The role of heat shock proteins in cancer

Cancer Lett. 2015 May 1;360(2):114-8. doi: 10.1016/j.canlet.2015.02.026. Epub 2015 Feb 23.

Abstract

Heat shock proteins (HSPs) are an evolutionary family of proteins that act as molecular chaperones. According to their size they have been classified into the following families; HSP90, HSP70, HSP60, HSP40 and HSP27. They prevent the formation of nonspecific protein aggregates and they assist proteins in the acquisition of their normal architecture. Moreover, HSPs are likely to have anti-apoptotic properties and are actively involved in various processes as tumor cell proliferation, invasion, metastases and death. Notably, these proteins have been reported to be significantly elevated in a plethora of human cancers. Their over-expression has been robustly associated with therapeutic resistance and poor survival. In this way, HSPs may have important therapeutic implications and they can be targeted by specific drugs. In this review, we discuss the influence of HSP27, HSP40, HSP60, HSP70 and HSP90 on human cancers. In addition, we report the existing scientific data on this issue with an effort to highlight the possible future implication of HSPs as tumor biomarkers or drug targets for improving prognosis and treatment of cancer patients around the world.

Keywords: HSP90; HSPs; Personalized cancer medicine; Targeted agents; Tumor biomarkers.

Publication types

  • Review

MeSH terms

  • Heat-Shock Proteins / metabolism*
  • Humans
  • Neoplasms / metabolism*

Substances

  • Heat-Shock Proteins