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Unfolded Protein Response Regulation in Keloid Cells

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TLDR
It is demonstrated here that there is a specific up-regulation of one facet of the UPR response, which may represent a specific molecular defect in KFs compared with NFs, and also suggests modulation of theUPR can be used in wound healing therapy.
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This article is published in Journal of Surgical Research.The article was published on 2011-05-01 and is currently open access. It has received 15 citations till now. The article focuses on the topics: Unfolded protein response.

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The role of NLRP3-CASP1 in inflammasome-mediated neuroinflammation and autophagy dysfunction in manganese-induced, hippocampal-dependent impairment of learning and memory ability

TL;DR: It is demonstrated that Mn activates the NLRP3-CASP1 inflammasome pathway in the hippocampus of mice and BV2 cells by triggering autophagy-lysosomal dysfunction, leading to hippocampal-dependent impairment in learning and memory, which is associated with the pathogenesis of Alzheimer disease.

From endoplasmic reticulum stress to the inflammatory response.

TL;DR: 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 as mentioned in this paper.
References
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Journal ArticleDOI

Signal integration in the endoplasmic reticulum unfolded protein response

TL;DR: Together, at least three mechanistically distinct arms of the UPR regulate the expression of numerous genes that function within the secretory pathway but also affect broad aspects of cell fate and the metabolism of proteins, amino acids and lipids.
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Protein folding in the cell.

TL;DR: Folding and assembly of polypeptides in vivo involves other proteins, many of which belong to families that have been highly conserved during evolution.
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XBP1 mRNA Is Induced by ATF6 and Spliced by IRE1 in Response to ER Stress to Produce a Highly Active Transcription Factor

TL;DR: The transcription factor XBP1, a target of ATF6, is identified as a mammalian substrate of such an unconventional mRNA splicing system and it is shown that only the spliced form of X BP1 can activate the UPR efficiently.
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The mammalian unfolded protein response

TL;DR: In the endoplasmic reticulum (ER), secretory and transmembrane proteins fold into their native conformation and undergo posttranslational modifications important for their activity and structure as mentioned in this paper.
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From endoplasmic-reticulum stress to the inflammatory response

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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