Prion-like Properties of Tau Protein: The Importance of Extracellular Tau as a Therapeutic Target
Open accessAbstract
Work over the past 4 years indicates that multiple proteins associated with neurodegenerative diseases, especially Tau and α-synuclein, can propagate aggregates between cells in a prion-like manner. This means that once an aggregate is formed it can escape the cell of origin, contact a connected cell, enter the cell, and induce further aggregation via templated conformational change. The prion model predicts a key role for extracellular protein aggregates in mediating progression of disease. This suggests new therapeutic approaches based on blocking neuronal uptake of protein aggregates and promoting their clearance. This will likely include therapeutic antibodies or small molecules, both of which can be developed and optimized in vitro prior to preclinical studies.
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HSPGs are essential players in the cellular uptake of Tau.
“Intriguingly, over the past decade, HSPGs have been revealed as essential players in the cellular uptake of Tau46–48.”
From The APOE-R136S mutation protects against APOE4-driven tau pathology, neurodegeneration, and neuroinflammation (2023) · cites this paper as [48]
The “Understanding Cell Uptake” section says that HSPGs initiate uptake of Tau aggregate seeds through macropinocytosis, and “Targeting Aggregate Binding to the Cell Surface” says Tau aggregates enter cells via HSPGs. The claim omits the aggregate qualifier: the paper says Tau monomers bind HSPGs but do not trigger uptake through this mechanism. (LLM, conf=0.85)
Experimental — accuracy not yet measuredHSPGs are largely responsible for neuronal Tau uptake.
“Previous work showed that HSPGs are largely responsible for neuronal Tau uptake46–48,57.”
From The APOE-R136S mutation protects against APOE4-driven tau pathology, neurodegeneration, and neuroinflammation (2023) · cites this paper as [48]
In “Understanding Cell Uptake” (page not available), the paper says HSPG binding initiates uptake of aggregated Tau seeds into neurons. It specifies that Tau monomers do not trigger uptake through this mechanism, and it does not establish that HSPGs account for most neuronal Tau uptake overall. The claim omits that limitation and overstates the pathway's share of uptake. (LLM, conf=0.86)
Experimental — accuracy not yet measured
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- Authors
- Holmes, B. B., & Diamond, M. I.
- Affiliations
- Washington University in St. Louis (US)
- Corresponding author
- Diamond, Marc I.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2014-07
- Volume
- 289
- Issue
- 29
- Pages
- 19855-19861
- ISSN
- 0021-9258 (ISSN-L)
- PMC
- PMC4106306
- OpenAlex
- W2068440450
- Cited by
- 202
- References
- 101
- Citations by year
- 2026: 8 · 2025: 9 · 2024: 10 · 2023: 14 · 2022: 13 · 2021: 10 · 2020: 28 · 2019: 22 · 2018: 27 · 2017: 15 · 2016: 18 · 2015: 17 · 2014: 10 · 2013: 1
- FWCI
- 2.34
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (1R01NS071835-01, 5 F31 NS079039-03)
- 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 › Neurology › Parkinson's Disease Mechanisms and Treatments
- Keywords
- tau protein, prion-like propagation, alpha-synuclein, neurodegenerative diseases, therapeutic antibodies, small molecule drugs, aggregate clearance
- MeSH terms
- Alzheimer Disease, Animals, Cell Membrane, Humans, Prions, Protein Conformation, Vaccines, Amyloid beta-Peptides, tau Proteins, Heparan Sulfate Proteoglycans, Protein Transport, Tauopathies, alpha-Synuclein, Protein Multimerization
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