Journal articles: 'ER stress'

1

Jaenicke, Lothar. "ER-Stress." Chemie in unserer Zeit 40, no. 3 (June 2006): 161. http://dx.doi.org/10.1002/ciuz.200690036.

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Zito, Ester. "Targeting ER stress/ER stress response in myopathies." Redox Biology 26 (September 2019): 101232. http://dx.doi.org/10.1016/j.redox.2019.101232.

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Kumar, Vaishali, and Shuvadeep Maity. "ER Stress-Sensor Proteins and ER-Mitochondrial Crosstalk—Signaling Beyond (ER) Stress Response." Biomolecules 11, no. 2 (January 28, 2021): 173. http://dx.doi.org/10.3390/biom11020173.

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Recent studies undoubtedly show the importance of inter organellar connections to maintain cellular homeostasis. In normal physiological conditions or in the presence of cellular and environmental stress, each organelle responds alone or in coordination to maintain cellular function. The Endoplasmic reticulum (ER) and mitochondria are two important organelles with very specialized structural and functional properties. These two organelles are physically connected through very specialized proteins in the region called the mitochondria-associated ER membrane (MAM). The molecular foundation of this relationship is complex and involves not only ion homeostasis through the shuttling of calcium but also many structural and apoptotic proteins. IRE1alpha and PERK are known for their canonical function as an ER stress sensor controlling unfolded protein response during ER stress. The presence of these transmembrane proteins at the MAM indicates its potential involvement in other biological functions beyond ER stress signaling. Many recent studies have now focused on the non-canonical function of these sensors. In this review, we will focus on ER mitochondrial interdependence with special emphasis on the non-canonical role of ER stress sensors beyond ER stress.

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4

Kawaguchi, S., and D. T. W. Ng. "Sensing ER Stress." Science 333, no. 6051 (September 29, 2011): 1830–31. http://dx.doi.org/10.1126/science.1212840.

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Gough, N. R. "Neuronal ER Stress." Science Signaling 3, no. 152 (December 14, 2010): ec378-ec378. http://dx.doi.org/10.1126/scisignal.3152ec378.

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Vincenz, Lisa, and F. Ulrich Hartl. "Sugarcoating ER Stress." Cell 156, no. 6 (March 2014): 1125–27. http://dx.doi.org/10.1016/j.cell.2014.02.035.

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Mateus, Duarte, Elettra Sara Marini, Cinzia Progida, and Oddmund Bakke. "Rab7a modulates ER stress and ER morphology." Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 1865, no. 5 (May 2018): 781–93. http://dx.doi.org/10.1016/j.bbamcr.2018.02.011.

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8

Gorman, Adrienne M., Sandra J. M. Healy, Richard Jäger, and Afshin Samali. "Stress management at the ER: Regulators of ER stress-induced apoptosis." Pharmacology & Therapeutics 134, no. 3 (June 2012): 306–16. http://dx.doi.org/10.1016/j.pharmthera.2012.02.003.

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9

Begum, Gulnaz, Lloyd Harvey, C. Edward Dixon, and Dandan Sun. "ER Stress and Effects of DHA as an ER Stress Inhibitor." Translational Stroke Research 4, no. 6 (August 20, 2013): 635–42. http://dx.doi.org/10.1007/s12975-013-0282-1.

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10

Lee, Amy S., and Linda M. Hendershot. "ER stress and cancer." Cancer Biology & Therapy 5, no. 7 (July 2006): 721–22. http://dx.doi.org/10.4161/cbt.5.7.3120.

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11

Lee, W., W. Yoo, and H. Chae. "ER Stress and Autophagy." Current Molecular Medicine 15, no. 8 (October 6, 2015): 735–45. http://dx.doi.org/10.2174/1566524015666150921105453.

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12

Koo, Seung-Hoi. "Obesity and ER Stress." Korean Journal of Obesity 20, no. 2 (2011): 45. http://dx.doi.org/10.7570/kjo.2011.20.2.45.

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13

Shi, Qi, and Xiao-Ping Dong. "CtmPrP and ER stress." Prion 5, no. 3 (July 2011): 123–25. http://dx.doi.org/10.4161/pri.5.3.16327.

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14

Zlotorynski, Eytan. "DR5 unfolds ER stress." Nature Reviews Molecular Cell Biology 15, no. 8 (July 16, 2014): 499. http://dx.doi.org/10.1038/nrm3843.

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15

Yoshida, Hiderou. "ER stress and diseases." FEBS Journal 274, no. 3 (January 8, 2007): 630–58. http://dx.doi.org/10.1111/j.1742-4658.2007.05639.x.

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16

LeBrasseur, Nicole. "ER stress shapes muscle." Journal of Cell Biology 169, no. 4 (May 16, 2005): 548. http://dx.doi.org/10.1083/jcb1694iti2.

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17

Riddihough, G. "Stress Testing the ER." Science 326, no. 5958 (December 3, 2009): 1323. http://dx.doi.org/10.1126/science.326.5958.1323-c.

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18

Ray, B. "STKE: Tolerating ER Stress." Science 306, no. 5698 (November 5, 2004): 945c. http://dx.doi.org/10.1126/science.306.5698.945c.

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19

Binet, François, and Przemyslaw Sapieha. "ER Stress and Angiogenesis." Cell Metabolism 22, no. 4 (October 2015): 560–75. http://dx.doi.org/10.1016/j.cmet.2015.07.010.

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20

Strzyz, Paulina. "ER stress boosts respiration." Nature Reviews Molecular Cell Biology 20, no. 8 (May 3, 2019): 453. http://dx.doi.org/10.1038/s41580-019-0139-x.

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21

Collison, Joanna. "ER stress causes osteoclastogenesis." Nature Reviews Rheumatology 14, no. 4 (February 15, 2018): 184. http://dx.doi.org/10.1038/nrrheum.2018.24.

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22

Hara, Takashi, and Fumihiko Urano. "ER stress and β cell death — therapeutic approach to combat ER stress." Folia Pharmacologica Japonica 144, no. 2 (2014): 53–58. http://dx.doi.org/10.1254/fpj.144.53.

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23

Miglioranza Scavuzzi, Bruna, and Joseph Holoshitz. "Endoplasmic Reticulum Stress, Oxidative Stress, and Rheumatic Diseases." Antioxidants 11, no. 7 (June 29, 2022): 1306. http://dx.doi.org/10.3390/antiox11071306.

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Background: The endoplasmic reticulum (ER) is a multi-functional organelle responsible for cellular homeostasis, protein synthesis, folding and secretion. It has been increasingly recognized that the loss of ER homeostasis plays a central role in the development of autoimmune inflammatory disorders, such as rheumatic diseases. Purpose/Main contents: Here, we review current knowledge of the contribution of ER stress to the pathogenesis of rheumatic diseases, with a focus on rheumatoid arthritis (RA) and systemic lupus erythematosus (SLE). We also review the interplay between protein folding and formation of reactive oxygen species (ROS), where ER stress induces oxidative stress (OS), which further aggravates the accumulation of misfolded proteins and oxidation, in a vicious cycle. Intervention studies targeting ER stress and oxidative stress in the context of rheumatic diseases are also reviewed. Conclusions: Loss of ER homeostasis is a significant factor in the pathogeneses of RA and SLE. Targeting ER stress, unfolded protein response (UPR) pathways and oxidative stress in these diseases both in vitro and in animal models have shown promising results and deserve further investigation.

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24

Xiao, Ting, Xiuci Liang, Hailan Liu, Feng Zhang, Wen Meng, and Fang Hu. "Mitochondrial stress protein HSP60 regulates ER stress-induced hepatic lipogenesis." Journal of Molecular Endocrinology 64, no. 2 (February 2020): 67–75. http://dx.doi.org/10.1530/jme-19-0207.

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Endoplasmic reticulum (ER) stress and mitochondrial dysfunction are associated with hepatic steatosis and insulin resistance. Molecular mechanisms underlying ER stress and/or mitochondrial dysfunction that cause metabolic disorders and hepatic steatosis remain to be fully understood. Here, we found that a high fat diet (HFD) or chemically induced ER stress can stimulate mitochondrial stress protein HSP60 expression, impair mitochondrial respiration, and decrease mitochondrial membrane potential in mouse hepatocytes. HSP60 overexpression promotes ER stress and hepatic lipogenic protein expression and impairs insulin signaling in mouse hepatocytes. Mechanistically, HSP60 regulates ER stress-induced hepatic lipogenesis via the mTORC1-SREBP1 signaling pathway. These results suggest that HSP60 is an important ER and mitochondrial stress cross-talking protein and may control ER stress-induced hepatic lipogenesis and insulin resistance.

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25

YOSHIUCHI, Kazutomi, Hideaki KANETO, Taka-aki MATSUOKA, Ryuichi KASAMI, Kenji KOHNO, Takao IWAWAKI, Yoshihisa NAKATANI, Yoshimitsu YAMASAKI, Iichiro SHIMOMURA, and Munehide MATSUHISA. "Pioglitazone Reduces ER Stress in the Liver: Direct Monitoring of in vivo ER Stress Using ER Stress-activated Indicator Transgenic Mice." Endocrine Journal 56, no. 9 (2009): 1103–11. http://dx.doi.org/10.1507/endocrj.k09e-140.

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26

Piña, Francisco Javier, Tinya Fleming, Kit Pogliano, and Maho Niwa. "Reticulons Regulate the ER Inheritance Block during ER Stress." Developmental Cell 37, no. 3 (May 2016): 279–88. http://dx.doi.org/10.1016/j.devcel.2016.03.025.

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27

Steenberg, Dorte, and Dorte Steenberg. "Stress-et fælles ansvar." Tidsskrift for Arbejdsliv 9, no. 2 (June 1, 2007): 86. http://dx.doi.org/10.7146/tfa.v9i2.108613.

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S tress er et samfundsmæssigt problem, og det er et anliggende for arbejdspladsen. Men først og fremmest er der for det menneske, der rammes, tale om en alvorlig situation, der kan betyde sygdom og i værste fald få livsvarige konsekvenser. Sat på spidsen kan man sige, at der er tale om et forbrug af mennesker på arbejdsmarkedet og et spild af mennesker, der er helt uacceptabel. Med andre ord: der må gøres noget.

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28

Ong, Gideon, and Susan E. Logue. "Unfolding the Interactions between Endoplasmic Reticulum Stress and Oxidative Stress." Antioxidants 12, no. 5 (April 22, 2023): 981. http://dx.doi.org/10.3390/antiox12050981.

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Oxidative stress is caused by an imbalance in cellular redox state due to the accumulation of reactive oxygen species (ROS). While homeostatic levels of ROS are important for cell physiology and signaling, excess ROS can induce a variety of negative effects ranging from damage to biological macromolecules to cell death. Additionally, oxidative stress can disrupt the function of redox-sensitive organelles including the mitochondria and endoplasmic reticulum (ER). In the case of the ER, the accumulation of misfolded proteins can arise due to oxidative stress, leading to the onset of ER stress. To combat ER stress, cells initiate a highly conserved stress response called the unfolded protein response (UPR). While UPR signaling, within the context of resolving ER stress, is well characterised, how UPR mediators respond to and influence oxidative stress is less defined. In this review, we evaluate the interplay between oxidative stress, ER stress and UPR signaling networks. Specifically, we assess how UPR signaling mediators can influence antioxidant responses.

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29

Ishiwata-Kimata, Yuki, Giang Quynh Le, and Yukio Kimata. "Stress-sensing and regulatory mechanism of the endoplasmic-stress sensors Ire1 and PERK." Endoplasmic Reticulum Stress in Diseases 5, no. 1 (October 1, 2018): 1–10. http://dx.doi.org/10.1515/ersc-2018-0001.

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Abstract Ire1 and its family protein PERK are endoplasmic reticulum (ER)-stress sensors that initiate cellular responses against ER accumulation of unfolded proteins. As reviewed in this article, many publications describe molecular mechanisms by which yeast Ire1 senses ER conditions and gets regulated. We also cover recent studies which reveal that mammalian Ire1 (IRE1α) and PERK are controlled in a similar but not exactly the same manner. ER-located molecular chaperone BiP captures these ER-stress sensors and suppresses their activity. Intriguingly, Ire1 is associated with BiP not as a chaperone substrate, but as a unique ligand. Unfolded proteins accumulated in the ER promote dissociation of the Ire1-BiP complex. Moreover, Ire1 is directly bound with unfolded proteins, leading to its cluster formation and potent activation. PERK also captures unfolded proteins and then forms self-oligomers. Meanwhile, membrane-lipid aberrancy is likely to activate these ER-stress sensors independently of ER accumulation of unfolded proteins. In addition, there exist a number of reports that touch on other factors that control activity of these ER-stress sensors. Such a multiplicity of regulatory mechanisms for these ER-stress sensors is likely to contribute to fine tuning of their activity.

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30

Wallington-Beddoe, Craig T., and Stuart M. Pitson. "Enhancing ER stress in myeloma." Aging 9, no. 7 (July 30, 2017): 1645–46. http://dx.doi.org/10.18632/aging.101273.

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31

Wrighton, Katharine H. "Inactivating PTP1B upon ER stress." Nature Reviews Molecular Cell Biology 13, no. 2 (January 5, 2012): 62–63. http://dx.doi.org/10.1038/nrm3269.

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32

Crunkhorn, Sarah. "ER stress modulator reverses diabetes." Nature Reviews Drug Discovery 14, no. 8 (July 31, 2015): 528. http://dx.doi.org/10.1038/nrd4702.

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33

Hurtley, Stella M. "ER regulates stress granule fission." Science 367, no. 6477 (January 30, 2020): 522.14–524. http://dx.doi.org/10.1126/science.367.6477.522-n.

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34

Lindholm, D., H. Wootz, and L. Korhonen. "ER stress and neurodegenerative diseases." Cell Death & Differentiation 13, no. 3 (January 6, 2006): 385–92. http://dx.doi.org/10.1038/sj.cdd.4401778.

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35

TAKAHASHI, Ryosuke. "Neurodegeneration caused by ER stress?" Folia Pharmacologica Japonica 124, no. 6 (2004): 375–82. http://dx.doi.org/10.1254/fpj.124.375.

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36

VanHook, Annalisa M. "ER-phagy to alleviate stress." Science Signaling 11, no. 516 (February 6, 2018): eaat1772. http://dx.doi.org/10.1126/scisignal.aat1772.

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37

Wang, Xiaoli, Colins O. Eno, Brian J. Altman, Yanglong Zhu, Guoping Zhao, Kristen E. Olberding, Jeffrey C. Rathmell, and Chi Li. "ER stress modulates cellular metabolism." Biochemical Journal 435, no. 1 (March 15, 2011): 285–96. http://dx.doi.org/10.1042/bj20101864.

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Changes in metabolic processes play a critical role in the survival or death of cells subjected to various stresses. In the present study, we have investigated the effects of ER (endoplasmic reticulum) stress on cellular metabolism. A major difficulty in studying metabolic responses to ER stress is that ER stress normally leads to apoptosis and metabolic changes observed in dying cells may be misleading. Therefore we have used IL-3 (interleukin 3)-dependent Bak−/−Bax−/− haemopoietic cells which do not die in the presence of the ER-stress-inducing drug tunicamycin. Tunicamycin-treated Bak−/−Bax−/− cells remain viable, but cease growth, arresting in G1-phase and undergoing autophagy in the absence of apoptosis. In these cells, we used NMR-based SIRM (stable isotope-resolved metabolomics) to determine the metabolic effects of tunicamycin. Glucose was found to be the major carbon source for energy production and anabolic metabolism. Following tunicamycin exposure, glucose uptake and lactate production are greatly reduced. Decreased 13C labelling in several cellular metabolites suggests that mitochondrial function in cells undergoing ER stress is compromised. Consistent with this, mitochondrial membrane potential, oxygen consumption and cellular ATP levels are much lower compared with untreated cells. Importantly, the effects of tunicamycin on cellular metabolic processes may be related to a reduction in cell-surface GLUT1 (glucose transporter 1) levels which, in turn, may reflect decreased Akt signalling. These results suggest that ER stress exerts profound effects on several central metabolic processes which may help to explain cell death arising from ER stress in normal cells.

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38

Minamino, Tetsuo, and Masafumi Kitakaze. "ER stress in cardiovascular disease." Journal of Molecular and Cellular Cardiology 48, no. 6 (June 2010): 1105–10. http://dx.doi.org/10.1016/j.yjmcc.2009.10.026.

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39

Haspel, Jeffrey. "Surf’s up for ER stress." Science Translational Medicine 9, no. 396 (June 28, 2017): eaan6728. http://dx.doi.org/10.1126/scitranslmed.aan6728.

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40

van der Harg, Judith, Anna Nolle, Susanne LaFleur, Jeroen Hoozemans, and Wiep Scheper. "Metabolic stress and ER proteostasis." Mitochondrion 24 (September 2015): S5—S6. http://dx.doi.org/10.1016/j.mito.2015.07.022.

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41

Ogen-Shtern, Navit, Tamuz Ben David, and Gerardo Z. Lederkremer. "Protein aggregation and ER stress." Brain Research 1648 (October 2016): 658–66. http://dx.doi.org/10.1016/j.brainres.2016.03.044.

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42

Bird, Lucy. "ER stress induces systemic inflammation." Nature Reviews Immunology 6, no. 3 (March 2006): 170. http://dx.doi.org/10.1038/nri1819.

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43

Leavy, Olive. "Mismanaged ER stress and inflammation." Nature Reviews Immunology 8, no. 11 (November 2008): 824. http://dx.doi.org/10.1038/nri2435.

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44

Jaurez, M., A. Grenon-Girard, J. Tardif, and N. Bousette. "Cardiac Lipotoxicity Causes Er Stress." Canadian Journal of Cardiology 29, no. 10 (October 2013): S118. http://dx.doi.org/10.1016/j.cjca.2013.07.160.

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45

Zhou, Yan, Dharmani Devi Murugan, Haroon Khan, Yu Huang, and Wai San Cheang. "Roles and Therapeutic Implications of Endoplasmic Reticulum Stress and Oxidative Stress in Cardiovascular Diseases." Antioxidants 10, no. 8 (July 22, 2021): 1167. http://dx.doi.org/10.3390/antiox10081167.

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In different pathological states that cause endoplasmic reticulum (ER) calcium depletion, altered glycosylation, nutrient deprivation, oxidative stress, DNA damage or energy perturbation/fluctuations, the protein folding process is disrupted and the ER becomes stressed. Studies in the past decade have demonstrated that ER stress is closely associated with pathogenesis of obesity, insulin resistance and type 2 diabetes. Excess nutrients and inflammatory cytokines associated with metabolic diseases can trigger or worsen ER stress. ER stress plays a critical role in the induction of endothelial dysfunction and atherosclerosis. Signaling pathways including AMP-activated protein kinase and peroxisome proliferator-activated receptor have been identified to regulate ER stress, whilst ER stress contributes to the imbalanced production between nitric oxide (NO) and reactive oxygen species (ROS) causing oxidative stress. Several drugs or herbs have been proved to protect against cardiovascular diseases (CVD) through inhibition of ER stress and oxidative stress. The present article reviews the involvement of ER stress and oxidative stress in cardiovascular dysfunction and the potential therapeutic implications.

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46

Booth, Laurence, Jane L. Roberts, Nichola Cruickshanks, Steven Grant, Andrew Poklepovic, and Paul Dent. "Regulation of OSU-03012 Toxicity by ER Stress Proteins and ER Stress–Inducing Drugs." Molecular Cancer Therapeutics 13, no. 10 (August 7, 2014): 2384–98. http://dx.doi.org/10.1158/1535-7163.mct-14-0172.

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47

Das, Indrajit, Chin Wen Png, Rajaraman D. Eri, Thu V. Tran, Rohan Lourie, Iulia Oancea, Denis I. Crane, Timothy H. Florin, and Michael A. McGuckin. "Dexamethasone Ameliorates Intestinal Epithelial Cell Endoplasmic Reticulum (ER) Stress and ER Stress Induced Colitis." Gastroenterology 140, no. 5 (May 2011): S—166. http://dx.doi.org/10.1016/s0016-5085(11)60673-2.

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48

Tardif, Keith D., Gulam Waris, and Aleem Siddiqui. "Hepatitis C virus, ER stress, and oxidative stress." Trends in Microbiology 13, no. 4 (April 2005): 159–63. http://dx.doi.org/10.1016/j.tim.2005.02.004.

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49

Naidoo, Nirinjini. "ER and aging—Protein folding and the ER stress response." Ageing Research Reviews 8, no. 3 (July 2009): 150–59. http://dx.doi.org/10.1016/j.arr.2009.03.001.

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50

Xu, Jiancheng, Qi Zhou, Wei Xu, and Lu Cai. "Endoplasmic Reticulum Stress and Diabetic Cardiomyopathy." Experimental Diabetes Research 2012 (2012): 1–12. http://dx.doi.org/10.1155/2012/827971.

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The endoplasmic reticulum (ER) is an organelle entrusted with lipid synthesis, calcium homeostasis, protein folding, and maturation. Perturbation of ER-associated functions results in an evolutionarily conserved cell stress response, the unfolded protein response (UPR) that is also called ER stress. ER stress is aimed initially at compensating for damage but can eventually trigger cell death if ER stress is excessive or prolonged. Now the ER stress has been associated with numerous diseases. For instance, our recent studies have demonstrated the important role of ER stress in diabetes-induced cardiac cell death. It is known that apoptosis has been considered to play a critical role in diabetic cardiomyopathy. Therefore, this paper will summarize the information from the literature and our own studies to focus on the pathological role of ER stress in the development of diabetic cardiomyopathy. Improved understanding of the molecular mechanisms underlying UPR activation and ER-initiated apoptosis in diabetic cardiomyopathy will provide us with new targets for drug discovery and therapeutic intervention.

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Journal articles on the topic 'ER stress'

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