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Journal articles on the topic 'Endoplasmic Reticulum'

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Published: 4 June 2021
Last updated: 6 July 2024

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1

Koch, G., M. Smith, D. Macer, P. Webster, and R. Mortara. "Endoplasmic reticulum contains a common, abundant calcium-binding glycoprotein, endoplasmin." Journal of Cell Science 86, no. 1 (December 1, 1986): 217–32. http://dx.doi.org/10.1242/jcs.86.1.217.

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The most abundant protein in microsomal membrane preparations from mammalian cells has been identified as a 100 X 10(3) Mr concanavalin A-binding glycoprotein. The glycosyl moiety of the glycoprotein is completely sensitive to endoglycosidase H, suggesting a predominantly endoplasmic reticulum localization in the cell. Using a monospecific antibody it was shown by binding and immunofluorescence studies that the glycoprotein is intracellular. Immunoelectron microscopy showed that the glycoprotein was at least 100 times more concentrated in the endoplasmic reticulum than in any other cellular organelle. It was found to be substantially overexpressed in cells and tissues rich in endoplasmic reticulum. Since it is the major common protein component associated with the endoplasmic reticulum we refer to it as endoplasmin. Calcium-binding studies show that endoplasmin is a major calcium-binding protein in cells, suggesting that at least one of its roles might be in the calcium-storage function of the endoplasmic reticulum. The amino-terminal sequence of endoplasmin is identical to that of a 100 X 10(3) Mr stress-related protein.
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2

Deneke, Jurgen. "Endoplasmic reticulum." Biochemical Society Transactions 28, no. 3 (June 1, 2000): A59. http://dx.doi.org/10.1042/bst028a059.

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3

Arozarena, Imanol, David Matallanas, María T. Berciano, Victoria Sanz-Moreno, Fernando Calvo, María T. Muñoz, Gustavo Egea, Miguel Lafarga, and Piero Crespo. "Activation of H-Ras in the Endoplasmic Reticulum by the RasGRF Family Guanine Nucleotide Exchange Factors." Molecular and Cellular Biology 24, no. 4 (February 15, 2004): 1516–30. http://dx.doi.org/10.1128/mcb.24.4.1516-1530.2004.

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ABSTRACT Recent findings indicate that in addition to its location in the peripheral plasma membrane, H-Ras is found in endomembranes like the endoplasmic reticulum and the Golgi complex. In these locations H-Ras is functional and can efficiently engage downstream effectors, but little is known about how its activation is regulated in these environments. Here we show that the RasGRF family exchange factors, both endogenous and ectopically expressed, are present in the endoplasmic reticulum but not in the Golgi complex. With the aid of H-Ras constructs specifically tethered to the plasma membrane, endoplasmic reticulum, and Golgi complex, we demonstrate that RasGRF1 and RasGRF2 can activate plasma membrane and reticular, but not Golgi-associated, H-Ras. We also show that RasGRF DH domain is required for the activation of H-Ras in the endoplasmic reticulum but not in the plasma membrane. Furthermore, we demonstrate that RasGRF mediation favors the activation of reticular H-Ras by lysophosphatidic acid treatment whereas plasma membrane H-Ras is made more responsive to stimulation by ionomycin. Overall, our results provide the initial insights into the regulation of H-Ras activation in the endoplasmic reticulum.
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4

BANHEGYI, G., P. BAUMEISTER, A. BENEDETTI, D. DONG, Y. FU, A. S. LEE, J. LI, et al. "Endoplasmic Reticulum Stress." Annals of the New York Academy of Sciences 1113, no. 1 (May 18, 2007): 58–71. http://dx.doi.org/10.1196/annals.1391.007.

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5

Terasaki, M., and T. S. Reese. "Characterization of endoplasmic reticulum by co-localization of BiP and dicarbocyanine dyes." Journal of Cell Science 101, no. 2 (February 1, 1992): 315–22. http://dx.doi.org/10.1242/jcs.101.2.315.

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The original concept of endoplasmic reticulum derived from the observation of a reticular network in cultured fibroblasts by electron microscopy of whole cells. It was previously reported that the fluorescent dye, DiOC6(3), stains a similar network as well as mitochondria and other organelles in living cells. Here, we investigate the significance of the structures labeled by DiO6(3) in CV-1 cells, a monkey epithelial cell line. First, we show that the network stained in living CV-1 cells is preserved by glutaraldehyde fixation and then we co-label it with an antibody against BiP (immunoglobulin binding protein), a protein commonly accepted to be present in the endoplasmic reticulum. Anti-BiP labeled the same network as that labeled by DiOC6(3), so this network now is identified as being part of the endoplasmic reticulum. DiOC6(3) labels many other membrane compartments in addition to the endoplasmic reticulum. This, along with its lipophilic properties, suggests that DiOC6(3) stains all intracellular membranes. However, the extensive reticular network in the thin peripheral regions of cultured cells is easily distinguished from these other membranes. Thus, staining by DiOC6(3) is a useful method for localizing the endoplasmic reticulum, particularly in thin peripheral regions of cultured cells.
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6

Villa, Antonello, Paola Podini, Alessandra Nori, Maria Carla Panzeri, Adelina Martini, Jacopo Meldolesi, and Pompeo Volpe. "The Endoplasmic Reticulum-Sarcoplasmic Reticulum Connection." Experimental Cell Research 209, no. 1 (November 1993): 140–48. http://dx.doi.org/10.1006/excr.1993.1294.

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7

Zhou, Long-Xia, An-Ning Yang, Jiu-Kai Chen, Li Zhao, Yan-Hua Wang, Xian-Mei Liu, Xin Cai, Ming-Hao Zhang, Yi-Deng Jiang, and Jun Cao. "Endoplasmic reticulum oxidoreductin 1α mediates homocysteine-induced hepatocyte endoplasmic reticulum stress." World Chinese Journal of Digestology 22, no. 34 (2014): 5228. http://dx.doi.org/10.11569/wcjd.v22.i34.5228.

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8

Kumar, Ravindra, Bandana Kumari, and Manish Kumar. "Prediction of endoplasmic reticulum resident proteins using fragmented amino acid composition and support vector machine." PeerJ 5 (September 4, 2017): e3561. http://dx.doi.org/10.7717/peerj.3561.

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BackgroundThe endoplasmic reticulum plays an important role in many cellular processes, which includes protein synthesis, folding and post-translational processing of newly synthesized proteins. It is also the site for quality control of misfolded proteins and entry point of extracellular proteins to the secretory pathway. Hence at any given point of time, endoplasmic reticulum contains two different cohorts of proteins, (i) proteins involved in endoplasmic reticulum-specific function, which reside in the lumen of the endoplasmic reticulum, called as endoplasmic reticulum resident proteins and (ii) proteins which are in process of moving to the extracellular space. Thus, endoplasmic reticulum resident proteins must somehow be distinguished from newly synthesized secretory proteins, which pass through the endoplasmic reticulum on their way out of the cell. Approximately only 50% of the proteins used in this study as training data had endoplasmic reticulum retention signal, which shows that these signals are not essentially present in all endoplasmic reticulum resident proteins. This also strongly indicates the role of additional factors in retention of endoplasmic reticulum-specific proteins inside the endoplasmic reticulum.MethodsThis is a support vector machine based method, where we had used different forms of protein features as inputs for support vector machine to develop the prediction models. During trainingleave-one-outapproach of cross-validation was used. Maximum performance was obtained with a combination of amino acid compositions of different part of proteins.ResultsIn this study, we have reported a novel support vector machine based method for predicting endoplasmic reticulum resident proteins, named as ERPred. During training we achieved a maximum accuracy of 81.42% withleave-one-outapproach of cross-validation. When evaluated on independent dataset, ERPred did prediction with sensitivity of 72.31% and specificity of 83.69%. We have also annotated six different proteomes to predict the candidate endoplasmic reticulum resident proteins in them. A webserver, ERPred, was developed to make the method available to the scientific community, which can be accessed athttp://proteininformatics.org/mkumar/erpred/index.html.DiscussionWe found that out of 124 proteins of the training dataset, only 66 proteins had endoplasmic reticulum retention signals, which shows that these signals are not an absolute necessity for endoplasmic reticulum resident proteins to remain inside the endoplasmic reticulum. This observation also strongly indicates the role of additional factors in retention of proteins inside the endoplasmic reticulum. Our proposed predictor, ERPred, is a signal independent tool. It is tuned for the prediction of endoplasmic reticulum resident proteins, even if the query protein does not contain specific ER-retention signal.
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9

Groenendyk, Jody, Xiao Fan, Zhenling Peng, Lukasz Kurgan, and Marek Michalak. "Endoplasmic reticulum and the microRNA environment in the cardiovascular system." Canadian Journal of Physiology and Pharmacology 97, no. 6 (June 2019): 515–27. http://dx.doi.org/10.1139/cjpp-2018-0720.

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Stress responses are important to human physiology and pathology, and the inability to adapt to cellular stress leads to cell death. To mitigate cellular stress and re-establish homeostasis, cells, including those in the cardiovascular system, activate stress coping response mechanisms. The endoplasmic reticulum, a component of the cellular reticular network in cardiac cells, mobilizes so-called endoplasmic reticulum stress coping responses, such as the unfolded protein response. MicroRNAs play an important part in the maintenance of cellular and tissue homeostasis, perform a central role in the biology of the cardiac myocyte, and are involved in pathological cardiac function and remodeling. In this paper, we review a link between endoplasmic reticulum homeostasis and microRNA with an emphasis on the impact on stress responses in the cardiovascular system.
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10

Römisch, Karin. "ENDOPLASMIC RETICULUM–ASSOCIATED DEGRADATION." Annual Review of Cell and Developmental Biology 21, no. 1 (November 2005): 435–56. http://dx.doi.org/10.1146/annurev.cellbio.21.012704.133250.

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11

Burchell, Ann. "Endoplasmic reticulum phosphate transport." Kidney International 49, no. 4 (April 1996): 953–58. http://dx.doi.org/10.1038/ki.1996.134.

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12

Orci, L., A. Perrelet, M. Ravazzola, M. Amherdt, J. E. Rothman, and R. Schekman. "Coatomer-rich endoplasmic reticulum." Proceedings of the National Academy of Sciences 91, no. 25 (December 6, 1994): 11924–28. http://dx.doi.org/10.1073/pnas.91.25.11924.

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13

CARLSON, J. "Endoplasmic reticulum storage disease." Histopathology 16, no. 3 (March 1990): 309–12. http://dx.doi.org/10.1111/j.1365-2559.1990.tb01124.x.

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14

Gorelick, Fred S., and Christine Shugrue. "Exiting the endoplasmic reticulum." Molecular and Cellular Endocrinology 177, no. 1-2 (May 2001): 13–18. http://dx.doi.org/10.1016/s0303-7207(01)00438-5.

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15

Mancias, Joseph D., and Jonathan Goldberg. "Exiting the Endoplasmic Reticulum." Traffic 6, no. 4 (March 7, 2005): 278–85. http://dx.doi.org/10.1111/j.1600-0854.2005.00279.x.

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16

Schröder, M. "Endoplasmic reticulum stress responses." Cellular and Molecular Life Sciences 65, no. 6 (November 26, 2007): 862–94. http://dx.doi.org/10.1007/s00018-007-7383-5.

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17

Soltys, Bohdan J., and Radhey S. Gupta. "Interrelationships of endoplasmic reticulum, mitochondria, intermediate filaments, and microtubules—a quadruple fluorescence labeling study." Biochemistry and Cell Biology 70, no. 10-11 (October 1, 1992): 1174–86. http://dx.doi.org/10.1139/o92-163.

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To study the interrelationships of endoplasmic reticulum, mitochondria, intermediate filaments, and microtubules, we have developed a quadruple fluorescence labeling procedure to visualize all four structures in the same cell. We applied this approach to study cellular organization in control cells and in cells treated with the microtubule drugs vinblastine or taxol. Endoplasmic reticulum was visualized by staining glutaraldehyde-fixed cells with the dye 3,3′-dihexyloxacarbocyanine iodide. After detergent permeabilization, triple immunofluorescence was carried out to specifically visualize mitochondria, vimentin intermediate filaments, and microtubules. Mitochondria in human fibroblasts were found to be highly elongated tubular structures (lengths up to greater than 50 μm), which in many cases were apparently fused to each other. Mitochondria were always observed to be associated with endoplasmic reticulum, although endoplasmic reticulum also existed independently. Intermediate filament distribution could not completely account for endoplasmic reticulum or mitochondrial distributions. Microtubules, however, always codistributed with these organelles. Microtubule depolymerization in vinblastine treated cells resulted in coaggregation of endoplasmic reticulum and mitochondria, and in the collapse of intermediate filaments. The spatial distributions of organelles compared with, intermediate filaments were not identical, indicating that attachment of organelles to intermediate filaments was not responsible for organelle aggregation. Mitochondrial associations with endoplasmic reticulum, on the other hand, were retained, indicating this association was stable regardless of endoplasmic reticulum form or microtubules. In taxol-treated cells, endoplasmic reticulum, mitochondria, and intermediate filaments were all associated with taxol- stabilized microtubule bundles.Key words: endoplasmic reticulum, mitochondria, intermediate filaments, microtubules.
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18

Das, Swapan K., Winston S. Chu, Ashis K. Mondal, Neeraj K. Sharma, Philip A. Kern, Neda Rasouli, and Steven C. Elbein. "Effect of pioglitazone treatment on endoplasmic reticulum stress response in human adipose and in palmitate-induced stress in human liver and adipose cell lines." American Journal of Physiology-Endocrinology and Metabolism 295, no. 2 (August 2008): E393—E400. http://dx.doi.org/10.1152/ajpendo.90355.2008.

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Obesity and elevated cytokine secretion result in a chronic inflammatory state and may cause the insulin resistance observed in type 2 diabetes. Recent studies suggest a key role for endoplasmic reticulum stress in hepatocytes and adipocytes from obese mice, resulting in reduced insulin sensitivity. To address the hypothesis that thiazolidinediones, which improve peripheral insulin sensitivity, act in part by reducing the endoplasmic reticulum stress response, we tested subcutaneous adipose tissue from 20 obese volunteers treated with pioglitazone for 10 wk. We also experimentally induced endoplasmic reticulum stress using palmitate, tunicamycin, and thapsigargin in the human HepG2 liver cell line with or without pioglitazone pretreatment. We quantified endoplasmic reticulum stress response by measuring both gene expression and phosphorylation. Pioglitazone significantly improved insulin sensitivity in human volunteers ( P = 0.002) but did not alter markers of endoplasmic reticulum stress. Differences in pre- and posttreatment endoplasmic reticulum stress levels were not correlated with changes in insulin sensitivity or body mass index. In vitro, palmitate, thapsigargin, and tunicamycin but not oleate induced endoplasmic reticulum stress in HepG2 cells, including increased transcripts CHOP, ERN1, GADD34, and PERK, and increased XBP1 splicing along with phosphorylation of eukaryotic initiation factor eIF2α, JNK1, and c- jun. Although patterns of endoplasmic reticulum stress response differed among palmitate, tunicamycin, and thapsigargin, pioglitazone pretreatment had no significant effect on any measure of endoplasmic reticulum stress, regardless of the inducer. Together, our data suggest that improved insulin sensitivity with pioglitazone is not mediated by a reduction in endoplasmic reticulum stress.
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19

Koch, G. L., D. R. Macer, and F. B. Wooding. "Endoplasmin is a reticuloplasmin." Journal of Cell Science 90, no. 3 (July 1, 1988): 485–91. http://dx.doi.org/10.1242/jcs.90.3.485.

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The location of endoplasmin in the endoplasmic reticulum was investigated by biochemical and immunoelectron microscopic analyses. The protein could be obtained in a soluble form by procedures that do not involve the use of any detergents. The soluble protein has the amino- and carboxy-terminal sequences of the intact molecule, showing that it has not been proteolysed. Application of the Triton X-114 phase-separation test does not reveal significant hydrophobicity in the molecule. Immunogold labelling studies on cells with a dilated endoplasmic reticulum (ER) lumen show that endoplasmin is uniformly distributed throughout the lumen, with no evidence of a preferential association with the membrane. These studies clearly demonstrate that endoplasmin is a luminal protein of the ER, i.e. a reticuloplasmin, and not an integral membrane protein.
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20

Hu, Yanan, Wenhao Yang, Liang Xie, Tao Liu, Hanmin Liu, and Bin Liu. "Endoplasmic reticulum stress and pulmonary hypertension." Pulmonary Circulation 10, no. 1 (January 2020): 204589401990012. http://dx.doi.org/10.1177/2045894019900121.

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Pulmonary hypertension is a fatal disease of which pulmonary vasculopathy is the main pathological feature resulting in the mean pulmonary arterial pressure higher than 25 mmHg. Moreover, pulmonary hypertension remains a tough problem with unclear molecular mechanisms. There have been dozens of studies about endoplasmic reticulum stress during the onset of pulmonary hypertension in patients, suggesting that endoplasmic reticulum stress may have a critical effect on the pathogenesis of pulmonary hypertension. The review aims to summarize the rationale to elucidate the role of endoplasmic reticulum stress in pulmonary hypertension. Started by reviewing the mechanisms responsible for the unfolded protein response following endoplasmic reticulum stress, the potential link between endoplasmic reticulum stress and pulmonary hypertension were introduced, and the contributions of endoplasmic reticulum stress to different vascular cells, mitochondria, and inflammation were described, and finally the potential therapies of attenuating endoplasmic reticulum stress for pulmonary hypertension were discussed.
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21

Erwin Ivessa, N., Claudia Kitzm�ller, and Maddalena Virgilio. "Endoplasmic-reticulum-associated protein degradation inside and outside of the endoplasmic reticulum." Protoplasma 207, no. 1-2 (March 1999): 16–23. http://dx.doi.org/10.1007/bf01294709.

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22

Hadley, Gina, Ain A. Neuhaus, Yvonne Couch, Daniel J. Beard, Bryan A. Adriaanse, Kostas Vekrellis, Gabriele C. DeLuca, Michalis Papadakis, Brad A. Sutherland, and Alastair M. Buchan. "The role of the endoplasmic reticulum stress response following cerebral ischemia." International Journal of Stroke 13, no. 4 (August 4, 2017): 379–90. http://dx.doi.org/10.1177/1747493017724584.

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Background Cornu ammonis 3 (CA3) hippocampal neurons are resistant to global ischemia, whereas cornu ammonis (CA1) 1 neurons are vulnerable. Hamartin expression in CA3 neurons mediates this endogenous resistance via productive autophagy. Neurons lacking hamartin demonstrate exacerbated endoplasmic reticulum stress and increased cell death. We investigated endoplasmic reticulum stress responses in CA1 and CA3 regions following global cerebral ischemia, and whether pharmacological modulation of endoplasmic reticulum stress or autophagy altered neuronal viability . Methods In vivo: male Wistar rats underwent sham or 10 min of transient global cerebral ischemia. CA1 and CA3 areas were microdissected and endoplasmic reticulum stress protein expression quantified at 3 h and 12 h of reperfusion. In vitro: primary neuronal cultures (E18 Wistar rat embryos) were exposed to 2 h of oxygen and glucose deprivation or normoxia in the presence of an endoplasmic reticulum stress inducer (thapsigargin or tunicamycin), an endoplasmic reticulum stress inhibitor (salubrinal or 4-phenylbutyric acid), an autophagy inducer ([4′-(N-diethylamino) butyl]-2-chlorophenoxazine (10-NCP)) or autophagy inhibitor (3-methyladenine). Results In vivo, decreased endoplasmic reticulum stress protein expression (phospho-eIF2α and ATF4) was observed at 3 h of reperfusion in CA3 neurons following ischemia, and increased in CA1 neurons at 12 h of reperfusion. In vitro, endoplasmic reticulum stress inducers and high doses of the endoplasmic reticulum stress inhibitors also increased cell death. Both induction and inhibition of autophagy also increased cell death. Conclusion Endoplasmic reticulum stress is associated with neuronal cell death following ischemia. Neither reduction of endoplasmic reticulum stress nor induction of autophagy demonstrated neuroprotection in vitro, highlighting their complex role in neuronal biology following ischemia.
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23

Pavelka, M., and A. Ellinger. "Early and late transformations occurring at organelles of the Golgi area under the influence of brefeldin A: an ultrastructural and lectin cytochemical study." Journal of Histochemistry & Cytochemistry 41, no. 7 (July 1993): 1031–42. http://dx.doi.org/10.1177/41.7.8515046.

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We investigated the early and late changes of the Golgi region under the influence of the fungal metabolite brefeldin A (BFA) by electron microscopy and lectin cytochemistry using the beta-galactose-specific lectin from the beetle Allomyrina dichotoma (Allo A). In control cells, Allo-A reactions were confined to trans-Golgi elements, the trans-Golgi network, and to endosomes and lysosomes; the nuclear envelope and endoplasmic reticulum were consistently free of Allo A reactions. Our findings with cells from three different lines (i.e., HepG2 hepatoma cells, WI38 fibroblasts, and L132 embryonic lung cells) showed tubular-reticular transformations of the Golgi stacks as early as 30 sec after application of BFA. The transformations started at the cis side and proceeded rapidly; after only a few minutes the Golgi apparatus was no longer apparent as an individual entity. Simultaneously, giant tubules grew out of the Golgi region and traversed the cytoplasm over micrometer-long distances. In part, they were reactive for Allo A. Reactions for beta-galactose occurred in cisternae of the endoplasmic reticulum after 4-5 min of BFA treatment; after 30 min the entire endoplasmic reticulum was intensely reactive for Allo A. At 5 min and later, the tubular-reticular transformations appeared more compact, forming glomerulus-like structures (glomerulini). These were closely associated with cisternae of the endoplasmic reticulum. Initially, glomerulini were mostly Allo A negative or showed peripheral Allo A-positive segments. The number of Allo A-positive glomerulini increased with the duration of treatment. Our findings identify the glomerulini as bipolar structures forming a link between the endoplasmic reticulum and the dissociating Golgi stacks.
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24

Krishnan, Hari B., Jerry A. White, and Steven G. Pueppke. "Immunocytochemical localization of wheat prolamins in the lumen of the rough endoplasmic reticulum." Canadian Journal of Botany 69, no. 11 (November 1, 1991): 2574–77. http://dx.doi.org/10.1139/b91-320.

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Antibodies raised against gliadins, the alcohol-soluble proteins of wheat (Triticum aestivum L.) seeds, were used to localize gliadins within the lumen of the endoplasmic reticulum. Endosperm cells at 20 days after anthesis contain extensive rough endoplasmic reticulum that is fragmented and dilated. The dilated endoplasmic reticulum encloses aggregates of proteinaceous material that reacts strongly with gliadin-specific antibodies. Key words: gliadins, immunocytochemistry, protein A – gold, rough endoplasmic reticulum, wheat.
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25

Martinez, Alexis, Cristian M. Lamaizon, Cristian Valls, Fabien Llambi, Nancy Leal, Patrick Fitzgerald, Cliff Guy, et al. "c-Abl Phosphorylates MFN2 to Regulate Mitochondrial Morphology in Cells under Endoplasmic Reticulum and Oxidative Stress, Impacting Cell Survival and Neurodegeneration." Antioxidants 12, no. 11 (November 16, 2023): 2007. http://dx.doi.org/10.3390/antiox12112007.

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The endoplasmic reticulum is a subcellular organelle key in the control of synthesis, folding, and sorting of proteins. Under endoplasmic reticulum stress, an adaptative unfolded protein response is activated; however, if this activation is prolonged, cells can undergo cell death, in part due to oxidative stress and mitochondrial fragmentation. Here, we report that endoplasmic reticulum stress activates c-Abl tyrosine kinase, inducing its translocation to mitochondria. We found that endoplasmic reticulum stress-activated c-Abl interacts with and phosphorylates the mitochondrial fusion protein MFN2, resulting in mitochondrial fragmentation and apoptosis. Moreover, the pharmacological or genetic inhibition of c-Abl prevents MFN2 phosphorylation, mitochondrial fragmentation, and apoptosis in cells under endoplasmic reticulum stress. Finally, in the amyotrophic lateral sclerosis mouse model, where endoplasmic reticulum and oxidative stress has been linked to neuronal cell death, we demonstrated that the administration of c-Abl inhibitor neurotinib delays the onset of symptoms. Our results uncovered a function of c-Abl in the crosstalk between endoplasmic reticulum stress and mitochondrial dynamics via MFN2 phosphorylation.
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26

Volpe, P., A. Villa, P. Podini, A. Martini, A. Nori, M. C. Panzeri, and J. Meldolesi. "The endoplasmic reticulum-sarcoplasmic reticulum connection: distribution of endoplasmic reticulum markers in the sarcoplasmic reticulum of skeletal muscle fibers." Proceedings of the National Academy of Sciences 89, no. 13 (July 1, 1992): 6142–46. http://dx.doi.org/10.1073/pnas.89.13.6142.

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27

Li, Yina, Mingyang Li, Shi Feng, Qingxue Xu, Xu Zhang, Xiaoxing Xiong, and Lijuan Gu. "Ferroptosis and endoplasmic reticulum stress in ischemic stroke." Neural Regeneration Research 19, no. 3 (July 20, 2023): 611–18. http://dx.doi.org/10.4103/1673-5374.380870.

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Abstract Ferroptosis is a form of non-apoptotic programmed cell death, and its mechanisms mainly involve the accumulation of lipid peroxides, imbalance in the amino acid antioxidant system, and disordered iron metabolism. The primary organelle responsible for coordinating external challenges and internal cell demands is the endoplasmic reticulum, and the progression of inflammatory diseases can trigger endoplasmic reticulum stress. Evidence has suggested that ferroptosis may share pathways or interact with endoplasmic reticulum stress in many diseases and plays a role in cell survival. Ferroptosis and endoplasmic reticulum stress may occur after ischemic stroke. However, there are few reports on the interactions of ferroptosis and endoplasmic reticulum stress with ischemic stroke. This review summarized the recent research on the relationships between ferroptosis and endoplasmic reticulum stress and ischemic stroke, aiming to provide a reference for developing treatments for ischemic stroke.
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28

Yang, Wei, and Wulf Paschen. "Unfolded protein response in brain ischemia: A timely update." Journal of Cerebral Blood Flow & Metabolism 36, no. 12 (October 14, 2016): 2044–50. http://dx.doi.org/10.1177/0271678x16674488.

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Folding and processing newly synthesized proteins are vital functions of the endoplasmic reticulum that are sensitive to a variety of stress conditions. The unfolded protein response is activated to restore endoplasmic reticulum function impaired by stress. While we know that brain ischemia impairs endoplasmic reticulum function, the role of unfolded protein response activation in post-ischemic recovery of neurologic function is only beginning to emerge. Here, we summarize what is known about endoplasmic reticulum stress and unfolded protein response in brain ischemia and discuss recent findings from myocardial ischemia studies that could help to advance research on endoplasmic reticulum stress and unfolded protein response in brain ischemia.
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29

Kaprielian, Z., S. W. Robinson, D. M. Fambrough, and P. D. Kessler. "Movement of Ca(2+)-ATPase molecules within the sarcoplasmic/endoplasmic reticulum in skeletal muscle." Journal of Cell Science 109, no. 10 (October 1, 1996): 2529–37. http://dx.doi.org/10.1242/jcs.109.10.2529.

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The endoplasmic reticulum undergoes rapid, microscopic changes in its structure, including extension and anastomosis of tubular elements. Such dynamism is expected to manifest itself also as rapid intermixing of membrane components, at least within subdomains of the endoplasmic reticulum. Here we present evidence of a similar dynamism in the sarcoplasmic reticulum of developing skeletal muscle. The sarcoplasmic reticulum is sometimes considered a specialized type of endoplasmic reticulum, but it appears to be a rather static set of membrane-bound elements, repetitively arranged to enwrap each sarcomere of each myofibril. Both endoplasmic reticulum and sarcoplasmic reticulum contain P-type Ca(2+)-ATPases that transport calcium from the cytosol into their lumen. In the experiments reported here, chicken and mouse cells were fused by polyethylene glycol, natural myogenic cell fusion, or Sendai virus. The redistribution of Ca(2+)-ATPase molecules between chick and mouse endoplasmic reticulum/sarcoplasmic reticulum was followed by immunofluorescence microscopy in which species-specific monoclonal antibodies to chick and mouse Ca(2+)-ATPases were used. Redistribution was time- and temperature-dependent but independent of protein synthesis as well as the method of cell fusion. Intermixing occurred on a time scale of tens of minutes at 37 degrees C. These results verify the dynamic nature of the sarcoplasmic reticulum and illustrate an aspect of the special relationship between endoplasmic reticulum and sarcoplasmic reticulum.
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30

Sewall, Tommy C., and Jeffrey C. Pommerville. "The role of endoplasmic reticulum during gametogenesis in the aquatic fungus Allomyces macrogynus." Canadian Journal of Botany 69, no. 2 (February 1, 1991): 336–41. http://dx.doi.org/10.1139/b91-045.

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The Chytridiomycete Allomyces macrogynus generates new membranes for cleavage furrow and nuclear-cap formation during gametogenesis and zoosporogenesis. Transmission electron microscopy after impregnation with a mixture of zinc iodide and osmium tetroxide clearly demonstrated changes in the endoplasmic reticulum. Endoplasmic reticulum was intensely stained but did not appear to contribute to the formation of the unstained flagellar membranes or cleavage furrows. However, the relative cytoplasmic volume of endoplasmic reticulum decreased as positively stained nuclear-cap membrane formed. These observations are consistent with the hypothesis that flagellar membranes and cleavage furrows are derived from trans-Golgi equivalents, whereas the nuclear-cap membrane is derived from the endoplasmic reticulum. Key words: Allomyces macrogynus, Chytridiomycetes, endoplasmic reticulum, gametogenesis, zoosporogenesis.
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31

Kachar, B., and T. S. Reese. "The mechanism of cytoplasmic streaming in characean algal cells: sliding of endoplasmic reticulum along actin filaments." Journal of Cell Biology 106, no. 5 (May 1, 1988): 1545–52. http://dx.doi.org/10.1083/jcb.106.5.1545.

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Electron microscopy of directly frozen giant cells of characean algae shows a continuous, tridimensional network of anastomosing tubes and cisternae of rough endoplasmic reticulum which pervade the streaming region of their cytoplasm. Portions of this endoplasmic reticulum contact the parallel bundles of actin filaments at the interface with the stationary cortical cytoplasm. Mitochondria, glycosomes, and other small cytoplasmic organelles enmeshed in the endoplasmic reticulum network display Brownian motion while streaming. The binding and sliding of endoplasmic reticulum membranes along actin cables can also be directly visualized after the cytoplasm of these cells is dissociated in a buffer containing ATP. The shear forces produced at the interface with the dissociated actin cables move large aggregates of endoplasmic reticulum and other organelles. The combination of fast-freezing electron microscopy and video microscopy of living cells and dissociated cytoplasm demonstrates that the cytoplasmic streaming depends on endoplasmic reticulum membranes sliding along the stationary actin cables. Thus, the continuous network of endoplasmic reticulum provides a means of exerting motive forces on cytoplasm deep inside the cell distant from the cortical actin cables where the motive force is generated.
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Tsujimoto, Masafumi, Kazuma Aoki, Atsushi Ohnishi, and Yoshikuni Goto. "Endoplasmic Reticulum Aminopeptidase 1 beyond Antigenic Peptide-Processing Enzyme in the Endoplasmic Reticulum." Biological and Pharmaceutical Bulletin 43, no. 2 (February 1, 2020): 207–14. http://dx.doi.org/10.1248/bpb.b19-00857.

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Liu, Yimo, Junmarie Soto Burgos, Yan Deng, Renu Srivastava, Stephen H. Howell, and Diane C. Bassham. "Degradation of the Endoplasmic Reticulum by Autophagy during Endoplasmic Reticulum Stress in Arabidopsis." Plant Cell 24, no. 11 (November 2012): 4635–51. http://dx.doi.org/10.1105/tpc.112.101535.

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34

Walczak, Christopher P., Kaleena M. Bernardi, and Billy Tsai. "Endoplasmic Reticulum-Dependent Redox Reactions Control Endoplasmic Reticulum-Associated Degradation and Pathogen Entry." Antioxidants & Redox Signaling 16, no. 8 (April 15, 2012): 809–18. http://dx.doi.org/10.1089/ars.2011.4425.

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35

Yang, Xiaoling, Hua Xu, Yinju Hao, Li Zhao, Xin Cai, Jue Tian, Minghao Zhang, et al. "Endoplasmic reticulum oxidoreductin 1α mediates hepatic endoplasmic reticulum stress in homocysteine-induced atherosclerosis." Acta Biochimica et Biophysica Sinica 46, no. 10 (September 3, 2014): 902–10. http://dx.doi.org/10.1093/abbs/gmu081.

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36

Lewis, M. J., S. J. Turco, and M. Green. "Structure and assembly of the endoplasmic reticulum. Biosynthetic sorting of endoplasmic reticulum proteins." Journal of Biological Chemistry 260, no. 11 (June 1985): 6926–31. http://dx.doi.org/10.1016/s0021-9258(18)88868-8.

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37

Rieusset, Jennifer. "Mitochondria and endoplasmic reticulum: Mitochondria–endoplasmic reticulum interplay in type 2 diabetes pathophysiology." International Journal of Biochemistry & Cell Biology 43, no. 9 (September 2011): 1257–62. http://dx.doi.org/10.1016/j.biocel.2011.05.006.

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Paiement, Jacques, and John Bergeron. "The shape of things to come: Regulation of shape changes in endoplasmic reticulum." Biochemistry and Cell Biology 79, no. 5 (October 1, 2001): 587–92. http://dx.doi.org/10.1139/o01-143.

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Shape changes in the endoplasmic reticulum control fundamental cell processes including nuclear envelope assembly in mitotic cells, calcium homeostasis in cytoplasmic domains of secreting and motile cells, and membrane traffic in the early secretion apparatus between the endoplasmic reticulum and Golgi. Opposing forces of assembly (membrane fusion) and disassembly (membrane fragmentation) ultimately determine the size and shape of this organelle. This review examines some of the regulatory mechanisms involved in these processes and how they occur at specific sites or subcompartments of the endoplasmic reticulum.Key words: rough endoplasmic reticulum, smooth endoplasmic reticulum, shape changes, assembly, membrane fusion, organelle size, vesicle formation.
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Black, Virginia H., Archana Sanjay, Klaus van Leyen, Brett Lauring, and Gert Kreibich. "Cholesterol and Steroid Synthesizing Smooth Endoplasmic Reticulum of Adrenocortical Cells Contains High Levels of Proteins Associated with the Translocation Channel." Endocrinology 146, no. 10 (October 1, 2005): 4234–49. http://dx.doi.org/10.1210/en.2005-0372.

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Steroid-secreting cells are characterized by abundant smooth endoplasmic reticulum whose membranes contain many enzymes involved in sterol and steroid synthesis. Yet they have relatively little morphologically identifiable rough endoplasmic reticulum, presumably required for synthesis and maintenance of the smooth membranes. In this study, we demonstrate that adrenal smooth microsomal subfractions enriched in smooth endoplasmic reticulum membranes contain high levels of translocation apparatus and oligosaccharyltransferase complex proteins, previously thought confined to rough endoplasmic reticulum. We further demonstrate that these smooth microsomal subfractions are capable of effecting cotranslational translocation, signal peptide cleavage, and N-glycosylation of newly synthesized polypeptides. This shifts the paradigm for distinction between smooth and rough endoplasmic reticulum. Confocal microscopy revealed the proteins to be distributed throughout the abundant tubular endoplasmic reticulum in these cells, which is predominantly smooth surfaced. We hypothesize that the broadly distributed translocon and oligosaccharyltransferase proteins participate in local synthesis and/or quality control of membrane proteins involved in cholesterol and steroid metabolism in a sterol-dependent and hormonally regulated manner.
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Titorenko, Vladimir I., and Richard A. Rachubinski. "Mutants of the Yeast Yarrowia lipolyticaDefective in Protein Exit from the Endoplasmic Reticulum Are Also Defective in Peroxisome Biogenesis." Molecular and Cellular Biology 18, no. 5 (May 1, 1998): 2789–803. http://dx.doi.org/10.1128/mcb.18.5.2789.

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ABSTRACT Mutations in the SEC238 and SRP54 genes of the yeast Yarrowia lipolytica not only cause temperature-sensitive defects in the exit of the precursor form of alkaline extracellular protease and of other secretory proteins from the endoplasmic reticulum and in protein secretion but also lead to temperature-sensitive growth in oleic acid-containing medium, the metabolism of which requires the assembly of functionally intact peroxisomes. The sec238A andsrp54KO mutations at the restrictive temperature significantly reduce the size and number of peroxisomes, affect the import of peroxisomal matrix and membrane proteins into the organelle, and significantly delay, but do not prevent, the exit of two peroxisomal membrane proteins, Pex2p and Pex16p, from the endoplasmic reticulum en route to the peroxisomal membrane. Mutations in the PEX1 and PEX6 genes, which encode members of the AAA family of N-ethylmaleimide-sensitive fusion protein-like ATPases, not only affect the exit of precursor forms of secretory proteins from the endoplasmic reticulum but also prevent the exit of the peroxisomal membrane proteins Pex2p and Pex16p from the endoplasmic reticulum and cause the accumulation of an extensive network of endoplasmic reticulum membranes. None of the peroxisomal matrix proteins tested associated with the endoplasmic reticulum in sec238A,srp54KO, pex1-1, and pex6KO mutant cells. Our data provide evidence that the endoplasmic reticulum is required for peroxisome biogenesis and suggest that inY. lipolytica, the trafficking of some membrane proteins, but not matrix proteins, to the peroxisome occurs via the endoplasmic reticulum, results in their glycosylation within the lumen of the endoplasmic reticulum, does not involve transport through the Golgi, and requires the products encoded by the SEC238, SRP54,PEX1, and PEX6 genes.
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Chanat, E., P. Martin, and M. Ollivier-Bousquet. "Alpha(S1)-casein is required for the efficient transport of beta- and kappa-casein from the endoplasmic reticulum to the Golgi apparatus of mammary epithelial cells." Journal of Cell Science 112, no. 19 (October 1, 1999): 3399–412. http://dx.doi.org/10.1242/jcs.112.19.3399.

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In lactating mammary epithelial cells, interaction between caseins is believed to occur after their transport out of the endoplasmic reticulum. We show here that, in alpha(S1)-casein-deficient goats, the rate of transport of the other caseins to the Golgi apparatus is highly reduced whereas secretion of whey proteins is not significantly affected. This leads to accumulation of immature caseins in distended rough endoplasmic reticulum cisternae. Casein micelles, nevertheless, were still observed in secretory vesicles. In contrast, no accumulation was found in mammary epithelial cells which lack beta-casein. In mammary epithelial cells secreting an intermediate amount of alpha(S1)-casein, less casein accumulated in the rough endoplasmic reticulum, and the transport of alpha(S1)-casein to the Golgi occurred with kinetics similar to that of control cells. In prolactin-treated mouse mammary epithelial HC11 cells, which do not express alpha(S)-caseins, endoplasmic reticulum accumulation of beta-casein was also observed. The amount of several endoplasmic reticulum-resident proteins increased in conjunction with casein accumulation. Finally, the permeabilization of rough endoplasmic reticulum vesicles allowed the recovery of the accumulated caseins in soluble form. We conclude that optimal export of the caseins out of the endoplasmic reticulum is dependent upon alpha(S1)-casein. Our data suggest that alpha(S1)-casein interacts with the other caseins in the rough endoplasmic reticulum and that the formation of this complex is required for their efficient export to the Golgi.
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Sprong, Hein, Sophie Degroote, Tommy Nilsson, Masao Kawakita, Nobuhiro Ishida, Peter van der Sluijs, and Gerrit van Meer. "Association of the Golgi UDP-Galactose Transporter with UDP-Galactose:Ceramide Galactosyltransferase Allows UDP-Galactose Import in the Endoplasmic Reticulum." Molecular Biology of the Cell 14, no. 8 (August 2003): 3482–93. http://dx.doi.org/10.1091/mbc.e03-03-0130.

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UDP-galactose reaches the Golgi lumen through the UDP-galactose transporter (UGT) and is used for the galactosylation of proteins and lipids. Ceramides and diglycerides are galactosylated within the endoplasmic reticulum by the UDP-galactose:ceramide galactosyltransferase. It is not known how UDP-galactose is transported from the cytosol into the endoplasmic reticulum. We transfected ceramide galactosyltransferase cDNA into CHOlec8 cells, which have a defective UGT and no endogenous ceramide galactosyltransferase. Cotransfection with the human UGT1 greatly stimulated synthesis of lactosylceramide in the Golgi and of galactosylceramide in the endoplasmic reticulum. UDP-galactose was directly imported into the endoplasmic reticulum because transfection with UGT significantly enhanced synthesis of galactosylceramide in endoplasmic reticulum membranes. Subcellular fractionation and double label immunofluorescence microscopy showed that a sizeable fraction of ectopically expressed UGT and ceramide galactosyltransferase resided in the endoplasmic reticulum of CHOlec8 cells. The same was observed when UGT was expressed in human intestinal cells that have an endogenous ceramide galactosyltransferase. In contrast, in CHOlec8 singly transfected with UGT 1, the transporter localized exclusively to the Golgi complex. UGT and ceramide galactosyltransferase were entirely detergent soluble and form a complex because they could be coimmunoprecipitated. We conclude that the ceramide galactosyltransferase ensures a supply of UDP-galactose in the endoplasmic reticulum lumen by retaining UGT in a molecular complex.
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43

Zeng, J., Y. Y. Huang, X. M. Xu, S. H. Li, and Dongchuan Zuo. "Both Caspase and Calpain are Involved in Endoplasmic Reticulum-Targeted BNIP3-Induced Cell Death." Folia Biologica 66, no. 2 (2020): 60–66. http://dx.doi.org/10.14712/fb2020066020060.

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Bcl-2/E1B-19K-interacting protein 3 (BNIP3) is a member of the apoptotic B-cell lymphoma-2 family that regulates cell death. Although BNIP3 targeted normally to the mitochondrial outer membrane by its transmembrane domain was originally considered to be essential for its pro-apoptotic activity, accumulating evidence has shown that BNIP3 is localized to endoplasmic reticulum at physiological conditions and that forced expression of BNIP3 can initiate cell death via multiple pathways depending on the subcellular compartment it targets. Targeting BNIP3 to endoplasmic reticulum has been shown to participate in cell death during endoplasmic reticulum stress. However, the molecular events responsible for BNIP3-induced cell death in the endoplasmic reticulum remain poorly understood. In the present study, the transmembrane domain of BNIP3 was replaced with a segment of cytochrome b5 that targets BNIP3 into endoplasmic reticulum, which induced cell death as effectively as its wild-type molecule in the SW480 cell line (colon carcinoma). Furthermore, a pan-caspase inhibitor, z-VAD-fmk, and PD150606, a specific calpain inhibitor, both significantly suppressed the endoplasmic reticulum-targeted BNIP3- induced cell death. These results suggest that endoplasmic reticulum-targeted BNIP3 induced a mixed mode of cell death requiring both caspases and calpains.
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44

Millott, Robyn, Elzbieta Dudek, and Marek Michalak. "The endoplasmic reticulum in cardiovascular health and disease." Canadian Journal of Physiology and Pharmacology 90, no. 9 (September 2012): 1209–17. http://dx.doi.org/10.1139/y2012-058.

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The endoplasmic reticulum has an intricate network of pathways built to deal with the secretory and integral membrane protein synthesis demands of the cell, as well as adaptive responses set up for the endoplasmic reticulum to rely on when stressed. These pathways are both essential and complex, and because of these 2 factors, several situations can lead to a dysfunctional endoplasmic reticulum and result in a dysfunctional cell with the potential to contribute to the progression of disease. The endoplasmic reticulum has been implicated in several metabolic, neurodegenerative, inflammatory, autoimmune, and renal diseases and disorders, and in particular, cardiovascular diseases. The role of the endoplasmic reticulum in cardiovascular disease shows how the change in function of a particular microscopic organelle can lead to macroscopic changes in the form of disease.
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45

Ekici, Nuran, Feruzan Dane, and Göksel Olgun. "Ultrastructural features of Mimulus aurantiacus (Scrophulariaceae) pollen tubes in vivo." Anais da Academia Brasileira de Ciências 81, no. 1 (March 2009): 29–37. http://dx.doi.org/10.1590/s0001-37652009000100005.

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The aim of this study is to give information on ultrastructure of in vivo pollen tubes of Mimulus aurantiacus which were collected from the Botanical Garden of the University of California at Berkeley. Materials were prepared according to electron microscopy methods and examined under Zeiss electron microscope. Four zones were examined in the pollen tubes of Mimulus aurantiacus. APICAL ZONE: Mitochondria, smooth endoplasmic reticulum, rough endoplasmic reticulum, dictyosomes and secretory vesicles were observed. SUBAPICAL ZONE: This area contained abundant rough endoplasmic reticulum and occasionally some smooth endoplasmic reticulum. The polysomes, mitochondria, proplastids that contain starch, small vacuoles and a few lipid bodies were detected. NUCLEAR ZONE: Both generative and vegetative cell nuclei lie in this zone. The vegetative cell nucleus was large and long. Rough endoplasmic reticulum, mitochondria, ribosomes, dictyosomes, and amyloplasts that are rich of starch were observed. VACUOLATION AND PLUG FORMATION ZONE: Cytoplasm of the tubes was full of large vacuoles. Few organelles such as mitochondria, dictyosome and rough endoplasmic reticulum were detected along their periphery.
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46

Fliegel, Larry, Kimberly Burns, Ken Wlasichuk, and Marek Michalak. "Peripheral membrane proteins of sarcoplasmic and endoplasmic reticulum. Comparison of carboxyl-terminal amino acid sequences." Biochemistry and Cell Biology 67, no. 10 (October 1, 1989): 696–702. http://dx.doi.org/10.1139/o89-104.

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Peripheral endoplasmic reticulum membrane proteins residing in the lumen of the endoplasmic reticulum occupy the same space as other secreted proteins. The presence of a four amino acid salvage or retention signal (KDEL-COOH = Lys-Asp-Glu-Leu-COOH) at the carboxyl-terminal end of peripheral membrane proteins has been shown to represent a signal or an essential part of a signal for their retention within the endoplasmic reticulum membrane. In heart and skeletal muscle, a number of sarcoplasmic reticulum proteins have recently been identified which are peripheral membrane proteins. The high-affinity calcium-binding protein (55 kilodaltons (kDa)) appears to conform to the above described mechanisms and contains the KDEL carboxyl-terminal tetrapeptide. Thyroid hormone binding protein is present in the sarcoplasmic reticulum, in addition to its endoplasmic reticulum location, and has a modified but related tetrapeptide sequence (RDEL = Arg-Asp-Glu-Leu), which also probably functions as the retention signal. Calsequestrin and a 53-kDa glycoprotein, two other peripheral membrane proteins residing in the lumen of the sarcoplasmic reticulum, do not contain the KDEL retention signal. The sarcoplasmic reticulum may have developed a unique retention mechanism(s) for these muscle-specific proteins.Key words: sarcoplasmic reticulum, endoplasmic reticulum, amino acid sequences, peripheral membrane proteins, KDEL retention sequence.
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47

VLIES, Dennis van der, Eward H. W. PAP, Jan Andries POST, Julio E. CELIS, and Karel W. A. WIRTZ. "Endoplasmic reticulum resident proteins of normal human dermal fibroblasts are the major targets for oxidative stress induced by hydrogen peroxide." Biochemical Journal 366, no. 3 (September 15, 2002): 825–30. http://dx.doi.org/10.1042/bj20020618.

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The membrane-permeable fluorescein-labelled tyramine conjugate (acetylTyrFluo) was used to identify the proteins of normal human dermal fibroblasts most susceptible to oxidation by hydrogen peroxide [Van der Vlies, Wirtz and Pap (2001) Biochemistry 40, 7783—7788]. By exposing the cells to H2O2 (0.1mM for 10min), TyrFluo was covalently linked to target proteins. TyrFluo-labelled and [35S]Met-labelled cell lysates were mixed and subjected to two-dimensional PAGE. After Western blotting the 35S-labelled proteins were visualized by autoradiography and the TyrFluo-labelled proteins by using anti-fluorescein antibody. The TyrFluo-labelled proteins were matched with the 35S-labelled proteins and identified by comparison with our mastermap of proteins. Protein disulphide isomerase (PDI), IgG-binding protein (BiP), calnexin, endoplasmin and glucose-regulated protein 58 (endoplasmic reticulum protein 57/GRP58) were identified as targets of oxidation. All these proteins reside in the endoplasmic reticulum and are part of the protein folding machinery. In agreement, confocal laser scanning microscopy showed co-localization of TyrFluo-labelled proteins and the KDEL receptor ERD-2, a marker for the endoplasmic reticulum.
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48

Liang, Wu-Lin, Meng-Ru Cai, Ming-Qian Zhang, Shuang Cui, Tian-Rui Zhang, Wen-Hao Cheng, Yong-Hong Wu, Wen-Jing Ou, Zhan-Hong Jia, and Shuo-Feng Zhang. "Chinese Herbal Medicine Alleviates Myocardial Ischemia/Reperfusion Injury by Regulating Endoplasmic Reticulum Stress." Evidence-Based Complementary and Alternative Medicine 2021 (December 7, 2021): 1–17. http://dx.doi.org/10.1155/2021/4963346.

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Myocardial ischemia/reperfusion injury is the main cause of increased mortality and disability in cardiovascular diseases. The injury involves many pathological processes, such as oxidative stress, calcium homeostasis imbalance, inflammation, and energy metabolism disorders, and these pathological stimuli can activate endoplasmic reticulum stress. In the early stage of ischemia, endoplasmic reticulum stress alleviates the injury as an adaptive survival response, but the long-term stress on endoplasmic reticulum amplifies oxidative stress, inflammation, and calcium overload to accelerate cell damage and apoptosis. Therefore, regulation of endoplasmic reticulum stress may be a mechanism to improve ischemia/reperfusion injury. Chinese herbal medicine has a long history of clinical application and unique advantages in the treatment of ischemic heart diseases. This review focuses on the effect of Chinese herbal medicine on myocardial ischemia/reperfusion injury from the perspective of regulation of endoplasmic reticulum stress.
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Dong, Yunzhou, Conrad Fernandes, Yanjun Liu, Yong Wu, Hao Wu, Megan L. Brophy, Lin Deng, et al. "Role of endoplasmic reticulum stress signalling in diabetic endothelial dysfunction and atherosclerosis." Diabetes and Vascular Disease Research 14, no. 1 (October 20, 2016): 14–23. http://dx.doi.org/10.1177/1479164116666762.

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It is well established that diabetes mellitus accelerates atherosclerotic vascular disease. Endothelial injury has been proposed to be the initial event in the pathogenesis of atherosclerosis. Endothelium not only acts as a semi-selective barrier but also serves physiological and metabolic functions. Diabetes or high glucose in circulation triggers a series of intracellular responses and organ damage such as endothelial dysfunction and apoptosis. One such response is high glucose-induced chronic endoplasmic reticulum stress in the endothelium. The unfolded protein response is an acute reaction that enables cells to overcome endoplasmic reticulum stress. However, when chronically persistent, endoplasmic reticulum stress response could ultimately lead to endothelial dysfunction and atherosclerosis. Herein, we discuss the scientific advances in understanding endoplasmic reticulum stress-induced endothelial dysfunction, the pathogenesis of diabetes-accelerated atherosclerosis and endoplasmic reticulum stress as a potential target in therapies for diabetic atherosclerosis.
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Alam, Rashedul, Mohammad Mamun Ur Rashid, Mohammad Fazlul Kabir, and Hyung-Ryong Kim. "Endoplasmic reticulum stress and organoids." Organoid 1 (January 31, 2021): e3. http://dx.doi.org/10.51335/organoid.2021.1.e3.

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Organoids represent an advanced tool in cell biology and have redefined biomedical research. Organoids are ideal for studies of biological processes, pharmacological studies, and therapeutic research to imitate pathological processes and preserve genetic integrity. The endoplasmic reticulum (ER) is the central organelle responsible for protein folding, post-translational adaptations, and membrane and luminal protein transportation. ER stress is a disorder influenced by a range of physiological and pathological causes, such as nutrient deficiency, impaired glycosylation, calcium depletion, oxidative stress, DNA damage, and energy disruption. Disturbance of the ER environment triggers aggregation of unfolded/misfolded proteins, accelerating ER stress. The unfolded protein response (UPR) is a transduction mechanism that activates cells in response to ER stress to restore ER homeostasis, altering cancer development and progression. However, the mechanisms through which sustained and unresolved UPR signaling triggers a switch from pro-survival to pro-death pathways remain unclear. Immutable and environmental stimuli that modify protein homeostasis are often incorporated into tumor cells, thereby generating ER stress. Herein, we discuss challenges and advances in fundamental and clinical cancer studies on ER stress. Additionally, current trends in organoid technology are summarized to fill the gap in our knowledge of the relationship between cancer and ER stress, with the UPR representing a future tool for investigating drug response screening and potentially revolutionizing the workflow of new cancer drug development.
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