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Cell Death Differ. 2007 Jun;14(6):1172-80. Epub 2007 Mar 30.

Endoplasmic reticulum stress-induced cell death mediated by the proteasome.

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1
The Buck Institute for Age Research, Novato, CA 94945, USA. lotti.egger@bluemail.ch

Abstract

Cells exposed to sustained endoplasmic reticulum (ER) stress undergo programmed cell death and display features typical of apoptosis, such as cysteine aspartyl protease (caspase) activation, cytochrome c release, and DNA fragmentation. Here, we show that the execution of cell death induced by ER stress is mediated via the proteasome. Inhibition of the proteasome by lactacystin prevented ER stress-induced degradation of Bcl-2, release of cytochrome c, processing of effector caspase-3, and exposure of phosphatidylserine. Owing to the ability of lactacystin to inhibit cytochrome c release, we propose that the pro-apoptotic activity of the proteasome lies upstream of mitochondrial activation. Thus, the proteasome serves as a principal mediator of ER stress-induced cell death in this system.

PMID:
17396132
PMCID:
PMC2748804
DOI:
10.1038/sj.cdd.4402125
[Indexed for MEDLINE]
Free PMC Article

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