From endoplasmic-reticulum stress to the inflammatory response
Kezhong Zhang,Randal J. Kaufman +1 more
TL;DR: 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.
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Abstract: 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.
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The protective microRNA-199a-5p-mediated unfolded protein response in hypoxic cardiomyocytes is regulated by STAT3 pathway
TL;DR: The activation of STAT3 signaling in cardiomyocytes during chronic hypoxia leads to downregulation of miR-199a-5p, which promotes the expression of many downstream target genes, which is an important pathway in the adaptive protection mechanism of myocardium during Hypoxia.
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Different early ER-stress responses in the CLN8(mnd) mouse model of neuronal ceroid lipofuscinosis.
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TL;DR: It is suggested that early ER-stress responses distinctly combined and ER- stress pathways integrated with inflammatory responses may contribute to the progression of the CLN8(mnd) disease in CNS structures.
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