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UPR IRE1

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https://www.readbyqxmd.com/read/29324796/quercetin-and-aconitine-synergistically-induces-the-human-cervical-carcinoma-hela-cell-apoptosis-via-endoplasmic-reticulum-er-stress-pathway
#1
Xiu-Mei Li, Jing Liu, Fang-Fang Pan, Dong-Dong Shi, Zhi-Guo Wen, Pei-Long Yang
Up till now, studies have not been conducted on how the combination of Quercetin (Q), Aconitine (A) and apoptosis induction affects human cervical carcinoma HeLa cells. The result of our findings shows that the combination of Q and A (QA) is capable of synergistically inhibiting the proliferation of HeLa cells in a number of concentrations. QA synergistically inhibits the proliferation of MDR1 gene in the HeLa cells. It is concluded based on our result that QA induces apoptosis and ER stress just as QA-induced ER stress pathway may mediate apoptosis by upregulating mRNA expression levels of eIF2α, ATF4, IRE1, XBP1, ATF6, PERK and CHOP in the HeLa cells...
2018: PloS One
https://www.readbyqxmd.com/read/29316036/inhibition-of-ire1-results-in-decreased-scar-formation
#2
Tatiana V Boyko, Rakesh Bam, Dadi Jiang, Zhen Wang, Namrata Bhatia, Misha C Tran, Michael T Longaker, Albert C Koong, George P Yang
Wound healing is characterized by the production of large amounts of protein necessary to replace lost cellular mass and extracellular matrix. The unfolded protein response (UPR) is an important adaptive cellular response to increased protein synthesis. One of the main components of the UPR is IRE1, an ER transmembrane protein with endonuclease activity that produces the activated form of the transcription factor XBP1. Using luciferase reporter mice for Xbp1 splicing, we showed that IRE1 was up-regulated during excisional wound healing at the time in wound healing consistent with that of the proliferative phase, when the majority of protein synthesis for cellular proliferation and matrix deposition occurs...
January 8, 2018: Wound Repair and Regeneration
https://www.readbyqxmd.com/read/29303481/in-vitro-fret-analysis-of-ire1-and-bip-association-and-dissociation-upon-endoplasmic-reticulum-stress
#3
Megan C Kopp, Piotr R Nowak, Natacha Larburu, Christopher J Adams, Maruf Mu Ali
The unfolded protein response (UPR) is a key signaling system that regulates protein homeostasis within the endoplasmic reticulum (ER). The primary step in UPR activation is the detection of misfolded proteins, the mechanism of which is unclear. We have previously suggested an allosteric mechanism for UPR induction (Carrara et al., 2015) based on qualitative pull-down assays. Here, we develop an in vitro Förster resonance energy transfer (FRET) UPR induction assay that quantifies IRE1 luminal domain and BiP association and dissociation upon addition of misfolded proteins...
January 5, 2018: ELife
https://www.readbyqxmd.com/read/29235576/the-unfolded-protein-response-impacts-melanoma-progression-by-enhancing-fgf-expression-and-can-be-antagonized-by-a-chemical-chaperone
#4
Karin Eigner, Yüksel Filik, Florian Mark, Birgit Schütz, Günter Klambauer, Richard Moriggl, Markus Hengstschläger, Herbert Stangl, Mario Mikula, Clemens Röhrl
The mechanisms hallmarking melanoma progression are insufficiently understood. Here we studied the impact of the unfolded protein response (UPR) - a signalling cascade playing ambiguous roles in carcinogenesis - in melanoma malignancy. We identified isogenic patient-derived melanoma cell lines harboring BRAFV600E-mutations as a model system to study the role of intrinsic UPR in melanoma progression. We show that the activity of the three effector pathways of the UPR (ATF6, PERK and IRE1) was increased in metastatic compared to non-metastatic cells...
December 13, 2017: Scientific Reports
https://www.readbyqxmd.com/read/29198525/a-j-protein-co-chaperone-recruits-bip-to-monomerize-ire1-and-repress-the-unfolded-protein-response
#5
Niko Amin-Wetzel, Reuben A Saunders, Maarten J Kamphuis, Claudia Rato, Steffen Preissler, Heather P Harding, David Ron
When unfolded proteins accumulate in the endoplasmic reticulum (ER), the unfolded protein response (UPR) increases ER-protein-folding capacity to restore protein-folding homeostasis. Unfolded proteins activate UPR signaling across the ER membrane to the nucleus by promoting oligomerization of IRE1, a conserved transmembrane ER stress receptor. However, the coupling of ER stress to IRE1 oligomerization and activation has remained obscure. Here, we report that the ER luminal co-chaperone ERdj4/DNAJB9 is a selective IRE1 repressor that promotes a complex between the luminal Hsp70 BiP and the luminal stress-sensing domain of IRE1α (IRE1LD)...
November 30, 2017: Cell
https://www.readbyqxmd.com/read/29184100/akt-mtor-signaling-modulates-the-dynamics-of-ire1-rnase-activity-by-regulating-er-mitochondria-contacts
#6
Miguel Sanchez-Alvarez, Miguel Angel Del Pozo, Chris Bakal
Inositol Requiring Enzyme-1 (IRE1) is the most conserved transducer of the Unfolded Protein Response (UPR), a surveillance mechanism that ensures homeostasis of the endoplasmic reticulum (ER) in eukaryotes. IRE1 activation orchestrates adaptive responses, including lipid anabolism, metabolic reprogramming, increases in protein folding competency, and ER expansion/remodeling. However, we still know surprisingly little regarding the principles by which this ER transducer is deactivated upon ER stress clearance...
November 28, 2017: Scientific Reports
https://www.readbyqxmd.com/read/29163417/csfv-infection-up-regulates-the-unfolded-protein-response-to-promote-its-replication
#7
Wencheng He, Hailuan Xu, Hongchao Gou, Jin Yuan, Jiedan Liao, Yuming Chen, Shuangqi Fan, Baoming Xie, Shaofeng Deng, Yangyi Zhang, Jinding Chen, Mingqiu Zhao
Classical swine fever (CSF) is an OIE-listed, highly contagious animal disease caused by classical swine fever virus (CSFV). The endoplasmic reticulum (ER) is an organelle in which the replication of many RNA viruses takes place. During viral infection, a series of events elicited in cells can destroy the ER homeostasis that cause ER stress and induce an unfolded protein response (UPR). In this study, we demonstrate that ER stress was induced during CSFV infection as several UPR-responsive elements such as XBP1(s), GRP78 and CHOP were up-regulated...
2017: Frontiers in Microbiology
https://www.readbyqxmd.com/read/29152224/recent-insights-into-perk-dependent-signaling-from-the-stressed-endoplasmic-reticulum
#8
REVIEW
Alexander McQuiston, J Alan Diehl
The unfolded protein response (UPR) is an evolutionarily conserved stress response to intra- and extracellular conditions that disrupt endoplasmic reticulum (ER) protein-folding capacity. The UPR is engaged by a variety of disease conditions, including most cancers as well as both metabolic and neurodegenerative disorders. Three transmembrane transducers-PERK, IRE1, and ATF6-are responsible for activating downstream signaling pathways that mediate the UPR and subsequent stress response pathways. PERK, an ER resident transmembrane protein kinase, initiates both pro-apoptotic and pro-survival signaling pathways...
2017: F1000Research
https://www.readbyqxmd.com/read/29124827/recovery-from-temporary-er-stress-in-plants-relies-on-tissue-specific-and-largely-independent-roles-of-bzip28-and-bzip60-as-well-as-an-antagonizing-function-of-bax-inhibitor1-onto-the-pro-adaptive-signaling-mediated-by-bzip28
#9
Cristina Ruberti, YaShiuan Lai, Federica Brandizzi
The unfolded protein response (UPR) is an ancient signaling pathway that commits to life-or-death outcomes in response to proteotoxic stress in the endoplasmic reticulum (ER). In plants, the membrane-tethered transcription factor bZIP28 and the ribonuclease-kinase IRE1 along with its splicing target, bZIP60, govern the two cytoprotective UPR signaling pathways known to date. The conserved ER membrane-associated BAX inhibitor1 (BI1) modulates ER stress-induced programmed cell death through yet-unknown mechanisms...
November 10, 2017: Plant Journal: for Cell and Molecular Biology
https://www.readbyqxmd.com/read/29113324/unfolded-protein-response-signaling-impacts-macrophage-polarity-to-modulate-breast-cancer-cell-clearance-and-melanoma-immune-checkpoint-therapy-responsiveness
#10
David R Soto-Pantoja, Adam S Wilson, Kenysha Yj Clear, Brian Westwood, Pierre L Triozzi, Katherine L Cook
The unfolded protein response (UPR) is a stress pathway controlled by GRP78 to mediate IRE1, PERK, and ATF6 signaling. We show that targeting GRP78, IRE1, and PERK differentially regulates macrophage polarization. Specifically, PERK targeting enhanced macrophage proliferation and macrophage-mediated killing but not GRP78 or IRE1. Targeting UPR in cancer cells also differentially affected macrophage cytolytic capacity. Tumoral IRE1 or GRP78 inhibition enhanced macrophage-mediated cancer cell clearance. Conditioned media from GRP78-silenced cancer cells caused reciprocal regulation of CD80 and CD206, suggesting control of plasticity by secreted factors...
October 6, 2017: Oncotarget
https://www.readbyqxmd.com/read/29074489/autophagy-and-the-unfolded-protein-response-promote-pro-fibrotic-effects-of-tgf%C3%AE-1-in-human-lung-fibroblasts
#11
Saeid Ghavami, Behzad Yeganeh, Amir A Zeki, Shahla Shojaei, Nicholas J Kenyon, Sean Ott, Afshin Samali, John Patterson, Javad Alizadeh, Adel Rezaei Moghadam, Ian M C Dixon, Helmut Unruh, Darryl A Knight, Martin Post, Thomas Klonisch, Andrew John Halayko
BACKGROUND: Idiopathic pulmonary fibrosis (IPF) is a lethal fibrotic lung disease in adults with limited treatment options. Autophagy and the unfolded protein response (UPR), fundamental processes induced by cell stress, are dysregulated in lung fibroblasts and epithelial cells from humans with IPF. METHODS: Human primary cultured lung parenchymal and airway fibroblasts from non-IPF and IPF donors were stimulated with TGFβ1 with or without the inhibitors of autophagy or UPR (IRE1α inhibitor)...
October 26, 2017: American Journal of Physiology. Lung Cellular and Molecular Physiology
https://www.readbyqxmd.com/read/29044123/ire1%C3%AE-xbp1s-branch-of-upr-links-hif1%C3%AE-activation-to-mediate-angii-dependent-endothelial-dysfunction-under-particulate-matter-pm-2-5-exposure
#12
Xiuduan Xu, Aodeng Qimuge, Hongli Wang, Chen Xing, Ye Gu, Shasha Liu, Huan Xu, Meiru Hu, Lun Song
Short- and long-term exposure to particulate matter (PM) 2.5 instigates adverse health effect upon the cardiovascular (CV) system. Disclosing the molecular events by which PM2.5 evokes CV injuries is essential in developing effective risk-reduction strategy. Here we found that rats after intratracheally instillation with PM2.5 displayed increased circulating level of ANGII, the major bioactive peptide in renin-angiotensin-system (RAS), which resulted from the elevation of ANGII production in the vascular endothelium...
October 18, 2017: Scientific Reports
https://www.readbyqxmd.com/read/29024602/knockdown-of-cemip-suppresses-proliferation-and-induces-apoptosis-in-colorectal-cancer-cells-downregulation-of-grp78-and-attenuation-of-unfolded-protein-response
#13
Guodong Liang, Xuedong Fang, Yubo Yang, Yan Song
Cell migration inducing hyaluronan binding protein (CEMIP) has been suggested as a contributor in the carcinogenesis of colorectal cancer (CRC). Cancer cells can adapt to endoplasmic reticulum (ER) stress by initiating unfolded protein response (UPR). This study aimed at investigating whether CEMIP affected the UPR of CRC cells, with a focus on 78 kDa glucose-regulated protein (GRP78, a major ER chaperone). We found that knockdown of CEMIP inhibited cell proliferation and induced a G1 arrest in SW480 CRC cells...
October 12, 2017: Biochemistry and Cell Biology, Biochimie et Biologie Cellulaire
https://www.readbyqxmd.com/read/28971800/an-unfolded-protein-induced-conformational-switch-activates-mammalian-ire1
#14
Gülsün Elif Karagöz, Diego Acosta-Alvear, Hieu T Nguyen, Crystal P Lee, Feixia Chu, Peter Walter
The unfolded protein response (UPR) adjusts the cell's protein folding capacity in the endoplasmic reticulum (ER) according to need. IRE1 is the most conserved UPR sensor in eukaryotic cells. It has remained controversial, however, whether mammalian and yeast IRE1 use a common mechanism for ER stress sensing. Here, we show that similar to yeast, human IRE1α's ER-lumenal domain (hIRE1α LD) binds peptides with a characteristic amino acid bias. Peptides and unfolded proteins bind to hIRE1α LD's MHC-like groove and induce allosteric changes that lead to its oligomerization...
October 3, 2017: ELife
https://www.readbyqxmd.com/read/28952924/unfolded-protein-response-transducer-ire1-mediated-signaling-independent-of-xbp1-mrna-splicing-is-not-required-for-growth-and-development-of-medaka-fish
#15
Tokiro Ishikawa, Makoto Kashima, Atsushi J Nagano, Tomoko Ishikawa-Fujiwara, Yasuhiro Kamei, Takeshi Todo, Kazutoshi Mori
When activated by the accumulation of unfolded proteins in the endoplasmic reticulum, metazoan IRE1, the most evolutionarily conserved unfolded protein response (UPR) transducer, initiates unconventional splicing of XBP1 mRNA. Unspliced and spliced mRNA are translated to produce pXBP1(U) and pXBP1(S), respectively. pXBP1(S) functions as a potent transcription factor, whereas pXBP1(U) targets pXBP1(S) to degradation. In addition, activated IRE1 transmits two signaling outputs independent of XBP1, namely activation of the JNK pathway, which is initiated by binding of the adaptor TRAF2 to phosphorylated IRE1, and regulated IRE1-dependent decay (RIDD) of various mRNAs in a relatively nonspecific manner...
September 27, 2017: ELife
https://www.readbyqxmd.com/read/28945192/regulated-ire1-dependent-mrna-decay-requires-no-go-mrna-degradation-to-maintain-endoplasmic-reticulum-homeostasis-in-s-pombe
#16
Nicholas R Guydosh, Philipp Kimmig, Peter Walter, Rachel Green
The unfolded protein response (UPR) monitors and adjusts the protein folding capacity of the endoplasmic reticulum (ER). In S. pombe, the ER membrane-resident kinase/endoribonuclease Ire1 utilizes a mechanism of selective degradation of ER-bound mRNAs (RIDD) to maintain homeostasis. We used a genetic screen to identify factors critical to the Ire1-mediated UPR and found several proteins, Dom34, Hbs1 and Ski complex subunits, previously implicated in ribosome rescue and mRNA no-go-decay (NGD). Ribosome profiling in ER-stressed cells lacking these factors revealed that Ire1-mediated cleavage of ER-associated mRNAs results in ribosome stalling and mRNA degradation...
September 25, 2017: ELife
https://www.readbyqxmd.com/read/28929194/adapting-secretory-proteostasis-and-function-through-the-unfolded-protein-response
#17
Madeline Y Wong, Andrew S DiChiara, Patreece H Suen, Kenny Chen, Ngoc-Duc Doan, Matthew D Shoulders
Cells address challenges to protein folding in the secretory pathway by engaging endoplasmic reticulum (ER)-localized protective mechanisms that are collectively termed the unfolded protein response (UPR). By the action of the transmembrane signal transducers IRE1, PERK, and ATF6, the UPR induces networks of genes whose products alleviate the burden of protein misfolding. The UPR also plays instructive roles in cell differentiation and development, aids in the response to pathogens, and coordinates the output of professional secretory cells...
September 20, 2017: Current Topics in Microbiology and Immunology
https://www.readbyqxmd.com/read/28921568/neuronal-activity-dependent-local-activation-of-dendritic-unfolded-protein-response-promotes-expression-of-brain-derived-neurotrophic-factor-in-cell-soma
#18
Atsushi Saito, Longjie Cai, Koji Matsuhisa, Yosuke Ohtake, Masayuki Kaneko, Soshi Kanemoto, Rie Asada, Kazunori Imaizumi
Unfolded protein response (UPR) has roles not only in resolving the accumulation of unfolded proteins owing to endoplasmic reticulum (ER) stress, but also in regulation of cellular physiological functions. ER stress transducers providing the branches of UPR signaling are known to localize in distal dendritic ER of neurons. These reports suggest that local activation of UPR branches may produce integrated outputs for distant communication, and allow regulation of local events in highly polarized neurons. Here, we demonstrated that synaptic activity- and brain-derived neurotrophic factor (BDNF)-dependent local activation of UPR signaling could be associated with dendritic functions through retrograde signal propagation by using murine neuroblastoma cell line, Neuro-2A and primary cultured hippocampal neurons derived from postnatal day 0 litter C57BL/6 mice...
September 16, 2017: Journal of Neurochemistry
https://www.readbyqxmd.com/read/28915629/ier3ip1-deficiency-leads-to-increased-%C3%AE-cell-death-and-decreased-%C3%AE-cell-proliferation
#19
Juan Sun, Decheng Ren
Mutations in the gene for Immediate Early Response 3 Interacting Protein 1 (IER3IP1) cause permanent neonatal diabetes mellitus in human. The mechanisms involved have not been determined and the role of IER3IP1 in β-cell survival has not been characterized. In order to determine if there is a molecular link between IER3IP1 deficiency and β-cell survival and proliferation, we knocked down Ier3ip1 gene expression in mouse MIN6 insulinoma cells. IER3IP1 suppression induced apoptotic cell death which was associated with an increase in Bim and a decrease in Bcl-xL...
August 22, 2017: Oncotarget
https://www.readbyqxmd.com/read/28888981/hypoxia-in-3t3-l1-adipocytes-suppresses-adiponectin-expression-via-the-perk-and-ire1-unfolded-protein-response
#20
Qian Guo, Sanli Jin, Hailong Hu, Ying Zhou, Yuheng Yan, He Zong, Yu Wang, Hongjuan He, Yuri Oh, Chuanpeng Liu, Ning Gu
Adiponectin, an adipocytokine produced by adipocytes, functions as an anti-inflammatory and anti-apoptotic substance, while also enhancing insulin sensitivity. Patients or model animals with obesity or diabetes typically present attenuated expression of adiponectin. Moreover, obesity and diabetes are often accompanied with hypoxia in adipose tissue, which may result in endoplasmic reticulum (ER) stress as well as low expression of adiponectin. The purpose of this study was to investigate the specific role of the unfolded protein response (UPR) involved in the low expression of adiponectin induced by hypoxia...
November 4, 2017: Biochemical and Biophysical Research Communications
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