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Death versus survival: functional interaction between the apoptotic and stress-inducible heat shock protein pathways Beere HMJ Clin Invest 2005[Oct]; 115 (10): 2633-9Induction of heat shock proteins (Hsps) following cellular damage can prevent apoptosis induced by both the intrinsic and the extrinsic pathways. The intrinsic pathway is characterized by mitochondrial outer membrane permeabilization (MOMP), cytochrome c release, apoptosome assembly, and caspase activation. Hsps promote cell survival by preventing MOMP or apoptosome formation as well as via regulation of Akt and JNK activities. Engagement of the TNF death receptors induces the extrinsic pathway that is characterized by Fas-associated death domain-dependent (FADD-dependent) caspase-8 activation or induction of NF-kappaB to promote cellular survival. Hsps can directly suppress proapoptotic signaling events or stabilizing elements of the NF-kappaB pathway to promote cellular survival.|Animals[MESH]|Apoptosis/*physiology[MESH]|Caspase 8[MESH]|Caspases/metabolism[MESH]|Cell Survival/physiology[MESH]|Heat-Shock Proteins/*metabolism[MESH]|Humans[MESH]|MAP Kinase Kinase 4/metabolism[MESH]|NF-kappa B/metabolism[MESH]|Proto-Oncogene Proteins c-akt/metabolism[MESH]|Signal Transduction/*physiology[MESH]|fas Receptor/metabolism[MESH] |
