Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-β View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2000-01

AUTHORS

Toshiyuki Nakagawa, Hong Zhu, Nobuhiro Morishima, En Li, Jin Xu, Bruce A. Yankner, Junying Yuan

ABSTRACT

Apoptosis, or cellular suicide, is important for normal development and tissue homeostasis, but too much or too little apoptosis can also cause disease1,2. The family of cysteine proteases, the so-called caspases, are critical mediators of programmed cell death3, and thus far 14 family members have been identified. Some of these, such as caspase-8 (refs 4, 5), mediate signal transduction downstream of death receptors located on the plasma membrane. Others, such as caspase-9 (ref. 6), mediate apoptotic signals after mitochondrial damage. Stress in the endoplasmic reticulum (ER) can also result in apoptosis7. Here we show that caspase-12 is localized to the ER and activated by ER stress, including disruption of ER calcium homeostasis and accumulation of excess proteins in ER, but not by membrane- or mitochondrial-targeted apoptotic signals. Mice that are deficient in caspase-12 are resistant to ER stress-induced apoptosis, but their cells undergo apoptosis in response to other death stimuli. Furthermore, we show that caspase-12-deficient cortical neurons are defective in apoptosis induced by amyloid-β protein but not by staurosporine or trophic factor deprivation. Thus, caspase-12 mediates an ER-specific apoptosis pathway and may contribute to amyloid-β neurotoxicity. More... »

PAGES

98-103

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/47513

DOI

http://dx.doi.org/10.1038/47513

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1020577355

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/10638761


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