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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

Structurally and Morphologically Distinct Pathological Tau Assemblies Differentially Affect GVB Accumulation.

Marta Jorge-Oliva¹, Jan R T van Weering^1,2, Wiep Scheper^1,2

¹Department of Functional Genomics, Center for Neurogenomics and Cognitive Research, Vrije Universiteit Amsterdam, Amsterdam Neuroscience-Neurodegeneration, 1081 HV Amsterdam, The Netherlands.

International Journal of Molecular Sciences

|July 14, 2023

Summary

This summary is machine-generated.

Pathological tau aggregates in neurons trigger granulovacuolar degeneration bodies (GVBs). Untagged tau filaments, shorter and randomly distributed, significantly increase GVB accumulation, suggesting aggregate structure influences neurodegeneration.

Keywords:

Tau aggregation granulovacuolar degeneration bodies neurodegenerative disease

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Modulation of Tau Subcellular Localization as a Tool to Investigate the Expression of Disease-related Genes

Modulation of Tau Subcellular Localization as a Tool to Investigate the Expression of Disease-related Genes

Published on: December 20, 2019

Area of Science:

Neuroscience
Cell Biology
Pathology

Background:

Tau aggregation is a key factor in tauopathies, a group of neurodegenerative diseases.
The precise neuronal response to tau pathology and its link to neurodegeneration remain unclear.
Granulovacuolar degeneration bodies (GVBs) are neuron-specific structures that respond to tau pathology.

Purpose of the Study:

To investigate how pathological tau assemblies influence GVB accumulation in neurons.
To determine the role of tau aggregate properties, such as structure and localization, in GVB formation.

Main Methods:

Utilized primary neuron models with different tau aggregation properties.
Employed confocal microscopy, transmission electron microscopy, and automated high-content microscopy for quantitative analysis.
Compared GVB load in neurons expressing GFP-tagged versus untagged tau variants.

Main Results:

Pathological tau assemblies exhibited distinct subcellular localization, morphology, and ultrastructure based on GFP tagging.
Increased GVB accumulation was observed in the untagged tau aggregation model.
Untagged tau aggregates were characterized by shorter, randomly distributed filaments within the neuronal soma.

Conclusions:

Tau aggregate structure and/or subcellular localization are critical determinants of GVB accumulation.
Understanding these factors may provide insights into the mechanisms of neurodegeneration in tauopathies.