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Propagation of Tau via Extracellular Vesicles
Open accessAbstract
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.
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“It has been proposed that intracellular tau can be released from neurons by exocytosis, including secretion (free protein), extracellular vesicles (such as exosomes and ectosomes/microvesicles), and neuronal death pathways [67].”
From Tau and neuroinflammation in Alzheimer’s disease: interplay mechanisms and clinical translation (2023) · cites this paper as [67]
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“Meanwhile, the extracellular tau can be taken up by neighboring cells, both neurons and glial cells, through various pathways, including phagocytosis [68], macropinocytosis [69], receptor-mediated uptake [67, 70], endocytosis [71], and/or membrane fusion of exosomes [72, 73].”
From Tau and neuroinflammation in Alzheimer’s disease: interplay mechanisms and clinical translation (2023) · cites this paper as [67]
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Metadata
- Authors
- Pérez, M., Avila, J., & Hernández, F.
- Affiliations
- Universidad Autónoma de Madrid (ES)
- Consejo Superior de Investigaciones Científicas (ES)
- Corresponding author
- Hernández, Félix
- Venue
- Frontiers in Neuroscience
- Publisher
- Frontiers Media SA
- Published
- 2019-07-02
- Volume
- 13
- Pages
- 698-698
- ISSN
- 1662-453X (ISSN-L)
- PMC
- PMC6614378
- OpenAlex
- W2954942173
- Cited by
- 118
- References
- 83
- Citations by year
- 2026: 14 · 2025: 14 · 2024: 17 · 2023: 18 · 2022: 11 · 2021: 24 · 2020: 18 · 2019: 2
- FWCI
- 1.62
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Frontiers in Neuroscience (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Biblos-e Archivo (Universidad Autónoma de Madrid) (submittedVersion, cc-by)
- DIGITAL.CSIC (Spanish National Research Council (CSIC)) (submittedVersion, cc-by)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Hispana (submittedVersion)
- Funders
- Comunidad de Madrid (S2017/BMD-3700, S2017/BMD)
- Ministerio de Ciencia, Innovación y Universidades
- Centro de Investigación Biomédica en Red sobre Enfermedades Neurodegenerativas (S2017/BMD-3700)
- Instituto de Salud Carlos III (S2017/BMD-3700)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Extracellular vesicles in disease
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- tau protein, extracellular vesicles, exosomes, Alzheimer's disease, tauopathy, protein aggregation, microglia, neurofibrillary tangles, amyloid-beta, hyperphosphorylated tau, Parkinson's disease, prion disease
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