Heat shock proteins in multiple myeloma

Oncotarget. 2014 Mar 15;5(5):1132-48. doi: 10.18632/oncotarget.1584.

Abstract

Heat shock proteins are molecular chaperones with a central role in protein folding and cellular protein homeostasis. They also play major roles in the development of cancer and in recent years have emerged as promising therapeutic targets. In this review, we discuss the known molecular mechanisms of various heat shock protein families and their involvement in cancer and in particular, multiple myeloma. In addition, we address the current progress and challenges in pharmacologically targeting these proteins as anti-cancer therapeutic strategies.

Publication types

  • Review

MeSH terms

  • Chaperonin 10 / metabolism
  • Chaperonin 60 / metabolism
  • DNA-Binding Proteins / antagonists & inhibitors
  • HSP27 Heat-Shock Proteins / metabolism
  • HSP70 Heat-Shock Proteins / antagonists & inhibitors
  • HSP70 Heat-Shock Proteins / metabolism
  • HSP90 Heat-Shock Proteins / antagonists & inhibitors
  • HSP90 Heat-Shock Proteins / metabolism
  • Heat Shock Transcription Factors
  • Heat-Shock Proteins / antagonists & inhibitors
  • Heat-Shock Proteins / metabolism
  • Heat-Shock Proteins / physiology*
  • Humans
  • Multiple Myeloma / drug therapy*
  • Multiple Myeloma / metabolism
  • Protein Folding
  • Signal Transduction
  • Transcription Factors / antagonists & inhibitors

Substances

  • Chaperonin 10
  • Chaperonin 60
  • DNA-Binding Proteins
  • HSP27 Heat-Shock Proteins
  • HSP70 Heat-Shock Proteins
  • HSP90 Heat-Shock Proteins
  • Heat Shock Transcription Factors
  • Heat-Shock Proteins
  • Transcription Factors