Citation Details
Involvement of caspase-4 in endoplasmic reticulum stress-induced apoptosis and A-induced cell death
| Authors |  Hitomi J, Katayama T, Eguchi Y, Kudo T, Taniguchi M, Koyama Y, Manabe T, Yamagishi S, Bando Y, Imaizumi K, Tsujimoto Y, Tohyama M |
| In | J Cell Biol (2004) 165(3): 347-356 |
| Cells used in publication | HeLa Epithelial Cells Cell Lines Species: human Tissue Origin: cervix |
| Substrate | siRNA |
| Application | RNAi |
| Topics | ApoptosisDiseases (e.g. HIV)Signal transduction |
| Research Area | Neurobiology |
Research Field
Recent studies have suggested that neuronal death in Alzheimer’s disease or in ischemia is related to stress acting on the endoplasmic reticulum (ER), which leads to intraluminal accumulation of unfolded proteins. ER stress induces three major cellular responses: unfolded protein response, ER-associated degradation by the proteasome, and apoptosis. Caspase-4 is primarily activated in ER stress-induced apoptosis and can function as an ER stress-specific caspase in humans.
Nucleofection Experiments
Caspase-4 was efficiently knocked down by transfection of human cervix carcinoma cell line HeLa with a caspase-4 siRNA, significantly increasing the resistance to ER stress-induced cell death.
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