Related Experiment Video
Updated: Apr 29, 2026

Intracellular Refolding Assay
Published on: January 24, 2012
Regulation of apoptosis by heat shock proteins
Donna Kennedy1, Richard Jäger, Dick D Mosser
1Department of Biochemistry, Apoptosis Research Centre, Biosciences Research Building, Corrib Village, NUI Galway, Dangan, Galway, Ireland.
Abstract:
Thermotolerance, the acquired resistance of cells to stress, is a well-established phenomenon. Studies of the key mediators of this response, the heat shock proteins (HSPs), have led to the discovery of the important roles played by these proteins in the regulation of apoptotic cell death. Apoptosis is critical for normal tissue homeostasis and is involved in diverse processes including development and immune clearance. Apoptosis is tightly regulated by both proapoptotic and antiapoptotic factors, and dysregulation of apoptosis plays a significant role in the pathophysiology of many diseases. In the recent years, HSPs have been identified as key determinants of cell survival, which can modulate apoptosis by directly interacting with components of the apoptotic machinery. Therefore, manipulation of the HSPs could represent a viable strategy for the treatment of diseases. Here, we review the current knowledge with regard to the mechanisms of HSP-mediated regulation of apoptosis.
Related Concept Videos
Regulation of the Unfolded Protein Response
The Intrinsic Apoptotic Pathway
The Extrinsic Apoptotic Pathway
Apoptosis
Caspases
Cellular Injury V: Apoptosis and Autophagy

