[HTML][HTML] Death versus survival: functional interaction between the apoptotic and stress-inducible heat shock protein pathways

HM Beere - The Journal of clinical investigation, 2005 - Am Soc Clin Investig
HM Beere
The Journal of clinical investigation, 2005Am Soc Clin Investig
Induction 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 …
Induction 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-κB to promote cellular survival. Hsps can directly suppress proapoptotic signaling events or stabilizing elements of the NF-κB pathway to promote cellular survival.
The Journal of Clinical Investigation