Heat shock proteins, cellular chaperones that modulate mitochondrial cell death pathways.
Stress or heat shock proteins (HSPs) are ubiquitous and highly conserved proteins whose expression is induced in response to a wide variety of physiological and environmental insults. They allow the cells to survive to otherwise lethal conditions. Various mechanisms have been proposed to account for the cytoprotective functions of HSPs. These proteins play an essential role in intracellular "house-keeping" by assisting the correct folding of nascent and stress-accumulated misfolded proteins and preventing their aggregation. Several HSPs have also demonstrated to directly interact with various components of the tightly regulated programmed cell death machinery, upstream, and downstream of the mitochondrial events. Finally, HSPs could play a role in the proteasome-mediated degradation of selected proteins under stress conditions. Altogether, these properties could make HSPs appropriate targets for modulating cell death pathways.
INSERM U-517, Faculty of Medicine and Pharmacy, 7 Boulevard Jeanne d'Arc, 21033 Dijon, France.
Arnaud
A
Parcellier
Sandeep
S
Gurbuxani
Elise
E
Schmitt
Eric
E
Solary
Carmen
C
Garrido
D000818:Animals; D017209:Apoptosis; D020169:Caspases / Q000502:physiology; D016923:Cell Death; D006360:Heat-Shock Proteins / Q000502:physiology*; D008928:Mitochondria / Q000378:metabolism*; D008954:Models, Biological; D018832:Molecular Chaperones / Q000502:physiology*; D015398:Signal Transduction
D006360:Heat-Shock Proteins; D018832:Molecular Chaperones; D020169:Caspases