages)

Pages 974414

Journal (Volume, Issue Number)

Frontiers in Aging Neuroscience (Volume 14)

Publication milestones

  • Published - 18/08/2022

Publication status

Published - 18/08/2022

ISSN

1663-4365

Publication IDs

  • Scopus: 85137245757
  • PubMed: 36062141

Funding Details

This work was supported by the UIN21517 School of Medicine, University of Monterrey.
FundersFunding numbers
UIN21517 School of Medicine, University of Monterrey
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