Dissertations / Theses on the topic 'Endoplasmic reticulum stress'
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Johnson, Charlotte. "Targeting endoplasmic reticulum stress and autophagy in cancer." Thesis, Cardiff University, 2015. http://orca.cf.ac.uk/84379/.
Full textZachariah, Matshediso. "High selenium induces endothelial dysfunction via endoplasmic reticulum stress." Thesis, University of Surrey, 2017. http://epubs.surrey.ac.uk/845246/.
Full textVoyias, Philip D. "Regulation of endoplasmic reticulum stress in adipose tissue metabolism." Thesis, University of Warwick, 2015. http://wrap.warwick.ac.uk/74256/.
Full textFurmanik, Malgorzata. "The role of endoplasmic reticulum stress in vascular calcification." Thesis, King's College London (University of London), 2015. http://kclpure.kcl.ac.uk/portal/en/theses/the-role-of-endoplasmic-reticulum-stress-in-vascular-calcification(a0138614-e3d8-42ef-9cbf-02a01f6e6eaf).html.
Full textDarling, Nicola Jane. "Regulation of ER stress-induced cell death by the ERK1/2 signalling pathway." Thesis, University of Cambridge, 2015. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.708709.
Full textSarkar, Deboleena Dipak. "Potential Role Of Endoplasmic Reticulum Redox Changes In Endoplasmic Reticulum Stress And Impaired Protein Folding In Obesity-Associated Insulin Resistance." Diss., The University of Arizona, 2013. http://hdl.handle.net/10150/306999.
Full textChan, Cheuk-wing Wilson. "ER stress in the pathogenesis of osteochondrodysplasia." Click to view the E-thesis via HKUTO, 2009. http://sunzi.lib.hku.hk/hkuto/record/B43085192.
Full textPreston, Amanda Miriam Clinical School St Vincent's Hospital Faculty of Medicine UNSW. "The role of endoplasmic reticulum stress in beta-cell lipoapoptosis." Publisher:University of New South Wales. Clinical School - St Vincent's Hospital, 2008. http://handle.unsw.edu.au/1959.4/41231.
Full textKatsoulieris, Elias. "Oxidatives and Endoplasmic Reticulum Stress in Kidney Priximal Tubule Cells." Thesis, University of Brighton, 2009. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.506517.
Full textNiederreiter, Lukas. "Endoplasmic reticulum (ER) stress transcription factor Xbp1 in intestinal tumourigenesis." Thesis, University of Cambridge, 2015. https://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.708846.
Full textGaifem, Joana Filipa Madureira. "" Role Of In Endoplasmic Reticulum Stress Response In Sacccharoromyces cerevisiae "." Master's thesis, Instituto de Ciências Biomédicas Abel Salazar, 2011. http://hdl.handle.net/10216/56926.
Full textBonilla, Myriam. "Endoplasmic reticulum stress linked to calcium signaling in saccharomyces cerevisiae." Available to US Hopkins community, 2003. http://wwwlib.umi.com/dissertations/dlnow/3080627.
Full textDas, Indrajit. "Therapeutic Targeting of Endoplasmic Reticulum Stress in Inflammatory Bowel Disease." Thesis, Griffith University, 2012. http://hdl.handle.net/10072/365999.
Full textThesis (PhD Doctorate)
Doctor of Philosophy (PhD)
School of Biomolecular and Physical Sciences
Science, Environment, Engineering and Technology
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Gendrisch, Fabian [Verfasser], and Stefan F. [Akademischer Betreuer] Martin. "The role of endoplasmic reticulum stress responses in contact dermatitis." Freiburg : Universität, 2018. http://d-nb.info/1211956318/34.
Full textMartin, Rachel E. "Targeted sensors to monitor oxidative stress in the endoplasmic reticulum." Thesis, University of Glasgow, 2014. http://theses.gla.ac.uk/5884/.
Full textGaifem, Joana Filipa Madureira. "" Role Of In Endoplasmic Reticulum Stress Response In Sacccharoromyces cerevisiae "." Dissertação, Instituto de Ciências Biomédicas Abel Salazar, 2011. http://hdl.handle.net/10216/56926.
Full textWang, Yongchao. "THE ROLE OF ENDOPLASMIC RETICULUM STRESS IN ETHANOL-INDUCED NEURODEGENERATION." UKnowledge, 2019. https://uknowledge.uky.edu/pharmacol_etds/33.
Full textMihai, Adina Daniela. "Obesity-related factors involved in endoplasmic reticulum stress induction in adipocytes." Thesis, Durham University, 2015. http://etheses.dur.ac.uk/11637/.
Full textPark, Soon Hyang. "The role of endoplasmic reticulum stress signaling in isolated islet apoptosis." Thesis, McGill University, 2009. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=32257.
Full textUn obstacle majeur lors de la transplantation des îlots pancréatiques est la perte des cellules β lors de la procédure d'isolation. En effet, lors de ce processus, les îlots sont exposés à divers stress cellulaires incluant ceux qui induisent un stress au niveau du réticulum endoplasmique (RE). Cette étude porte donc sur la signalisation menant à l'apoptose en réponse au stress du RE sur les îlots isolés. L'activation d'eIF2α, de JNK1 et de l'épissage de XBP1 qui est suivi par une augmentation de l'activité de la caspase-3 fut observées sur des îlots isolés chez l'humain. L'absence de la protéine tyrosine phosphatase 1B (PTP1B) avait précédemment été démontrée comme pouvant contribuer à la diminution de la signalisation déclenchée par le stress du RE et l'apoptose chez les fibroblastes. Malgré des résultats encourageants concernant l'utilisation d'un inhibiteur et d'un miRNA qui ciblent PTP1B, un lien concluant entre l'inhibition de cette enzyme et l'amélioration de la survie des cellules β n'a pas été observé Cette étude fournit la première évidence qui clarifie le rôle de la signalisation induite par le stress du RE lors de l'apoptose des îlots pancréatiques. De plus, elle pourrait résulter en une nouvelle approche thérapeutique pour augmenter la survie des cellules β lors de la transplantation d'îlots.
Hühn, Martin [Verfasser]. "Endoplasmic Reticulum (ER)-stress signalling in the alveolar epithelium / Martin Hühn." Gießen : Universitätsbibliothek, 2013. http://d-nb.info/1065395310/34.
Full textMahmood, Ahsan. "Role of SLMAP in Endoplasmic Reticulum Stress and Unfolded Protein Response." Thèse, Université d'Ottawa / University of Ottawa, 2013. http://hdl.handle.net/10393/24399.
Full textNakano, Kenzo. "Chloroquine induces apoptosis in pancreatic neuroendocrine neoplasms via endoplasmic reticulum stress." Doctoral thesis, Kyoto University, 2021. http://hdl.handle.net/2433/263541.
Full textBrown, Max Adam. "Investigation of how endoplasmic reticulum stress causes insulin resistance and neuroinflammation." Thesis, Durham University, 2015. http://etheses.dur.ac.uk/11438/.
Full textFonseca, Sonya G. "Role of WFS1 in Regulating Endoplasmic Reticulum Stress Signaling: A Dissertation." eScholarship@UMMS, 2009. https://escholarship.umassmed.edu/gsbs_diss/414.
Full textShank, Karin Janel. "Coordination of the endoplasmic reticulum stress response and lipid metabolism in plants." NCSU, 2000. http://www.lib.ncsu.edu/theses/available/etd-20000729-161702.
Full textThe endoplasmic reticulum (ER) stress response is an important signal transduction pathway that senses ER stress caused by misfolded proteins or increased secretory protein traffic and induces molecular chaperone expression to counter such stress. The response has been well characterized in yeast and mammals where it has been associated with a variety of metabolic pathways, such as phospholipid biosynthesis, translational inhibition, and ER associated degradation. In plants, however, the connections of the ER stress response with metabolic pathways other than those involved in chaperone biosynthesis have not been characterized. This study defines a connection between phospholipid synthesis and the ER stress response in plants. Two model systems were used to characterize this association, the maize mutant floury-2 (fl2), which displays a unique endosperm specific ER stress response mediated by a mutant seed storage protein, and soybean cell cultures treated with the pharmacological agents tunicamycin (Tm) or azetidine-2-carboxylic acid (AZC). These chemicals interfere with normal protein synthesis and processing events, and are well characterized inducers of ER stress responses in animals, plants, and yeast. Investigation of both of these systems revealed a common theme; induction of the ER stress response in plants leads to increased activity and/or expression of various phospholipid biosynthetic enzymes. These increases were correlated with previously described amplifications in expression of the molecular chaperones binding protein (BiP), protein disulfide isomerase (PDI) and calreticulin. Certain aspects of the ER stress response may be unique to plants. A seed-specific result of the ER stress response was the accumulation of triacylglycerols (TG), which specifically increased in the endosperm of the fl2 mutant to more than 3-fold higher than normal endosperm levels by 36 days after pollination (DAP). The maize and soybean systems used in this study provide a starting point for the investigation of other details of the ER stress response in plants and represent important tools for future efforts to define the components of the signaling pathway.
Misiewicz, Michael. "Identification of a novel endoplasmic reticulum stress response element regulated by XBP1." Thesis, McGill University, 2013. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=116963.
Full textLa protéine Prion (PrP), qui est l'agent infectieux causant les encéphalopathies transmissibles, n'a pas toujours un rôle bien identifié dans la cellule, malgré 30 ans de recherche sur sa fonction physiologique. Cependant, de plus en plus de preuves commencent à impliquer PrP dans des fonctions de protection dans la cellule. Dans cette étude, nous avons étudié la régulation peu connue du promoteur du gène qui encode PrP (PRNP). Par homologie de séquence, nous avons identifié un nouvel élément dans le promoteur de PRNP qui ressemble à l'Endoplasmic Reticulum Stress Response Element (ERSE). Ce nouvel ERSE (appelé ERSE-26) est capable de réguler l'expression du PRNP de manière endogène en réponse au stress dans le réticulum endoplasmique (RE). Pour savoir si l'ERSE-26 existe ailleurs dans le génome et afin de trouver d'autres gènes régulé avec PRNP, nous avons fait une recherche bioinformatique dans le génome entier. Nous avons identifié 38 gènes contenant aussi un ERSE-26 dans leur promoteur. Afin de confirmer l'expression de ces gènes en réponse au stress ER, nous avons traité des cultures de neurones primaires humains et des cellules MCF-7 avec les activateurs du stress RE Brefeldin A, Tunicamycin et Thapsigargin, puis vérifié l'expression par Transcriptase Inverse PCR (RT-PCR) ou RT-PCR quantitative. Nous avons montré l'induction des gènes GADD45B, SESN2 et PRNP, et d'autres ont montré une tendance positive. Ensuite, un plasmide rapporteur luciferase contenant l'ERSE-26 seulement a été utilisé pour montrer que le facteur de transcription du stress ER XBP1 est un facteur de transcription responsable pour l'activité de l'ERSE-26. Finalement, nous avons fait une recherche dans la littérature afin de déterminer la fonction des gènes contenant ERSE-26. Les gènes répondant au stress oxydant et les gènes pro-survie étaient parmi les gènes ERSE-26, et aussi ont été le plus induits, soutenant le rôle protecteur du PrP dans la cellule.
Lari, Federica. "Resolution of proteotoxic stress in the endoplasmic reticulum by ubiquitin ligase complexes." Thesis, University of Oxford, 2016. https://ora.ox.ac.uk/objects/uuid:871e0484-3de4-4d0d-8206-4af16a8b743e.
Full textLevet, Clémence. "Mild Endoplasmic Reticulum Stress Protects From Cell Death : The Role Of Autophagy." Thesis, Lyon 1, 2012. http://www.theses.fr/2012LYO10209.
Full textThe last years have been very successful in identifying mechanisms, which control apoptosis in metazoan. However, the regulation of cell death in specific cell type remains to be determined. An excess of neuron apoptosis can lead to neurodegenerative diseases such as Huntington, Parkinson or Alzheimer diseases. Neurodegeneration is usually associated to Endoplasmic Reticulum stress (ER stress), autophagy or oxidative stress. However, the role of these mechanisms in the regulation of neurodegeneration is not clearly established. To test the role of ER stress in the regulation of neuronal death, we used several models of neurodegeneration in Drosophila and mammals. First, we have shown that the genetic induction of ER stress protected photoreceptors of the Drosophila eye from apoptosis. Then, we have shown that the protective effect of ER stress is conserved in both Drosophila and mouse models of Parkinson disease. In order to characterize the protective effect of ER stress, we have studied the activation of protective mechanisms upon ER stress. We have shown that in the Drosophila retina, ER stress can induce an anti-oxidative response and autophagy. Interestingly, autophagy is only activated in presence of both ER stress and cell death signal. We have focused on the role of autophagy in the protective effect of ER stress. We have shown that the activation of autophagy was required for the protective effect of ER stress. Thus, we have shown that ER stress response is not only involved in the reduction of misfolded protein accumulation, but can also protect neurons form cell death by activating autophagy
Page, Lindsay N. "Endoplasmic Reticulum Stress Contributes to Cyclosporine A-Induced Lens Epithelial Cell Loss." The Ohio State University, 2020. http://rave.ohiolink.edu/etdc/view?acc_num=osu1585948655611948.
Full textBicknell, Alicia Anne. "Two MAP kinases regulate novel aspects of the endoplasmic reticulum stress response." Diss., [La Jolla] : University of California, San Diego, 2009. http://wwwlib.umi.com/cr/ucsd/fullcit?p3369545.
Full textTitle from first page of PDF file (viewed September 14, 2009). Available via ProQuest Digital Dissertations. Vita. Includes bibliographical references (p. 160-185).
Pino, Steven C. "Role of Endoplasmic Reticulum Stress Response Signaling in T Cells: A Dissertation." eScholarship@UMMS, 2008. https://escholarship.umassmed.edu/gsbs_diss/381.
Full textThomas, Sally Edwina. "The role of cell cycle checkpoints in the survival of endoplasmic reticulum stress." Thesis, University of Cambridge, 2013. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.608043.
Full textTan, Zhijia, and 谭志佳. "Molecular analyses of chondrocyte differentiation and adaptation to ER stress." Thesis, The University of Hong Kong (Pokfulam, Hong Kong), 2013. http://hdl.handle.net/10722/209435.
Full textpublished_or_final_version
Biochemistry
Doctoral
Doctor of Philosophy
Gwiazda, Kamila Sabina. "Role of endoplasmic reticulum calcium stores in beta-cell ER stress and lipotoxicity." Thesis, University of British Columbia, 2009. http://hdl.handle.net/2429/12553.
Full textTillman, Erik J. (Erik James). "Genetic analysis of endoplasmic reticulum homeostasis during stress and infection of Caenorhabditis elegans." Thesis, Massachusetts Institute of Technology, 2018. http://hdl.handle.net/1721.1/119917.
Full textThis electronic version was submitted by the student author. The certified thesis is available in the Institute Archives and Special Collections.
Cataloged from student-submitted PDF version of thesis.
Includes bibliographical references.
Animals experience intrinsic and extrinsic stressors throughout development and adulthood. To maintain cellular and organismal homeostasis, eukaryota and metazoa rely on conserved, integrated stress response pathways. Throughout its life cycle, the free-living nematode Caenorhabditis elegans encounters diverse microbial taxa, including both nutritional and pathogenic species. Intestinal infection with the pathogenic bacteria Pseudomonas aeruginosa induces a transcriptional innate immune response leading to the secretion of immune effector molecules into the intestinal lumen. Previous work has demonstrated a critical role for the endoplasmic reticulum unfolded protein response in surviving immune activation during larval development. Specifically, the most ancient IRE-1/XBP-1 branch of the UPR is required for larval development during immune activation, whether or not pathogen is present. To understand additional mechanisms regulating ER homeostasis in C. elegans, we conducted a forward genetic screen and identified suppressors of xbp-1 mutant larval lethality on P. aeruginosa. In this work, I outline the characterization of several identified mutations that each affect a gene encoding a broadly conserved transcriptional regulator. A mutation in the gene encoding the forkhead DNA binding domain-containing transcription factor FKH-9 enhances ER homeostasis outside the context of infection and immune activation, but paradoxically sensitizes animals to perturbations in cytosolic proteostasis. My results suggest that loss of fkh-9 enhances translocation of misfolded proteins out of the ER, thereby disrupting cytosolic proteostasis and decreasing proteasomal function. These findings implicate a critical need for balancing proteostasis across cellular compartments during organismal stress, and further investigation of the additional characterized mutants will elucidate the breadth of this phenomenon.
by Erik J. Tillman.
Ph. D.
Nugent, Ashleigh Elizabeth. "The Presence of Extracellular Matrix Alters the Chondrocyte Response to Endoplasmic Reticulum Stress." Kent State University / OhioLINK, 2010. http://rave.ohiolink.edu/etdc/view?acc_num=kent1271375344.
Full textMlynarczyk, Coraline. "Regulation of p21CDKN1A in the endoplasmic reticulum stress response : mechanism, function and implications." Paris 7, 2013. http://www.theses.fr/2013PA077128.
Full textStress to the endoplasmic reticulum (ER) occurs during nutrient or oxygen limitation as can be found in solid tumors and is characterized by an accumulation of misfolded proteins in the ER lumen. We have previously shown that the resulting unfolded protein response (UPR) induces the p53 isoform p53/47 and a subsequent 14-3-3 sigma-mediated G2 arrest that helps to restore ER homeostasis. This contrasts with the p21coKNiA-dependent Gl arrest caused by p53 following DNA damage. A large proportion of anticancer therapies are based on genotoxic agents and we sought to determine how ER stress affects the p53-mediated response to DNA damage. It appeared that the UPR down regulates expression of p21 in a p53-dependent manner and prevents p21 induction by DNA damage, resulting in increased apoptosis. P53/47 impedes p21 promoter transactivation by p53 and the coordinated activity of both isoforms represses de novo p21 protein synthesis, via codons 76 to 164 of the p21 mRNA. It is further demonstrated that p21, if not suppressed, prevents ER stress-induced G2 arrest via directing 14-3-3 sigma degradation by the E3 ubiquitin ligase COP1. Therefore, this work i) illustrates how p53 controls an intrinsic balance between the Gl and G2 checkpoints in response to different stress signals; ii) uncovers a novel level at which p53 can regulate expression of its target genes; iii) reveals a pro-proliferative role for p21, whose suppression is essential during ER stress and iv) identifies conditions displayed by solid tumor cells that may be used to potentiate the cytotoxicity of existing anticancer drugs
Zha, Beth Shoshana. "HIV Protease Inhibitors Trigger Lipid Metabolism Dysregulation Through Endoplasmic Reticulum Stress and Autophagy." VCU Scholars Compass, 2011. http://scholarscompass.vcu.edu/etd/273.
Full textEgawa, Naohiro. "The endoplasmic reticulum stress sensor, ATF6α, protects against neurotoxin-induced dopaminergic neuronal death." Kyoto University, 2011. http://hdl.handle.net/2433/142092.
Full textLipson, Kathryn L. "The Role of Endoplasmic Reticulum Stress Signaling in Pancreatic Beta Cells: a Dissertation." eScholarship@UMMS, 2008. https://escholarship.umassmed.edu/gsbs_diss/363.
Full textHerrenbruck, Adrienne Rose. "EFFECTS OF HIGH FAT EXPOSURE ON SKELETAL MUSCLE AUTOPHAGY AND ENDOPLASMIC RETICULUM STRESS." UKnowledge, 2018. https://uknowledge.uky.edu/khp_etds/53.
Full textPirot, Pierre. "Identification and characterization of the endoplasmic reticulum (ER)-stress pathways in pancreatic beta-cells." Doctoral thesis, Universite Libre de Bruxelles, 2007. http://hdl.handle.net/2013/ULB-DIPOT:oai:dipot.ulb.ac.be:2013/210623.
Full textAccumulating evidence suggest that ER stress contributes to beta-cell apoptosis in both type 1 and type 2 diabetes. Type 1 diabetes is characterized by a severe insulin deficiency resulting from chronic and progressive destruction of pancreatic beta-cells by the immune system. During this autoimmune assault, beta-cells are exposed to cytokines secreted by the immune cells infiltrating the pancreatic islets. Our group has previously shown that the pro-inflamatory cytokines interleukin-1beta (IL1-beta and interferon-gamma (IFN-gamma), via nitric oxide (NO) formation, downregulate expression and function of the ER Ca2+ pump SERCA2. This depletes beta-cell ER Ca2+ stores, leading to ER stress and apoptosis. Of note, IL1-beta alone triggers ER stress but does not induce beta-cell death, while IFN-gamma neither causes ER stress nor induces beta-cell death. Together, these cytokines cause beta-cell apoptosis but the mechanisms behind this synergistic effect were unknown.
Type 2 diabetes is characterized by both peripheral resistance to insulin, usually as a result of obesity, and deficient insulin secretion secondary to beta cell failure. Obese patients have high levels of circulating free fatty acids (FFA) and several studies have shown that the FFA palmitate induces ER stress and beta-cell apoptosis.
In the present work we initially established an experimental model to specifically activate the ER stress response in pancreatic beta-cells. For this purpose, insulinoma cells (INS-1E) or primary rat beta-cells were exposed to the reversible chemical SERCA pump blocker cyclopiazonic acid (CPA). Dose-response and time course experiments determined the best conditions to induce a marked ER stress without excessive cell death (<25%).
The first goal of the work was to understand the synergistic effects of IL1-beta and IFN-gamma leading to pancreatic beta-cell apoptosis. Our group previously observed, by microarray analysis of primary beta-cells, that IFN-gamma down-regulates mRNAs encoding for some ER chaperones. Against this background, our hypothesis was that IFN-gamma aggravates beta-cell ER stress by decreasing the ability of these cells to mount an adequate UPR. To test this hypothesis, we investigated whether IFN-gamma pre-treatment augments CPA-induced ER stress and beta cell death. The results obtained indicated that IFN-gamma pre-treatment potentiates CPA-induced apoptosis in INS-1E and primary beta-cells. This effect was specific for IFN-gamma since neither IL1-beta nor a low dose CPA pre-treatment potentiated CPA-induced apoptosis in INS-1E cells. These effects of IFN-gamma were mediated via the down regulation of genes involved in beta cell defense against ER stress, including the ER chaperones BiP, Orp150 and Grp94 as well as Sec61, a component of the ERAD pathway. This had functional consequences as evidenced by a decreased basal and CPA-induced activity of a reporter construct for the unfolded protein response element (UPRE) and augmented expression of the pro-apoptotic transcription factor Chop.
We next investigated the molecular regulation of the Chop gene in INS-1E cells in response to several pro-apoptotic and ER stress inducing agents, namely cytokines (IL1-beta and IFN-gamma), palmitate, or CPA. Detailed mutagenesis studies of the Chop promoter showed differential regulation of Chop transcription by these compounds. While cytokines (via NO production)- and palmitate-induced Chop expression was mediated via a C/EBP-ATF composite and AP-1 binding sites, CPA induction required the C/EBP-ATF site and the ER stress response element (ERSE). Cytokines, palmitate and CPA induced ATF4 protein expression and further binding to the C/EBP-ATF composite site, as shown by Western blot and EMSA experiments. There was also formation of distinct AP-1 dimers and binding to the AP-1 site after exposure to cytokines or palmitate.
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Doctorat en Sciences biomédicales et pharmaceutiques
info:eu-repo/semantics/nonPublished
Al-Sheikh, Hashem M. "Transcriptional regulation of the glucoamylase-encoding gene under endoplasmic reticulum stress in Aspergillus niger." Thesis, University of Nottingham, 2005. http://eprints.nottingham.ac.uk/13097/.
Full textCarne, Naomi Angharad. "The effect of endoplasmic reticulum and reductive stress on the human dermal fibroblast proteome." Thesis, Durham University, 2018. http://etheses.dur.ac.uk/12794/.
Full textCoelho, Dina Raquel da Silva. "The Role of the Endoplasmic Reticulum Stress Transducer Ire1 during Photoreceptor Differentiation in Drosophila." Doctoral thesis, Universidade Nova de Lisboa. Instituto de Tecnologia Química e Biológica, 2013. http://hdl.handle.net/10362/12071.
Full textThe accumulation of misfolded proteins in the lumen of the endoplasmic reticulum (ER) causes ER stress and activates a homeostatic mechanism termed the Unfolded Protein Response (UPR). The most conserved arm of the UPR is mediated by the ER transmembrane protein Ire1 that removes an unconventional intron from Xbp1 mRNA upon ER stress. Xbp1spliced is an effective transcription factor that up-regulates ER chaperones and enzymes.(...)
Hata, Masayuki. "KUS121, a VCP modulator, attenuates ischemic retinal cell death via suppressing endoplasmic reticulum stress." Kyoto University, 2018. http://hdl.handle.net/2433/232075.
Full textLi, Yi. "Mechanisms of Transcriptional Regulation of Cat-1 Gene Expression by Endoplasmic Reticulum (ER) Stress." Case Western Reserve University School of Graduate Studies / OhioLINK, 2009. http://rave.ohiolink.edu/etdc/view?acc_num=case1238790728.
Full textDuRose, Jenny Bratlien. "The unfolded protein response integrating stress signals from the endoplasmic reticulum to the nucleolus /." Diss., Connect to a 24 p. preview or request complete full text in PDF format. Access restricted to UC campuses, 2008. http://wwwlib.umi.com/cr/ucsd/fullcit?p3330123.
Full textTitle from first page of PDF file (viewed November 13, 2008). Available via ProQuest Digital Dissertations. Vita. Includes bibliographical references.
López, Ignacio. "P53-mediated control of mRNA translation during Endoplasmic Reticulum stress : mechanisms and physiological implications." Thesis, Sorbonne Paris Cité, 2016. http://www.theses.fr/2016USPCC220/document.
Full textPhysiological fluctuations of protein production/folding and pathological processes like viralinfection, aging and cancers can lead to Endoplasmic Reticulum (ER) stress. It is a statecharacterized by the accumulation of unfolded or misfolded proteins in the ER lumen that triggers the Unfolded Protein Response. In restoring ER proteostasis, the UPR inhibits global capdependent protein synthesis and promotes proteases and ER chaperons, notably BiP, which also functions as the main UPR sensor. Our group has previously shown that during ER stress, a selective induction of the p53 tumour suppressor protein isoform p53ΔN40 (also known as p53/47, Δ40p53, ΔNp53, p47) by PERK leads to G2 arrest, and that this depends on a suppression of p21CDKN1A expression by p53 full-length (p53FL) and p53ΔN40 acting at transcription and translation. The main topic of my work has been to understand how p53 promotes apoptosis during prolonged ER stress. I could show that this depends on the down regulation of BiP expression via a direct interaction between a restricted region of the bip mRNA's coding sequence and p53 protein. The trans-suppression is mediated by a 7-aa domain of the p53 protein present in both p53FL and p53ΔN40. The inhibition of BiP expression during ER stress leads to an increase in apoptosis via activation of the BH3-only BIK protein by liberating it from a repressive interaction with BiP. Moreover, BIK is further activated during ER stress by transcription induction mediated by p53FL and/or p53ΔN40. These results links for the first time the RNA-binding capacity of p53 and the control of mRNA translation with a particular cellular response. The work also shows that p53 controls the translation of two additional mRNAs in what appears to be two different mechanisms. Both mechanisms rely on sequences present in the mRNAs but differ in the requirement of a direct interaction with the p53 protein. Like with BiP, the RNA-binding capacity of p53 shuts down the translation of fgf-2 and p53 mRNAs. To this category we can now also include the mdmx mRNA. On the other hand, suppression of p21CDKN1A translation was not shown to require an interaction with p53 and this is also the case for suppression of MDM2. The physiological implications of MDMX and MDM2 suppression are discussed. These data illustrate that p53-mediated mRNA translation suppression plays a physiological role during the UPR and further supports the specific role of the p53ΔN40 during ER stress
Yang, Ling. "Bcl-2-associated athanogene-1 (BAG-1) Modulates the Endoplasmic Reticulum Stress Response in Chondrocytes." Kent State University / OhioLINK, 2007. http://rave.ohiolink.edu/etdc/view?acc_num=kent1175103480.
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