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Hsp90: a novel target for the disruption of multiple signaling cascades

Stephanie C Bishop1, Joseph A Burlison, Brian S J Blagg

  • 1Department of Molecular Biosciences, The University of Kansas, Lawrence, Kansas 66045-7563, USA.

Current Cancer Drug Targets
|November 6, 2007
PubMed

Insights

Heat shock protein 90 (Hsp90) is a key target for novel anti-cancer drugs. Inhibiting Hsp90 disrupts multiple cancer pathways, blocking tumor growth and proliferation.

Area of Science:

  • Oncology
  • Molecular Biology
  • Drug Discovery

Background:

  • Heat shock protein 90 (Hsp90) is a molecular chaperone.
  • Hsp90 is crucial for the stability and function of numerous oncogenic proteins.
  • Its role spans all six hallmarks of cancer, making it a promising therapeutic target.

Purpose of the Study:

  • To review the literature on Hsp90's role in cancer.
  • To summarize recent advances in developing Hsp90 inhibitors.
  • To highlight Hsp90 as a target for novel anti-cancer agents.

Main Methods:

  • Literature review of recent scientific publications.
  • Analysis of structure-based drug design approaches for Hsp90 inhibitors.
  • Summary of compounds currently in clinical development.

Main Results:

  • Hsp90 facilitates proteins involved in all six hallmarks of cancer.
  • Inhibition of Hsp90 disrupts multiple oncogenic signaling pathways simultaneously.
  • Structure-based drug design has yielded novel Hsp90 inhibitors.

Conclusions:

  • Hsp90 is a validated and important target for anti-cancer drug development.
  • Targeting Hsp90 offers a strategy for simultaneously disrupting multiple cancer mechanisms.
  • Several novel Hsp90 inhibitors are advancing through clinical trials.

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