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Related Experiment Video

Updated: May 25, 2026

In Vitro Assay for Studying the Aggregation of Tau Protein and Drug Screening

In Vitro Assay for Studying the Aggregation of Tau Protein and Drug Screening

Published on: November 20, 2018

Hsp70 alters tau function and aggregation in an isoform specific manner.

Kellen Voss¹, Benjamin Combs, Kristina R Patterson

¹Department of Molecular Biosciences, University of Kansas, Lawrence, Kansas 66045, United States.

|January 13, 2012

Summary

Heat shock protein 70 (Hsp70) directly inhibits abnormal tau protein aggregation, particularly the three-repeat isoforms, without disrupting normal microtubule function. This suggests Hsp70 as a potential therapeutic target for tauopathies.

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Last Updated: May 25, 2026

In Vitro Assay for Studying the Aggregation of Tau Protein and Drug Screening

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Purification of Hsp104, a Protein Disaggregase

Purification of Hsp104, a Protein Disaggregase

Published on: September 30, 2011

Area of Science:

Neuroscience
Molecular Biology
Biochemistry

Background:

Tauopathies are neurodegenerative diseases characterized by the abnormal aggregation of tau protein.
Tau aggregation involves conformational changes exposing hydrophobic regions, leading to oligomer and filament formation.
Molecular chaperones, like heat shock protein 70 (Hsp70), typically prevent protein misfolding and aggregation.

Purpose of the Study:

To investigate the differential effects of Hsp70 on the aggregation and microtubule assembly of various tau protein isoforms.
To determine if Hsp70 directly inhibits tau aggregation or acts indirectly.
To assess the impact of Hsp70 on normal tau function in microtubule formation.

Main Methods:

In vitro assays were used to study the aggregation of individual tau isoforms in the presence and absence of Hsp70.
Microtubule assembly was measured to assess the impact of Hsp70 on normal tau function.
Direct inhibition of tau aggregation by Hsp70 was evaluated.

Main Results:

Hsp70 directly inhibits the aggregation of all six tau isoforms.
Hsp70 was more effective in inhibiting the aggregation of the three-repeat tau isoforms.
Hsp70 did not impede the ability of tau isoforms to promote microtubule formation.

Conclusions:

Hsp70 effectively targets dysfunctional tau protein aggregation without interfering with normal tau function.
Targeting Hsp70 may offer a therapeutic strategy for tauopathies, such as Alzheimer's disease, by mitigating pathological tau accumulation.
The differential effect of Hsp70 on tau isoforms warrants further investigation for targeted therapeutic development.