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Heat shock proteins, cellular chaperones that modulate mitochondrial cell death pathways
- Source :
- Biochemical and Biophysical Research Communications. 304:505-512
- Publication Year :
- 2003
- Publisher :
- Elsevier BV, 2003.
-
Abstract
- 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.
- Subjects :
- Programmed cell death
Cell Death
Biophysics
Apoptosis
hemic and immune systems
Cell Biology
Mitochondrion
Biology
Models, Biological
Biochemistry
Mitochondria
Hsp70
Cell biology
Heat shock factor
Caspases
Heat shock protein
Animals
HSP60
Signal transduction
Molecular Biology
Heat-Shock Proteins
Intracellular
Molecular Chaperones
Signal Transduction
Subjects
Details
- ISSN :
- 0006291X
- Volume :
- 304
- Database :
- OpenAIRE
- Journal :
- Biochemical and Biophysical Research Communications
- Accession number :
- edsair.doi.dedup.....044dc04be7036ac55fb1e25788896b18
- Full Text :
- https://doi.org/10.1016/s0006-291x(03)00623-5