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Kennedy, D,Jager, R,Mosser, DD,Samali, A
2014
May
Regulation of Apoptosis by Heat Shock Proteins
Published
1
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cell death apoptosis intrinsic pathway heat shock proteins caspases heat shock response STRESS-INDUCED APOPTOSIS CYTOCHROME-C RELEASE HEAT-SHOCK-PROTEIN-70 INHIBITS APOPTOSIS KAPPA-B ACTIVATION MOLECULAR CHAPERONES CELL-DEATH BAX TRANSLOCATION PC12 CELLS PROTEASOMAL DEGRADATION CONFERS RESISTANCE
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. (C) 2014
327
338
10.1002/iub.1274
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