Preparation and Characterization of Neurotoxic Tau Oligomers
Abstract
Tau aggregation is a pathological hallmark of Alzheimer's disease, Parkinson's disease, and many other neurodegenerative disorders known as tauopathies. Tau aggregates take on many forms, and their formation is a multistage process with intermediate stages. Recently, tau oligomers have emerged as the pathogenic species in tauopathies and a possible mediator of amyloid-β toxicity in Alzheimer's disease. Here, we use a novel, physiologically relevant method (oligomer cross-seeding) to prepare homogeneous populations of tau oligomers and characterize these oligomers in vitro. We show that both Aβ and α-synuclein oligomers induce tau aggregation and the formation of β-sheet-rich neurotoxic tau oligomers.
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Tau oligomers form prior to and independent of NFTs.
“Several groups have demonstrated that tau oligomers, which form prior to and independent of NFTs, are the toxic agents responsible for synaptic dysfunction in AD and drive cognitive decline [26, 49, 50, 58, 95].”
From Enhanced microglial dynamics and a paucity of tau seeding in the amyloid plaque microenvironment contribute to cognitive resilience in Alzheimer’s disease (2024) · cites this paper as [49]
Tau oligomers are the toxic agents responsible for synaptic dysfunction in AD and drive cognitive decline.
“Several groups have demonstrated that tau oligomers, which form prior to and independent of NFTs, are the toxic agents responsible for synaptic dysfunction in AD and drive cognitive decline [26, 49, 50, 58, 95].”
From Enhanced microglial dynamics and a paucity of tau seeding in the amyloid plaque microenvironment contribute to cognitive resilience in Alzheimer’s disease (2024) · cites this paper as [49]
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“Several groups have demonstrated that tau oligomers, which form prior to and independent of NFTs, are the toxic agents responsible for synaptic dysfunction in AD and drive cognitive decline [26, 49, 50, 58, 95].”
BackgroundSelf-citationContinuous Monitoring of Tau-Induced Neurotoxicity in Patient-Derived iPSC-Neurons
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- Authors
- Lasagna-Reeves, C. A., Castillo-Carranza, D. L., Guerrero-Muñoz, M. J., Jackson, G. R., & Kayed, R.
- Affiliations
- The George P. and Cynthia Woods Mitchell Center for Neurodegenerative Diseases, Department of Neurology and Department of Neuroscience and Cell Biology, University of Texas Medical Branch, Galveston, Texas 77555-1045, United States
- The University of Texas Medical Branch at Galveston (US)
- Corresponding author
- Kayed, Rakez
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 2010-11-08
- Volume
- 49
- Issue
- 47
- Pages
- 10039-10041
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W2035216963
- Cited by
- 359
- References
- 11
- Citations by year
- 2026: 14 · 2025: 12 · 2024: 22 · 2023: 18 · 2022: 25 · 2021: 26 · 2020: 42 · 2019: 24 · 2018: 21 · 2017: 24 · 2016: 21 · 2015: 23 · 2014: 25 · 2013: 24 · 2012: 22
- FWCI
- 13.21
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biochemistry (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Prion Diseases and Protein Misfolding
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Keywords
- tau oligomers, tau aggregation, tauopathy, Alzheimer's disease, Parkinson's disease, amyloid-beta, alpha-synuclein, neurotoxicity
- MeSH terms
- Humans, Amyloid beta-Peptides, tau Proteins, Protein Structure, Secondary, Neurodegenerative Diseases, Cell Line, Tumor, alpha-Synuclein, Protein Multimerization
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