Clinical and Translational Oncology

, Volume 12, Issue 3, pp 166–173

Heat shock proteins as targets in oncology

  • Alejandra Giménez Ortiz
  • Joaquín Montalar Salcedo
Educational Series Molecular Targets in Oncology

DOI: 10.1007/s12094-010-0486-8

Cite this article as:
Giménez Ortiz, A. & Montalar Salcedo, J. Clin Transl Oncol (2010) 12: 166. doi:10.1007/s12094-010-0486-8


Heat shock proteins are ubiquitous molecular chaperones involved in posttranslational folding, stability, activation and maturation of many proteins that are essential mediators of signal transduction and cell cycle progression. Hsp90 proteins are the best studied proteins of this family. A growing number of Hsp90 client proteins have been shown to be important for the development, proliferation and survival of several types of cancer. Inhibition of Hsp90 leads to the degradation of known oncogene products, such as Her2, BRAF and others, leading to the simultaneous blockade of multiple oncogenic transduction pathways. Hsp90 inhibitors, derived from the natural compound geldanamycin, are attractive targets for anticancer drug development. We will review the clinical data on Hsp90 inhibitors in different malignancies. The best known of them, 17-AAG, has shown significant antitumour activity against a broad variety of cancers in preclinical studies, including breast, myeloma, melanoma, prostate and lung cancers. Hsp90 inhibitors can be used as single agents or in combination with other targeted treatments or chemotherapy and radiotherapy. The results of clinical phase II and III trials evaluating the efficacy of these drugs in different types of tumours are awaited.


HSP Hsp90 inhibitors Chaperones Cancer 17-AAG 

Copyright information

© Feseo 2010

Authors and Affiliations

  • Alejandra Giménez Ortiz
    • 1
  • Joaquín Montalar Salcedo
    • 2
  1. 1.Servicio de Oncología MédicaHospital Universitario La FeValenciaSpain
  2. 2.Jefe de Servicio Oncología MédicaHospital Universitario La FeValenciaSpain

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