From endoplasmic-reticulum stress to the inflammatory response

By Kezhong Zhang, R. Kaufman. Nature, 2008

1,951 citations recorded by the source corpus.

The endoplasmic reticulum is responsible for much of a cell's protein synthesis and folding, but it also has an important role in sensing cellular stress. Recently, it has been shown that the endoplasmic reticulum mediates a specific set of intracellular signalling pathways in response to the accumulation of unfolded or misfolded proteins, and these pathways are collectively known as the unfolded-protein response. New observations suggest that the unfolded-protein response can initiate inflammation, and the coupling of these responses in specialized cells and tissues is now thought to be fundamental in the pathogenesis of inflammatory diseases. The knowledge gained from this emerging field will aid in the development of therapies for modulating cellular stress and inflammation.

Subfields: Cell Biology, Epidemiology, Physiology

View Paper: https://www.semanticscholar.org/paper/9c78b5be9827b39628cbcb772f0e95a93c849285

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Citations in the corpus

Pathophysiology of placental‐derived fetal growth restriction (2018, background): “The difference in the degree of activation may have pathophysiological significance, for high levels of activation of the UPR are associated with stimulation of the release of proinflammatory cytokines, cell senescence, and even apoptosis (Figure 6).(90,91) The nuclear factor kappa-light-chain-enhan”
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Toll-like receptor activation of XBP1 regulates innate immune responses in macrophages (2010, background): “Discussion Similarities in signaling pathways stemming from TLR and ER-stress receptors have been note”
Reactive Oxygen Species in Inflammation and Tissue Injury (2014, positive): “Although the basis by which TNFR1 mutations leads to increased mitochondrial ROS is not clear, possible mechanisms include retention of the mutated protein in the endoplasmic reticulum, which can induce unfolded protein response, triggering calcium release from ER and depolarizing mitochondria by di”
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Lectin-type oxidized LDL receptor-1 distinguishes population of human polymorphonuclear myeloid-derived suppressor cells in cancer patients (2016, background): “The ER stress response pathway has been shown to regulate inflammation by activating the NF-kB pathway (35, 44, 45).”
Thioredoxin-interacting protein mediates ER stress-induced β cell death through initiation of the inflammasome (2012, background): “The crosstalk between inflammation and ER stress has been suggested to play a significant role in b cell dysfunction and death (Zhang and Kaufman, 2008).”
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