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High-throughput Measurement of Plasma Membrane Resealing Efficiency in Mammalian Cells
Published on: January 7, 2019
Tau oligomers impair artificial membrane integrity and cellular viability
Katharina Flach1, Isabel Hilbrich, Andrea Schiffmann
1Department of Molecular and Cellular Mechanisms of Neurodegeneration, Paul Flechsig Institute of Brain Research, Faculty of Medicine, Jahnallee 59, University of Leipzig, 04109 Leipzig, Germany.
The Journal of Biological Chemistry
|November 7, 2012
Summary
Oligomeric Tau aggregation intermediates are the most toxic forms of Tau protein, decreasing cell viability and increasing vesicle leakage. This suggests a common toxicity mechanism for amyloidogenic proteins like Tau.
Area of Science:
- Neuroscience
- Biochemistry
- Cell Biology
Background:
- Microtubule-associated protein Tau stabilizes microtubules in neurons.
- In tauopathies, Tau detaches from microtubules and aggregates into toxic filaments.
- Oligomeric intermediates are implicated as cytotoxic species in other amyloidogenic proteins.
Purpose of the Study:
- To investigate if oligomeric Tau aggregation intermediates are the primary cytotoxic species in Tau fibrillogenesis.
- To assess the toxicity of Tau monomers, intermediates, and fibrils on cell viability and membrane integrity.
Main Methods:
- Assessed cell viability and membrane integrity of SH-SY5Y neuroblastoma cells.
- Tested artificial phospholipid vesicles for membrane permeability.
- Treated cells and vesicles with Tau monomers, aggregation intermediates, and fibrils.
Main Results:
- Oligomeric Tau aggregation intermediates significantly decreased cell viability.
- Oligomeric Tau intermediates increased leakage in artificial phospholipid vesicles.
- Tau fibrils and monomers showed less toxicity compared to oligomeric intermediates.
Conclusions:
- Oligomeric Tau aggregation intermediates are the most toxic species in Tau fibrillogenesis.
- Tau protein shares a common toxicity-mediating mechanism with other amyloidogenic proteins.
- These findings support the hypothesis of a unified mechanism of toxicity for amyloidogenic proteins.
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