• Tribology and Lubricants
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• v.18 no.1
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• pp.16-23
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• 2002

For increasing the yield stress of ER fluids, the compressing ER electrode was developed and the compressing electrorheological (ER) behavior of anhydrous ER fluids in silicone oil of phosphorous ester cellulose powder was investigated. Under constant electric field, not only the current density but also the yield stress of anhydrous ER fluids were studied as varying the compressing length of ER electrode distance. From the experimental results the compressing of ER electrode had a large influence to the ER properties of anhydrous ER fluids. The current density was proportional to the compressing length of ER electrode under constant electric field and volume fraction also tile compressing yield stress was proportional to the volume fraction of dispersed particles under constant electric field and compressing length. When the ER electrode was compressed with 150mm after charging the electric field, 4 kV, tile yield stress of phosphoric ester cellulose ER fluids increased to thirteen times comparing with the yield stress measured at normal electrode.

• Proceedings of the Korean Society of Tribologists and Lubrication Engineers Conference
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• 2001.11a
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• pp.138-145
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• 2001

For increasing the yield stress of ER fluids, the compressing ER electrode was developed and the compressing electrorheological (ER) behavior of anhydrous ER fluids in silicone oil of phosphorous ester cellulose powder was investigated. Under constant electric field, not only the current density but also the yield stress of anhydrous ER fluids were studied as varying the compressing length of compressing ER electrode. From the experimental results, the compressing of ER electrode had a large influence to the ER properties of anhydrous ER fluids. The current density was proportional to the compressing length of ER electrode under constant electric field and volume fraction also the compressing yield stress was proportional to the volume fraction of dispersed particles under constant electric field and compressing length. When the ER electrode was compressed with 150mm after charging the electric field, 4 kV, the yield stress of phosphoric ester cellulose ER fluids increased to thirteen times comparing with the yield stress measured at normal electrode.

• Molecules and Cells
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• v.41 no.8
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• pp.705-716
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• 2018

The endoplasmic reticulum (ER) is a critical organelle for protein synthesis, folding and modification, and lipid synthesis and calcium storage. Dysregulation of ER functions leads to the accumulation of misfolded- or unfolded-protein in the ER lumen, and this triggers the unfolded protein response (UPR), which restores ER homeostasis. The UPR is characterized by three distinct downstream signaling pathways that promote cell survival or apoptosis depending on the stressor, the intensity and duration of ER stress, and the cell type. Mammalian cells express the UPR transducers IRE1, PERK, and ATF6, which control transcriptional and translational responses to ER stress. Direct links between ER stress and immune responses are also evident, but the mechanisms by which UPR signaling cascades are coordinated with immunity remain unclear. This review discusses recent investigations of the roles of ER stress in immune responses that lead to differentiation, maturation, and cytokine expression in immune cells. Further understanding of how ER stress contributes to the pathogenesis of immune disorders will facilitate the development of novel therapies that target UPR pathways.

• Molecules and Cells
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• v.41 no.11
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• pp.964-970
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• 2018

Atherosclerosis preferentially involves in prone area of low and disturbed blood flow while steady and high levels of laminar blood flow are relatively protected from atherosclerosis. Disturbed flow induces endoplasmic reticulum (ER) stress and the unfolded protein response (UPR). ER stress is caused under stress that disturbs the processing and folding of proteins resulting in the accumulation of misfolded proteins in the ER and activation of the UPR. Prolonged or severe UPR leads to activate apoptotic signaling. Recent studies have indicated that disturbed flow significantly up-regulated $p-ATF6{\alpha}$, $p-IRE1{\alpha}$, and its target spliced XBP-1. However, the role of laminar flow in ER stress-mediated endothelial apoptosis has not been reported yet. The present study thus investigated the role of laminar flow in ER stress-dependent endothelial cell death. The results demonstrated that laminar flow protects ER stress-induced cleavage forms of PARP-1 and caspase-3. Also, laminar flow inhibits ER stress-induced $p-eIF2{\alpha}$, ATF4, CHOP, spliced XBP-1, ATF6 and JNK pathway; these effects are abrogated by pharmacological inhibition of PI3K with wortmannin. Finally, nitric oxide affects thapsigargin-induced cell death in response to laminar flow but not UPR. Taken together, these findings indicate that laminar flow inhibits UPR and ER stress-induced endothelial cell death via PI3K/Akt pathway.

• Journal of Life Science
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• v.17 no.6 s.86
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• pp.847-858
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• 2007

The endoplasmic reticulum (ER) is an important intracellular organelle for folding and maturation of newly synthesized transmembrane and secretory proteins. The ER provides stringent quality control systems to ensure that only correctly folded proteins exit the ER and unfolded or misfolded proteins are retained and ultimately degraded. The ER has evolved stress response both signaling pathways the unfolded protein response (UPR) to cope with the accmulation of unfolded or misfolded proteins and ER overload response (EOR). Accumulating evidence suggests that, in addition to responsibility for protein processing, ER is also an important signaling compartment and a sensor of cellular stress. In this respect, production of bio-functional recombinant-proteins requires efficient functioning of the ER secretory pathway in host cells. This review briefly summarizes our understanding of the ER signaling developed in the recent years to help of the secretion capacities of recombinant cells.

• Biomedical Science Letters
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• v.11 no.2
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• pp.135-141
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• 2005

A Jopock (Jpk), a trans-acting factor associating with the position-specific regulatory element of murine Hoxa-7, has shown to have a toxicity to both prokaryotic and eukaryotic cells when overexpressed. Since Jpk protein harbors a transmembrane domain and a putative endoplasmic reticulum (ER)-retention signal at the N-terminus, a subcellular localization of the protein was analyzed after fusing it into the green fluorescent protein (GFP): Both N-term (Jpk-EGFP) and C-term tagged-Jpk (EGFP-Jpk) showed to be localized in the ER when analyzed under the fluorescence microscopy after staining the cells with ER- and MitoTracker. Since ER stress triggers the ER-stress mediated apoptosis to eliminate the damaged cells, we analyzed the expression pattern of Jpk under ER-stress condition. When MCF7 cells were treated with the ER-stress inducer such as DTT and EGTA, the expression of Jpk was upregulated at the transcriptional level like that of Grp78, a molecular chaperone well known to be overexpressed under ER-stress condition. In the presence of high concentration of ER-sterss inducer (10 mM), about 70 (DTT) to $95\%$ (EGTA) of cells died stronly expressing ($10\~12$ fold) Jpk. Whereas at the low concentration ($0.001\~1.0\;mM$) of the inducer, the expression of Jpk was increased about 2.5 (EGTA) to 5 fold (DTT), which is rather similar to those of ER chaperone protein Grp78. These results altogether indicate that the ER-stress upregulated the expression of Jpk and the excess stress induces the ER-stress induced apoptosis and the concomitant expression of Jpk.

• Biomedical Science Letters
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• v.12 no.4
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• pp.435-438
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• 2006

In eukaryotes, ER stress induces UPR (unfolded protein response) via IRE1 activation which sends a molecular signal for XBP1 mRNA splicing in the cytosol. During this mRNA splicing, 23 nt removed in which contains PstI site and then resulting XBP1 product is not digested with PstI restriction enzyme. In this study, using this XBP1 mRNA splicing mechanism, the effect of heat shock on thyrocytes is studied, because heat shock response in the thyrocytes needs more study to understand thyroid physiology under alternative environments. ER inducible drugs (tunicamycin, DTT, $Ca^{2+}$ ionopore A23187, BFA) induce ER stress in the thyrocytes. From 3 hours after heat shock, ER stress is induced and which is reversible when heat shock is without. While $Ca^{2+}$ ionopore A23187 is reversible from ER stress by washing out the drug, thapsigagin is irreversible. Other ER inducible drugs are not so sensitive to ER stress repairing. XBP1 mRNA splicing in a cell is very available method to detect ER stress. It needs only a small quantity of total RNA and processing also very easy.

• The Korean Journal of Physiology and Pharmacology
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• v.22 no.5
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• pp.567-575
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• 2018

Acute kidney injury (AKI), which is defined as a rapid decline of renal function, becomes common and recently recognized to be closely intertwined with chronic kidney diseases. Current treatment for AKI is largely supportive, and endoplasmic reticulum (ER) stress has emerged as a novel mediator of AKI. Since carbon monoxide attenuates ER stress, the objective of the present study aimed to determine the protective effect of carbon monoxide releasing molecule-2 (CORM2) on AKI associated with ER stress. Kidney injury was induced after LPS (15 mg/kg) treatment at 12 to 24 h in C57BL/6J mice. Pretreatment of CORM2 (30 mg/kg) effectively prevented LPS-induced oxidative stress and inflammation during AKI in mice. CORM2 treatment also effectively inhibited LPS-induced ER stress in AKI mice. In order to confirm effect of CO on the pathophysiological role of tubular epithelial cells in AKI, we used mProx24 cells. Pretreatment of CORM2 attenuated LPS-induced ER stress, oxidative stress, and inflammation in mProx24 cells. These data suggest that CO therapy may prevent ER stress-mediated AKI.

• Biomolecules & Therapeutics
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• v.20 no.3
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• pp.346-351
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• 2012

Cells show various stress signs when they are challenged with severe physiological problems. Majority of such cellular stresses are conveyed to endoplasmic reticulum (ER) and unfolded protein response (UPR) serves as typical defense mechanism against ER stress. This study investigated an interaction between ER stress agents using macropage cell line Raw 264.7. When activated by lipopolysaccharide (LPS), the cell lines showed typical indicators of ER stress. Along with molecular chaperones, the activation process leads to the production of additional inflammatory mediators. Following activation, the macrophage cell line was further treated with TUN and characterized in terms of chaperone expression and cytokine secretion. When treated with TUN, the activated macrophage cell leads to increased secretion of IL-6 although expression of ER stress markers, GRP94 and GRP78 increased. The secretion of cytokines continued until the addition of BFA which inhibits protein targeting from ER to Golgi. However, secretion of cytokines was ceased upon dual treatments with BFA and TG. This result strongly implies that cells may differently deal with various polypeptides depending on the urgency in cellular function under ER stress. Considering IL-6 is one of the most important signal molecules in macrophage, the molecule might be able to circumvent ER stress and UPR to reach its targeting site.

• Journal of Life Science
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• v.22 no.8
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• pp.1132-1136
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• 2012

Many kind of cell stresses induce gene expression of unfolded protein response (UPR)-associated factors. This study demonstrated that up- and down-regulation of gene expression of endoplasmic reticulum (ER) stress chaperones and ER stress sensors was induced by immobilization stress in the rat organs (adrenal gland, liver, lung, muscle). However, no statistically significant regulation was detected in the others (heart, spleen, thymus, kidney, testis). The results are the first to show that immobilization stress induces UPR associated gene expression, will help to explain immobilization stress-associated ER stress.