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Li, Gang; Mongillo, Marco; Chin, King-Tung; Harding, Heather; Ron, David; Marks, Andrew R; Tabas, Ira
The Journal of cell biology, 09/2009, Letnik: 186, Številka: 6Journal Article
Endoplasmic reticulum (ER) stress-induced apoptosis is involved in many diseases, but the mechanisms linking ER stress to apoptosis are incompletely understood. Based on roles for C/EPB homologous protein (CHOP) and ER calcium release in apoptosis, we hypothesized that apoptosis involves the activation of inositol 1,4,5-triphosphate (IP3) receptor (IP3R) via CHOP-induced ERO1-α (ER oxidase 1 α). In ER-stressed cells, ERO1-α is induced by CHOP, and small interfering RNA (siRNA) knockdown of ERO1-α suppresses apoptosis. IP3-induced calcium release (IICR) is increased during ER stress, and this response is blocked by siRNA-mediated silencing of ERO1-α or IP3R1 and by loss-of-function mutations in Ero1a or CHOP: Reconstitution of ERO1-α in Chop⁻/⁻ macrophages restores ER stress-induced IICR and apoptosis. In vivo, macrophages from wild-type mice but not Chop⁻/⁻ mice have elevated IICR when the animals are challenged with the ER stressor tunicamycin. Macrophages from insulin-resistant ob/ob mice, another model of ER stress, also have elevated IICR. These data shed new light on how the CHOP pathway of apoptosis triggers calcium-dependent apoptosis through an ERO1-α-IP3R pathway.
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