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In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein

In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein

Published on: January 2, 2015

Abundant tau filaments and nonapoptotic neurodegeneration in transgenic mice expressing human P301S tau protein.

Bridget Allen¹, Esther Ingram, Masaki Takao

¹Medical Research Council Laboratory of Molecular Biology, Cambridge CB2 2QH, United Kingdom.

The Journal of Neuroscience : the Official Journal of the Society for Neuroscience

|November 6, 2002

Summary

Transgenic mice expressing a mutated human Tau gene developed neurological deficits and neurodegeneration. These mice exhibit hyperphosphorylated Tau protein, forming filaments similar to those in human tauopathies.

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Area of Science:

Neuroscience
Genetics
Pathology

Background:

Mutations in the Tau gene are linked to frontotemporal dementia and parkinsonism (FTDP-17).
Transgenic animal models allow studying pathogenic human Tau mutations in vivo.

Purpose of the Study:

To characterize a mouse model expressing the P301S mutation in the human Tau gene.
To investigate the resulting neurological phenotype and pathological changes.

Main Methods:

Generation and characterization of transgenic mice expressing human Tau with the P301S mutation.
Light and electron microscopy to examine neuronal pathology and Tau aggregation.
Biochemical analysis of hyperphosphorylated Tau in brain and spinal cord.

Main Results:

Homozygous mice developed paraparesis by 5-6 months.
Accumulation of hyperphosphorylated Tau and filament formation (resembling FTDP-17 and Alzheimer's disease pathologies).
Significant motor neuron loss in the spinal cord.

Conclusions:

The P301S Tau mutation in transgenic mice recapitulates key pathological features of human tauopathies.
This model provides insights into Tau hyperphosphorylation and neurodegeneration mechanisms.