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An In Vitro Model for Studying Tau Aggregation Using Lentiviral-mediated Transduction of Human Neurons
Published on: May 23, 2019
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Propagation of Tau aggregates
Michel Goedert1, Maria Grazia Spillantini2
1MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge, CB2 0QH, UK. mg@mrc-lmb.cam.ac.uk.
Molecular Brain
|June 1, 2017
Summary
Tau aggregates spread like prions in the brain, initiating neurodegeneration. Research shows these protein clumps release from cells and seed new aggregates in distant regions, contributing to disease progression.
Area of Science:
- Neuroscience
- Cell Biology
- Protein Biochemistry
Background:
- Accumulating evidence since 2009 suggests Tau aggregates initiate neurodegeneration.
- Tau aggregate propagation is often described as prion-like, involving self-amplifying cascades.
Purpose of the Study:
- To investigate the prion-like propagation of Tau aggregates in the brain.
- To understand the mechanisms of Tau seeding and spreading.
Main Methods:
- Intracerebral injection of Tau inclusions in mouse models.
- Analysis of Tau aggregate formation, release, and uptake between cells.
- Characterization of Tau fibril morphology.
Main Results:
- Tau aggregate injection induced ordered assembly of monomeric Tau.
- Aggregates spread to distant brain regions.
- Short fibrils were identified as the primary species of seed-competent Tau.
Conclusions:
- Tau aggregates exhibit prion-like propagation characteristics, including cell-to-cell spreading.
- Distinct Tau conformers (strains) may exist, potentially explaining different tauopathies.
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