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Related Experiment Video

Updated: Apr 14, 2026

Malachite Green Assay for the Discovery of Heat-Shock Protein 90 Inhibitors

Malachite Green Assay for the Discovery of Heat-Shock Protein 90 Inhibitors

Published on: January 20, 2023

HSP90 inhibitors decrease AID levels and activity in mice and in human cells.

Damien Montamat-Sicotte¹, Ludivine C Litzler^1,2, Cecilia Abreu³

¹Institut de Recherches Cliniques de Montréal, Montréal, Canada.

European Journal of Immunology

|April 28, 2015

Summary

This summary is machine-generated.

Heat shock protein 90 (HSP90) inhibitors reduce levels of activation-induced deaminase (AID) in mice, impacting antibody production and leukemia. This suggests HSP90 inhibitors may offer new therapies targeting AID-related diseases.

Keywords:

Activation induced deaminase (AID)Antibody response Class switch recombination HSP90 inhibitors Leukemia

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Area of Science:

Immunology
Molecular Biology
Oncology

Background:

Activation-induced deaminase (AID) is crucial for antibody diversification but also implicated in autoimmune diseases and cancer.
Current therapeutic strategies are limited by the lack of specific inhibitors for AID.
The HSP90 chaperone pathway is known to stabilize AID in B cells.

Purpose of the Study:

To investigate whether HSP90 inhibitors can effectively target AID in vivo.
To explore the therapeutic potential of modulating AID function through HSP90 inhibition.

Main Methods:

Chronic administration of HSP90 inhibitors to immunized mice.
Assessment of AID protein levels, isotype switching, and disease severity in mouse models.
In vitro studies on human B cells and breast cancer cell lines to evaluate HSP90 inhibition effects on AID.

Main Results:

HSP90 inhibitors significantly decreased AID protein levels and isotype switching in immunized mice.
Reduced disease severity in a mouse model of B-cell lymphoblastic leukemia.
Human AID protein levels were sensitive to HSP90 inhibition in both normal and leukemic B cells, and epithelial-mesenchymal transition was prevented in vitro.

Conclusions:

HSP90 inhibitors serve as an indirect method to target AID in vivo.
Endogenous human AID demonstrates broad sensitivity to HSP90 inhibitors.
This approach holds promise for therapeutic applications in AID-related pathologies.