Acta Pharmaceutica Sinica B (Jun 2012)

Discovery and development of natural heat shock protein 90 inhibitors in cancer treatment

  • Yong Li,
  • Dongmei Zhang,
  • Jun Xu,
  • Junmin Shi,
  • Lei Jiang,
  • Nan Yao,
  • Wencai Ye

DOI
https://doi.org/10.1016/j.apsb.2012.03.009
Journal volume & issue
Vol. 2, no. 3
pp. 238 – 245

Abstract

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Heat shock protein 90 (Hsp90) is a highly conserved molecular chaperone that plays a vital role in the signal transduction of cancers. Hsp90 inhibitors are able to inhibit Hsp90 or the complex of Hsp90 and co-chaperones resulting in the degradation of Hsp90-dependent client proteins through the ubiquitination-proteasome pathway, thereby leading to the growth inhibition of tumor cells. This review will briefly discuss the molecular structure and biological function of Hsp90, and focus on a summary of recent progress in the development and testing of natural Hsp90 inhibitors and their different means by which they interact with Hsp90.

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