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Updated: Jul 3, 2026
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In Vitro Assay for Studying the Aggregation of Tau Protein and Drug Screening
Published on: November 20, 2018
Assessing the toxicity of tau aggregation
Carolyn A Rankin1, T Chris Gamblin
1Department of Molecular Biosciences, University of Kansas, Lawrence, KS 66045, USA.
Journal of Alzheimer'S Disease : JAD
|August 9, 2008
Summary
Tau aggregation is toxic in neurodegenerative diseases like Alzheimer's. However, the exact toxic form of aggregated tau protein remains unclear, despite various model systems and assays.
Area of Science:
- Neuroscience
- Biochemistry
- Pathology
Background:
- Abnormally phosphorylated and aggregated tau protein forms pathological structures central to neurodegeneration in tauopathies.
- These structures are hypothesized to be toxic mediators driving disease progression in conditions like Alzheimer's disease.
Purpose of the Study:
- To review and compare recent model systems and assay methods used to investigate tau pathology and toxicity.
- To clarify the role of tau aggregation in neurodegeneration.
Main Methods:
- Comparative analysis of diverse animal models for tauopathy.
- Examination of various assay methodologies for assessing tau aggregation and toxicity.
- Evaluation of the impact of tau expression levels and aggregation-enhancing modifications.
Main Results:
- Evidence from animal models presents conflicting roles for tau aggregation (pathogenic, beneficial, or incidental).
- Expression levels of tau and specific modifications significantly influence experimental outcomes.
- Tau aggregation is demonstrably toxic, but the specific toxic species is not definitively identified.
Conclusions:
- Tau aggregation plays a toxic role in neurodegenerative tauopathies.
- Further research is needed to pinpoint the precise toxic species of aggregated tau protein.
