Cited by 213Extracellular vesicles in diseasePrion Diseases and Protein MisfoldingAlzheimer's disease research and treatments

The role of extracellular vesicles in neurodegenerative diseases

Quek, Camelia, Hill, Andrew F.·2017·Biochemical and Biophysical Research Communications

Abstract

Extracellular vesicles, including exosomes, are small membranous vesicles released from many biotypes, contributing to the disease progression and spreading. These extracellular vesicles provide an important mode of cell-to-cell communication by delivering proteins, lipids and RNA to target cells. Exosomes are found associated with neurodegenerative diseases, which are characterised by progressive degeneration of neurons and often associated with misfolded protein. The common diseases include Parkinson's disease (PD), Alzheimer's diseases (AD), amyotrophic lateral sclerosis (ALS), and the prion diseases. Of all neurodegenerative diseases, prion diseases are classified as the distinctive group owing to its transmissible and infectious nature of misfolded prion protein. The infectious prion particles have been demonstrated to be present in exosomes to spread prion infectivity within cells. Similarly, misfolded proteins involved in other neurodegenerative diseases such as Amyloid-β and tau in AD, α-synuclein in PD, and superoxide dismutase 1 in ALS have been demonstrated to exploit exosomes for induced spreading of misfolded proteins in a prion-like mechanism. Furthermore, RNA molecules can be taken up by the recipient cells as cargo in exosomes. These RNAs can module the expression of the target genes by repressing or inhibiting protein translation. Here we review the role of exosomes in prion diseases and other common neurodegenerative diseases, and discuss the potential of these vesicles for disease pathogenesis.

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Crossref · 10.1016/j.bbrc.2016.09.090

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  • Recent research has highlighted the significant role of sEVs in the propagation of misfolded proteins in neurodegenerative diseases, suggesting they may facilitate intercellular transfer and contribute to the progression and severity of these conditions.

    “Recent research has highlighted the significant role of sEVs in the propagation of these misfolded proteins, suggesting they may facilitate intercellular transfer and contribute to the progression and severity of these conditions [130–132].”

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Authors
Quek, C., & Hill, A. F.
Affiliations
The University of Melbourne (AU)
Corresponding author
Hill, Andrew F.
Venue
Biochemical and Biophysical Research Communications
Publisher
Elsevier BV
Published
2017-02
Volume
483
Issue
4
Pages
1178-1186
ISSN
0006-291X (ISSN-L)
OpenAlex
W2521063020
Cited by
213
References
13
Citations by year
2026: 17 · 2025: 18 · 2024: 26 · 2023: 14 · 2022: 17 · 2021: 26 · 2020: 26 · 2019: 31 · 2018: 23 · 2017: 13 · 2016: 1
FWCI
2.05
Type
journal article
Language
en
Open access
closed
Locations
  • Biochemical and Biophysical Research Communications (publishedVersion)
  • PubMed (publishedVersion)
  • Victoria University Research Repository (Victoria University) (submittedVersion)
Funders
  • Australian Research Council (FT100100560)
  • National Health and Medical Research Council (628946)
  • University of Melbourne International Research Scholarship
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Extracellular vesicles in disease
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Prion Diseases and Protein Misfolding
  • Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
Keywords
extracellular vesicles, exosomes, neurodegenerative diseases, prion disease, prion protein, protein misfolding, prion-like spreading, Parkinson's disease, Alzheimer's disease, amyotrophic lateral sclerosis, amyloid-beta, tau protein, alpha-synuclein, superoxide dismutase 1, RNA transfer, cell-to-cell communication, pathogenesis
MeSH terms
Extracellular Vesicles, Animals, Humans, Prion Diseases, Neurodegenerative Diseases

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