Heat shock proteins as emerging therapeutic targets

Br J Pharmacol. 2005 Nov;146(6):769-80. doi: 10.1038/sj.bjp.0706396.


Chaperones (stress proteins) are essential proteins to help the formation and maintenance of the proper conformation of other proteins and to promote cell survival after a large variety of environmental stresses. Therefore, normal chaperone function is a key factor for endogenous stress adaptation of several tissues. However, altered chaperone function has been associated with the development of several diseases; therefore, modulators of chaperone activities became a new and emerging field of drug development. Inhibition of the 90 kDa heat shock protein (Hsp)90 recently emerged as a very promising tool to combat various forms of cancer. On the other hand, the induction of the 70 kDa Hsp70 has been proved to be an efficient help in the recovery from a large number of diseases, such as, for example, ischemic heart disease, diabetes and neurodegeneration. Development of membrane-interacting drugs to modify specific membrane domains, thereby modulating heat shock response, may be of considerable therapeutic benefit as well. In this review, we give an overview of the therapeutic approaches and list some of the key questions of drug development in this novel and promising therapeutic approach.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • HSP90 Heat-Shock Proteins / antagonists & inhibitors
  • HSP90 Heat-Shock Proteins / metabolism
  • Heat-Shock Proteins / antagonists & inhibitors*
  • Heat-Shock Proteins / metabolism
  • Humans
  • Models, Biological
  • Neoplasms / drug therapy*
  • Neoplasms / metabolism


  • HSP90 Heat-Shock Proteins
  • Heat-Shock Proteins