On the role of Hsp27 in regulating apoptosis

Apoptosis. 2003 Jan;8(1):61-70. doi: 10.1023/a:1021601103096.


Heat shock proteins (Hsps) comprise several different families of proteins that are induced in response to a wide variety of physiological and environmental insults. One such protein which is highly induced during the stress response is a 27-kDa protein, termed Hsp27 whose expression is seen to correlate with increased survival in response to cytotoxic stimuli. It has been shown to prevent cell death by a wide variety of agents that cause apoptosis. Hsp27 is a molecular chaperone with an ability to interact with a large number of proteins. Recent evidence has shown that Hsp27 regulates apoptosis through an ability to interact with key components of the apoptotic signalling pathway, in particular, those involved in caspase activation and apoptosis. This article will review recent advances in the field and will address some of the potential mechanisms by which Hsp27 functions as an anti-apoptotic molecule.

Publication types

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

MeSH terms

  • Animals
  • Apoptosis*
  • Caspase Inhibitors
  • Caspases / metabolism
  • Cytoskeleton / metabolism
  • Enzyme Activation
  • HSP27 Heat-Shock Proteins
  • Heat-Shock Proteins*
  • Humans
  • Models, Biological
  • Molecular Chaperones / metabolism
  • Neoplasm Proteins / physiology*
  • Neoplasms / metabolism
  • Neoplasms / pathology*
  • Oxidation-Reduction
  • Protein Binding
  • Reactive Oxygen Species
  • Signal Transduction


  • Caspase Inhibitors
  • HSP27 Heat-Shock Proteins
  • HSPB1 protein, human
  • Heat-Shock Proteins
  • Molecular Chaperones
  • Neoplasm Proteins
  • Reactive Oxygen Species
  • Caspases