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https://www.readbyqxmd.com/read/29334839/bax-inhibitor-1-is-required-for-resisting-the-early-brain-injury-induced-by-subarachnoid-hemorrhage-through-regulating-ire1-jnk-pathway
#1
Lei Shi, Zaizong Wang, Xianjin Liu, Mao Li, Shangfei Zhang, Xiaobin Song
Background and Purpose Bax inhibitor-1 (BI-1) has been identified as a suppressor of Bax-mediated cell apoptosis by regulation of endoplasmic reticulum stress-induced cell death. However, the role of BI-1 in Early Brain Injury (EBI) after subarachnoid hemorrhage (SAH) remains unclear. In the present study, we aim to explore the neuroprotective functions of BI-1 in EBI after SAH by using models of SAH that induced endovascular perforation in rats. Method The neurological score, brain water content and blood-brain barrier (BBB) permeability were evaluated simultaneously as prognostic indicators...
January 16, 2018: Neurological Research
https://www.readbyqxmd.com/read/29324796/quercetin-and-aconitine-synergistically-induces-the-human-cervical-carcinoma-hela-cell-apoptosis-via-endoplasmic-reticulum-er-stress-pathway
#2
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
#3
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/29315210/isoaaptamine-induces-t-47d-cells-apoptosis-and-autophagy-via-oxidative-stress
#4
Chih-Fung Wu, Man-Gang Lee, Mohamed El-Shazly, Kuei-Hung Lai, Seng-Chung Ke, Chiang-Wen Su, Shou-Ping Shih, Ping-Jyun Sung, Ming-Chang Hong, Zhi-Hong Wen, Mei-Chin Lu
Aaptos is a genus of marine sponge which belongs to Suberitidae and is distributed in tropical and subtropical oceans. Bioactivity-guided fractionation of Aaptos sp. methanolic extract resulted in the isolation of aaptamine, demethyloxyaaptamine, and isoaaptamine. The cytotoxic activity of the isolated compounds was evaluated revealing that isoaaptamine exhibited potent cytotoxic activity against breast cancer T-47D cells. In a concentration-dependent manner, isoaaptamine inhibited the growth of T-47D cells as indicated by short-(MTT) and long-term (colony formation) anti-proliferative assays...
January 9, 2018: Marine Drugs
https://www.readbyqxmd.com/read/29311133/dual-ire1-rnase-functions-dictate-glioblastoma-development
#5
Stéphanie Lhomond, Tony Avril, Nicolas Dejeans, Konstantinos Voutetakis, Dimitrios Doultsinos, Mari McMahon, Raphaël Pineau, Joanna Obacz, Olga Papadodima, Florence Jouan, Heloise Bourien, Marianthi Logotheti, Gwénaële Jégou, Néstor Pallares-Lupon, Kathleen Schmit, Pierre-Jean Le Reste, Amandine Etcheverry, Jean Mosser, Kim Barroso, Elodie Vauléon, Marion Maurel, Afshin Samali, John B Patterson, Olivier Pluquet, Claudio Hetz, Véronique Quillien, Aristotelis Chatziioannou, Eric Chevet
Proteostasis imbalance is emerging as a major hallmark of cancer, driving tumor aggressiveness. Evidence suggests that the endoplasmic reticulum (ER), a major site for protein folding and quality control, plays a critical role in cancer development. This concept is valid in glioblastoma multiform (GBM), the most lethal primary brain cancer with no effective treatment. We previously demonstrated that the ER stress sensor IRE1α (referred to as IRE1) contributes to GBM progression, through XBP1 mRNA splicing and regulated IRE1-dependent decay (RIDD) of RNA Here, we first demonstrated IRE1 signaling significance to human GBM and defined specific IRE1-dependent gene expression signatures that were confronted to human GBM transcriptomes...
January 8, 2018: EMBO Molecular Medicine
https://www.readbyqxmd.com/read/29303481/in-vitro-fret-analysis-of-ire1-and-bip-association-and-dissociation-upon-endoplasmic-reticulum-stress
#6
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/29236388/inhibition-of-ire1-modifies-hypoxic-regulation-of-g6pd-gpi-tkt-taldo1-pgls-and-rpia-genes-expression-in-u87-glioma-cells
#7
O H Minchenko, I A Garmash, D O Minchenko, A Y Kuznetsova, O O Ratushna
We have studied the effect of hypoxia on the expression level of mRNA of the basic enzymes of pentose-phosphate cycle (G6PD, TKT, TALDO1, PGLS and RPIA) and glucose-6-phosphate isomerase (GPI) in U87 glioma cells in relation to inhibition of IRE1 (inositol requiring enzyme 1). It was shown that hypoxia leads to up-regulation of the expression of GPI and PGLS genes and to down-regulation of TALDO1 and RPIA genes in control glioma cells. Changes for GPI gene were more significant than for other genes. At the same time, inhibition of IRE1 modified the effect of hypoxia on the expression of all studied genes...
January 2017: Ukrainian Biochemical Journal
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
#8
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/29230396/altered-expression-of-endoplasmic-reticulum-stress-related-genes-in-the-middle-frontal-cortex-of-subjects-with-autism-spectrum-disorder
#9
Amanda Crider, Anthony O Ahmed, Anilkumar Pillai
The endoplasmic reticulum (ER) is an important organelle responsible for the folding and sorting of proteins. Disturbances in ER homeostasis can trigger a cellular response known as the unfolded protein response, leading to accumulation of unfolded or misfolded proteins in the ER lumen called ER stress. A number of recent studies suggest that mutations in autism spectrum disorder (ASD)-susceptible synaptic genes induce ER stress. However, it is not known whether ER stress-related genes are altered in the brain of ASD subjects...
November 2017: Molecular Neuropsychiatry
https://www.readbyqxmd.com/read/29212664/genetic-bypass-of-essential-rna-repair-enzymes-in-budding-yeast
#10
Patrick D Cherry, Laura K White, Kerri York, Jay R Hesselberth
RNA repair enzymes catalyze rejoining of an RNA molecule after cleavage of phosphodiester linkages. RNA repair in budding yeast is catalyzed by two separate enzymes that process tRNA exons during their splicing and HAC1 mRNA exons during activation of the unfolded protein response. The RNA ligase Trl1 joins 2',3'-cyclic phosphate and 5'-hydroxyl RNA fragments, creating a new phosphodiester linkage with a 2'-phosphate at the junction. The 2'-phosphate is subsequently removed by the 2'-phosphotransferase Tpt1, which catalyzes phosphate transfer to NAD+, producing nicotinamide and a unique ADP ribose metabolite...
December 6, 2017: RNA
https://www.readbyqxmd.com/read/29212205/jnk-inhibitor-alleviates-apoptosis-of-fetal-neural-stem-cells-induced-by-emulsified-isoflurane
#11
Lei Zhou, Zeyong Yang, Xianfu Lu, Xingxing Li, Xiaohu An, Jing Chai, Qiling Yang, Shikai Yan, Yuanhai Li
Isoflurane can provide both neuroprotection and neurotoxicity in various culture models and in rodent developing brains. Emulsified Isoflurane (EI) is an emulsion formulation of isoflurane, while its underlying molecular mechanism of developemental nerve toxicity largely remains unclear. We hypothesized that EI induced fetal neural stem cells (FNSCs) apoptosis, endoplasmic reticulum (ER) stress and c-Jun N-terminal kinase (JNK) activation. FNSCs were isolated from the cortex of SD rats during 14 days of gestation...
November 7, 2017: Oncotarget
https://www.readbyqxmd.com/read/29198525/a-j-protein-co-chaperone-recruits-bip-to-monomerize-ire1-and-repress-the-unfolded-protein-response
#12
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
#13
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/29176553/notoginsenoside-r1-alleviates-oxygen-glucose-deprivation-reoxygenation-injury-by-suppressing-endoplasmic-reticulum-calcium-release-via-plc
#14
Yan Wang, Liu Tu, Yingbo Li, Di Chen, Zhao Liu, Xuelian Hu, Shali Wang
As documented in our previous study, notoginsenoside R1 (NGR1) can inhibit neuron apoptosis and the expression of endoplasmic reticulum (ER) stress-associated pro-apoptotic proteins in hypoxic-ischemic encephalopathy. Recent evidence indicates that the Phospholipase C (PLC)/inositol 1,4,5-trisphosphate receptor (IP3R) is important for the regulation of Ca2+ release in the ER. Ca2+ imbalance can stimulate ER stress, CAMKII, and cell apoptosis. The purpose of this study was to further investigate the neuroprotective effect of NGR1 and elucidate how NGR1 regulates ER stress and cell apoptosis in the oxygen-glucose deprivation/reoxygenation (OGD/R) model...
November 24, 2017: Scientific Reports
https://www.readbyqxmd.com/read/29169414/-over-expressed-bax-inhibitor-1-bi-1-inhibits-apoptosis-of-hippocampal-neurons-via-endoplasmic-reticulum-ire1-jnk-pathway-in-rats-with-subarachnoid-hemorrhage
#15
Jiaxin Liu, Shuai Zhou, Xiying Qian, Yueting Zhang, Jianhua Zhao
Objective To investigate the protective effect of lentivirus-mediated BI-1 overexpression on hippocampal neurons in rats with subarachnoid hemorrhage (SAH) and the relationship with endoplasmic reticulum IRE1-JNK signaling pathway. Methods The lentivirus solution of BI-1 over-expression was injected into the brain of rats 24 hours before SAH rat model was established by intravascular puncture method. At 24 hours after modeling, the brain water content and neurological score of the rats were measured. The apoptosis of hippocampal neurons was detected by TUNEL assay...
October 2017: Xi Bao Yu Fen Zi Mian Yi Xue za Zhi, Chinese Journal of Cellular and Molecular Immunology
https://www.readbyqxmd.com/read/29163417/csfv-infection-up-regulates-the-unfolded-protein-response-to-promote-its-replication
#16
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
#17
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
#18
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
#19
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/29107182/identification-of-the-internal-ribosome-entry-sites-ires-of-prion-protein-gene
#20
Xiao-Nuan Luo, Qin-Qin Song, Jie Yu, Juan Song, Xin-Ling Wang, Dong Xia, Peng Sun, Jun Han
Many studies demonstrated that there are several type bands of prion protein in cells. However, the formation of different prion protein bands is elusive. After several low molecular weight bands of prion protein appeared in SMB-S15 cells infected with scrapie agent Chandler, we think that IRES-dependent translation mechanism induced by prion is involved in the formation of prion protein bands. Then we designed a series of pPrP-GFP fusing plasmids and bicistronic plasmids to identify the IRES sites of prion protein gene and found 3 IRES sites inside of PrP mRNA...
October 26, 2017: International Journal of Biochemistry & Cell Biology
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