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Updated: Jun 10, 2026

Ex Vivo Treatment Response of Primary Tumors and/or Associated Metastases for Preclinical and Clinical Development of Therapeutics
Published on: October 2, 2014
Targeting the dynamic HSP90 complex in cancer
Jane Trepel1, Mehdi Mollapour, Giuseppe Giaccone
1Medical Oncology Branch Center for Cancer Research, National Cancer Institute, Building 10, room 1-5940, 9000 Rockville Pike, Bethesda, MD 20892, USA.
Abstract:
The molecular chaperone heat shock protein 90 (HSP90) has been used by cancer cells to facilitate the function of numerous oncoproteins, and it can be argued that cancer cells are 'addicted' to HSP90. However, although recent reports of the early clinical efficacy of HSP90 inhibitors are encouraging, the optimal use of HSP90-targeted therapeutics will depend on understanding the complexity of HSP90 regulation and the degree to which HSP90 participates in both neoplastic and normal cellular physiology.
Insights
Cancer cells rely on heat shock protein 90 (HSP90) to support oncoprotein function. Understanding HSP90
Area of Science:
- Molecular biology
- Oncology
- Biochemistry
Background:
- Heat shock protein 90 (HSP90) is a molecular chaperone crucial for cancer cell survival.
- Cancer cells exhibit a dependency, or 'addiction,' to HSP90 for the function of numerous oncoproteins.
Purpose of the Study:
- To explore the complex role of HSP90 in cancer.
- To investigate the implications of HSP90 regulation for targeted cancer therapeutics.
Main Methods:
- Analysis of HSP90's role in neoplastic cellular physiology.
- Evaluation of HSP90's involvement in normal cellular functions.
Main Results:
- HSP90 facilitates the function of multiple oncoproteins in cancer cells.
- HSP90 plays a role in both cancer and normal cellular physiology.
Conclusions:
- Optimal use of HSP90 inhibitors requires a deep understanding of HSP90's complex regulatory network.
- Further research into HSP90's dual role is essential for developing effective HSP90-targeted cancer therapies.
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