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In Vitro Characterization of Histone Chaperones using Analytical, Pull-Down and Chaperoning Assays
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Chaperone substrate provides missing link for cancer drug discovery.
Katherine M Byrd1, Brian S J Blagg1
1From the Department of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana 46545.
The Journal of Biological Chemistry
|February 18, 2018
Summary
Researchers identified two inhibitors of apoptosis proteins (IAPs) as specific targets of heat shock protein 70 (Hsp70). This discovery provides crucial biomarkers for monitoring Hsp70 inhibition in cancer drug development.
Area of Science:
- Molecular biology
- Cancer research
- Biochemistry
Background:
- Heat shock proteins (Hsp70 and Hsp90) are overexpressed in various cancers.
- These chaperones are recognized as significant targets for cancer chemotherapeutics.
- A lack of specific biomarkers for Hsp70 inhibition has hindered the development of targeted therapies.
Purpose of the Study:
- To identify specific client substrates of Hsp70.
- To establish reliable biomolecular readouts for monitoring Hsp70 activity.
- To facilitate the development of novel Hsp70-specific inhibitors for cancer treatment.
Main Methods:
- The study focused on identifying specific protein interactions with Hsp70.
- Investigated the role of inhibitors of apoptosis proteins (IAPs) in relation to Hsp70.
- Utilized biochemical assays to validate Hsp70 client substrates.
Main Results:
- Two specific inhibitors of apoptosis proteins (IAPs) were identified as direct client substrates of Hsp70.
- This finding establishes IAPs as potential biomarkers for Hsp70 activity.
- The results provide a foundation for developing assays to assess Hsp70 inhibition.
Conclusions:
- The identification of IAPs as Hsp70 client substrates offers a novel approach to monitor Hsp70 inhibition.
- These findings pave the way for the development of targeted cancer therapies focused on Hsp70.
- The study contributes to a better understanding of chaperone networks in cancer biology.
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