Journal
JOURNAL OF BIOCHEMISTRY
Volume 151, Issue 3, Pages 217-219Publisher
OXFORD UNIV PRESS
DOI: 10.1093/jb/mvr143
Keywords
apoptosis; CHOP; inflammation; ER stress; UPR
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Funding
- Grants-in-Aid for Scientific Research [20390477, 22020007] Funding Source: KAKEN
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The accumulation of unfolded proteins in the endoplasmic reticulum (ER) induces ER stress. To restore ER homeostasis, cells possess a highly specific ER quality-control system called the unfold protein response (UPR). In the case of prolonged ER stress or UPR malfunction, apoptosis signalling is activated. This ER stress-induced apoptosis has been implicated in the pathogenesis of several conformational diseases. CCAAT-enhancer-binding protein homologous protein (CHOP) is induced by ER stress and mediates apoptosis. Recent studies by the Gotoh group have shown that the CHOP pathway is also involved in ER stress-induced cytokine production in macrophages. The multifunctional roles of CHOP in the ER stress response are discussed below.
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