, Volume 8, Issue 1, pp 61–70

On the role of Hsp27 in regulating apoptosis


DOI: 10.1023/A:1021601103096

Cite this article as:
Concannon, C.G., Gorman, A.M. & Samali, A. Apoptosis (2003) 8: 61. 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.


Copyright information

© Kluwer Academic Publishers 2003

Authors and Affiliations

  1. 1.Department of Biochemistry and National Centre for Biomedical Engineering ScienceNational University of IrelandGalwayIreland