The UPR in atherosclerosis

Zhou, Alex X.; Tabas, Ira

doi:10.1007/s00281-013-0372-x

Cited by 121Endoplasmic Reticulum Stress and DiseaseAtherosclerosis and Cardiovascular DiseasesIon Channels and Receptors

The UPR in atherosclerosis

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Zhou, Alex X., Tabas, Ira·2013·Seminars in Immunopathology

DOI 10.1007/s00281-013-0372-xPMC PMC3967405

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Abstract

Multiple systemic factors and local stressors in the arterial wall can disturb the functions of endoplasmic reticulum (ER), causing ER stress in endothelial cells (ECs), smooth muscle cells (SMCs), and macrophages during the initiation and progression of atherosclerosis. As a protective response to restore ER homeostasis, the unfolded protein response (UPR) is initiated by three major ER sensors: protein kinase RNA-like ER kinase (PERK), inositol-requiring protein 1α (IRE1α), and activating transcription factor 6 (ATF6). The activation of the various UPR signaling pathways displays a temporal pattern of activation at different stages of the disease. The ATF6 and IRE1α pathways that promote the expression of protein chaperones in ER are activated in ECs in athero-susceptible regions of pre-lesional arteries and before the appearance of foam cells. The PERK pathway that reduces ER protein client load by blocking protein translation is activated in SMCs and macrophages in early lesions. The activation of these UPR signaling pathways aims to cope with the ER stress and plays a pro-survival role in the early stage of atherosclerosis. However, with the progression of atherosclerosis, the extended duration and increased intensity of ER stress in lesions lead to prolonged and enhanced UPR signaling. Under this circumstance, the PERK pathway induces expression of death effectors, and possibly IRE1α activates apoptosis signaling pathways, leading to apoptosis of macrophages and SMCs in advanced lesions. Importantly, UPR-mediated cell death is associated with plaque instability and the clinical progression of atherosclerosis. Moreover, UPR signaling is linked to inflammation and possibly to macrophage differentiation in lesions. Therapeutic approaches targeting the UPR may have promise in the prevention and/or regression of atherosclerosis. However, more progress is needed to fully understand all of the roles of the UPR in atherosclerosis and to harness this information for therapeutic advances.

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In atherosclerotic plaques, there is evidence of UPR activation.
“Moreover, in the atherosclerotic plaques, there is evidence of UPR activation [419].”
From GANAB and N-Glycans Substrates Are Relevant in Human Physiology, Polycystic Pathology and Multiple Sclerosis: A Review (2022) · cites this paper as [419]

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Chiribau, C.-B., Gaccioli, F., Huang, C. C., Yuan, C. L., & Hatzoglou, M. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.01507-09 · Cited by 104 · see citing works
Free cholesterol overloading induced smooth muscle cells death and activated both ER- and mitochondrial-dependent death pathway
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High Dietary Taurine Reduces Apoptosis and Atherosclerosis in the Left Main Coronary Artery
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Peptides derived from the bifunctional kinase/RNase enzyme IRE1α modulate IRE1α activity and protect cells from endoplasmic reticulum stress
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Involvement of Endoplasmic Stress Protein C/EBP Homologous Protein in Arteriosclerosis Acceleration With Augmented Biological Stress Responses
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Coronary Artery Endothelial Transcriptome In Vivo
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Hyperhomocysteinemia induced by methionine supplementation does not independently cause atherosclerosis in C57BL/6J mice
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Blockade of Oxidized LDL-Triggered Endothelial Apoptosis by Quercetin and Rutin through Differential Signaling Pathways Involving JAK2
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Induction of the unfolded protein response after monocyte to macrophage differentiation augments cell survival in early atherosclerotic lesions
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M2 macrophages exhibit higher sensitivity to oxLDL-induced lipotoxicity than other monocyte/macrophage subtypes
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Quercetin protects macrophages from oxidized low-density lipoprotein-induced apoptosis by inhibiting the endoplasmic reticulum stress-C/EBP homologous protein pathway
Yao, S., Sang, H., Song, G., Yang, N., Liu, Q., Zhang, Y., Jiao, P., Zong, C., & Qin, S. (2012) · Experimental Biology and Medicine · doi:10.1258/ebm.2012.012027 · Cited by 41 · see citing works
Is homocysteine important as risk factor for coronary heart disease?
Cesari, M., Rossi, G. P., Sticchi, D., & Pessina, A. C. (2005) · Nutrition Metabolism and Cardiovascular Diseases · doi:10.1016/j.numecd.2004.04.002 · Cited by 39 · see citing works
Paraoxonase-2 Modulates Stress Response of Endothelial Cells to Oxidized Phospholipids and a Bacterial Quorum–Sensing Molecule
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Amelioration of Glucolipotoxicity-Induced Endoplasmic Reticulum Stress by a “Chemical Chaperone” in Human THP-1 Monocytes
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Vascular oxidative stress, nitric oxide and atherosclerosis
Li, H., Horke, S., & Förstermann, U. (2014) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2014.09.001 · Cited by 656 · see citing works
A Molecular Web: Endoplasmic Reticulum Stress, Inflammation, and Oxidative Stress
Chaudhari, N., Talwar, P., Parimisetty, A., Lefebvre dâ€™Hellencourt, C., & Ravanan, P. (2014) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2014.00213 · Cited by 600 · see citing works
Molecular Mechanisms of Acrolein Toxicity: Relevance to Human Disease
Moghe, A., Ghare, S. S., Lamoreau, B., Mohammad, M., Barve, S. S., McClain, C. J., & Joshi‐Barve, S. (2015) · Toxicological Sciences · doi:10.1093/toxsci/kfu233 · Cited by 513 · see citing works
Targeting IRE1 with small molecules counteracts progression of atherosclerosis
Tufanlı, Ö., Telkoparan‐Akillilar, P., Acosta‐Alvear, D., Kocatürk, B., Onat, U. İ., Hamid, S. M., Çimen, İ., Walter, P., Weber, C., & Erbay, E. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1621188114 · Cited by 192 · see citing works
Impact of high cholesterol and endoplasmic reticulum stress on metabolic diseases: An updated mini-review
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The UPR Activator ATF6 Responds to Proteotoxic and Lipotoxic Stress by Distinct Mechanisms
Tam, A. B., Roberts, L. S., Chandra, V. K., Rivera, I. G., Nomura, D. K., Forbes, D. J., & Niwa, M. (2018) · Developmental Cell · doi:10.1016/j.devcel.2018.04.023 · Cited by 180 · see citing works
ER Stress and Angiogenesis
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Scavenger Receptor-A (CD204): A Two-Edged Sword in Health and Disease
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The Role of Damage-Associated Molecular Patterns (DAMPs) in Human Diseases : Part II: DAMPs as diagnostics, prognostics and therapeutics in clinical medicine
Land, W. G. (2015) · Sultan Qaboos University medical journal · doi:10.18295/2075-0528.1676 · Cited by 153 · see citing works
Homeostasis control in health and disease by the unfolded protein response
Acosta‐Alvear, D., Harnoss, J. M., Walter, P., & Ashkenazi, A. (2024) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-024-00794-0 · Cited by 139 · see citing works
ER Stress Activates the NLRP3 Inflammasome: A Novel Mechanism of Atherosclerosis
Chen, X.-N., Guo, X.-C., Ge, Q., Zhao, Y.-X., Mu, H., & Zhang, J.-P. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/3462530 · Cited by 125 · see citing works
Macrophage Apoptosis and Necrotic Core Development in Atherosclerosis: A Rapidly Advancing Field with Clinical Relevance to Imaging and Therapy
González, L., & Trigatti, B. L. (2016) · Canadian Journal of Cardiology · doi:10.1016/j.cjca.2016.12.010 · Cited by 130 · see citing works
IRE1α–XBP1 signaling in leukocytes controls prostaglandin biosynthesis and pain
Chopra, S., Giovanelli, P., Alvarado-Vazquez, P. A., Alonso, S., Song, M., Sandoval, T. A., Chae, C.-S., Tan, C., Fonseca, M. M., Gutierrez, S., et al. (2019) · Science · doi:10.1126/science.aau6499 · Cited by 125 · see citing works
The Role of Endoplasmic Reticulum Stress in Cardiovascular Disease and Exercise
Hong, J., Kim, K., Kim, J.-H., & Park, Y. (2017) · International Journal of Vascular Medicine · doi:10.1155/2017/2049217 · Cited by 114 · see citing works
Causes and consequences of endoplasmic reticulum stress in rheumatic disease
Navid, F., & Colbert, R. A. (2016) · Nature Reviews Rheumatology · doi:10.1038/nrrheum.2016.192 · Cited by 108 · see citing works
Prevention of atherosclerosis by bioactive palmitoleate through suppression of organelle stress and inflammasome activation
Çimen, İ., Kocatürk, B., Koyuncu, S., Tufanlı, Ö., Onat, U. İ., Yıldırım, A., Apaydın, O., Demirsoy, Ş., Aykut, G., Nguyen, U. T., et al. (2016) · Science Translational Medicine · doi:10.1126/scitranslmed.aaf9087 · Cited by 104 · see citing works
Endoplasmic Reticulum Stress Promotes Macrophage-derived Foam Cell Formation by Up-regulating Cluster of Differentiation 36 (CD36) Expression
Yao, S., Miao, C., Tian, H., Sang, H., Yang, N., Jiao, P., Han, J., Zong, C., & Qin, S. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.524512 · Cited by 104 · see citing works
Catalpol Inhibits Homocysteine-induced Oxidation and Inflammation via Inhibiting Nox4/NF-κB and GRP78/PERK Pathways in Human Aorta Endothelial Cells
Hu, H., Wang, C., Jin, Y., Meng, Q., Liu, Q., Liu, Z., Liu, K., Liu, X., & Sun, H. (2018) · Inflammation · doi:10.1007/s10753-018-0873-9 · Cited by 103 · see citing works
Basic mechanisms in endoplasmic reticulum stress and relation to cardiovascular diseases
Sözen, E., Karademir-Yilmaz, B., & Özer, N. K. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.09.031 · Cited by 100 · see citing works
Natural products targeting ER stress pathway for the treatment of cardiovascular diseases
Choy, K., Murugan, D., & Mustafa, M. (2018) · Pharmacological Research · doi:10.1016/j.phrs.2018.04.013 · Cited by 95 · see citing works
Intercepting the Lipid-Induced Integrated Stress Response Reduces Atherosclerosis
Onat, U. İ., Yıldırım, A., Tufanlı, Ö., Çimen, İ., Kocatürk, B., Veli, Z., Hamid, S. M., Shimada, K., Chen, S., Sin, J., et al. (2019) · Journal of the American College of Cardiology · doi:10.1016/j.jacc.2018.12.055 · Cited by 84 · see citing works
Endoplasmic reticulum stress-induced hepatic stellate cell apoptosis through calcium-mediated JNK/P38 MAPK and Calpain/Caspase-12 pathways
Huang, Y., Li, X., Wang, Y., Wang, H., Huang, C. Z., & Li, J. (2014) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-014-2073-8 · Cited by 79 · see citing works
Dickkopf1 destabilizes atherosclerotic plaques and promotes plaque formation by inducing apoptosis of endothelial cells through activation of ER stress
Di, M., Wang, L., Li, M., Zhang, Y., Liu, X., Zeng, R., Wang, H., Chen, Y., Chen, W., Zhang, Y., et al. (2017) · Cell Death and Disease · doi:10.1038/cddis.2017.277 · Cited by 74 · see citing works
Endoplasmic reticulum stress in hepatic steatosis and inflammatory bowel diseases
Guo, B., & Li, Z. (2014) · Frontiers in Genetics · doi:10.3389/fgene.2014.00242 · Cited by 73 · see citing works
Calcium signalling and ER stress in insulin resistance and atherosclerosis
Özcan, L., & Tabas, I. A. (2016) · Journal of Internal Medicine · doi:10.1111/joim.12562 · Cited by 68 · see citing works
Self-citation
Endoplasmic Reticulum Stress Effector CCAAT/Enhancer‐binding Protein Homologous Protein (CHOP) Regulates Chronic Kidney Disease–Induced Vascular Calcification
Miyazaki‐Anzai, S., Masuda, M., Demos-Davies, K. M., Keenan, A. L., Saunders, S. J., Masuda, R., Jablonski, K., Cavasin, M. A., Kendrick, J., Chonchol, M., et al. (2014) · Journal of the American Heart Association · doi:10.1161/jaha.114.000949 · Cited by 64 · see citing works
Activation of aldehyde dehydrogenase 2 slows down the progression of atherosclerosis via attenuation of ER stress and apoptosis in smooth muscle cells
Yang, M., Wang, Y., Han, B., Yang, B. Y., Qiang, Y.-W., Zhang, Y., Wang, Z., Huang, X. S., Liu, J., Chen, Y., et al. (2017) · Acta Pharmacologica Sinica · doi:10.1038/aps.2017.81 · Cited by 63 · see citing works
NF-κB and its crosstalk with endoplasmic reticulum stress in atherosclerosis
Li, W., Jin, K., Luo, J., Xu, W., Wu, Y., Zhou, J., Wang, Y., Xu, R., Jiao, L., Wang, T., et al. (2022) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2022.988266 · Cited by 64 · see citing works
Endoplasmic Reticulum Stress Pathway, the Unfolded Protein Response, Modulates Immune Function in the Tumor Microenvironment to Impact Tumor Progression and Therapeutic Response
Ramirez, M. U., Hernandez, S. R., Soto‐Pantoja, D. R., & Cook, K. L. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms21010169 · Cited by 62 · see citing works
Protein Thiol Redox Signaling in Monocytes and Macrophages
Short, J. D., Downs, K. P., Tavakoli, S., & Asmis, R. (2016) · Antioxidants and Redox Signaling · doi:10.1089/ars.2016.6697 · Cited by 58 · see citing works
Posttranscriptional and transcriptional regulation of endothelial nitric-oxide synthase during hypoxia: the role of microRNAs
Kalinowski, L., Janaszak‐Jasiecka, A., Siekierzycka, A., Bartoszewska, S., Woźniak, M., Lejnowski, D., Collawn, J. F., & Bartoszewski, R. (2016) · Cellular & Molecular Biology Letters · doi:10.1186/s11658-016-0017-x · Cited by 59 · see citing works
The effects of endoplasmic reticulum stress inducer thapsigargin on the toxicity of ZnO or TiO 2 nanoparticles to human endothelial cells
Gu, Y., Cheng, S., Chen, G., Shen, Y., Li, X., Jiang, Q. L., Li, J., & Cao, Y. (2016) · Toxicology Mechanisms and Methods · doi:10.1080/15376516.2016.1273429 · Cited by 57 · see citing works
Protein aggregation, cardiovascular diseases, and exercise training: Where do we stand?
Gouveia, M., Xia, K., Colón, W., Vieira, S. I., & Ribeiro, F. (2017) · Ageing Research Reviews · doi:10.1016/j.arr.2017.07.005 · Cited by 54 · see citing works
Experimental reconstitution of chronic ER stress in the liver reveals feedback suppression of BiP mRNA expression
Gomez, J. A., & Rutkowski, D. T. (2016) · eLife · doi:10.7554/elife.20390 · Cited by 52 · see citing works
Possible role of fibroblast growth factor 21 on atherosclerosis via amelioration of endoplasmic reticulum stress-mediated apoptosis in apoE−/− mice
Wu, X., Qi, Y., Chang, J.-R., Lu, W., Zhang, J., Wang, S., Cheng, S., Zhang, M., Fan, Q., Lv, Y., et al. (2014) · Heart and Vessels · doi:10.1007/s00380-014-0557-9 · Cited by 51 · see citing works
Scutellarin exerts protective effects against atherosclerosis in rats by regulating the Hippo–FOXO3A and PI3K/AKT signaling pathways
Fu, Y., Sun, S., Sun, H., Peng, J., Ma, X., Bao, L., Ji, R., Luo, C., Gao, C., Zhang, X., et al. (2019) · Journal of Cellular Physiology · doi:10.1002/jcp.28446 · Cited by 48 · see citing works
Pathological Crosstalk Between Oxidized LDL and ER Stress in Human Diseases: A Comprehensive Review
Varghese, D. S., & Ali, B. R. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.674103 · Cited by 48 · see citing works
Methamphetamine-mediated endoplasmic reticulum (ER) stress induces type-1 programmed cell death in astrocytes via ATF6, IRE1α and PERK pathways
Shah, A. B., & Kumar, A. (2016) · Oncotarget · doi:10.18632/oncotarget.10025 · Cited by 45 · see citing works
Unfolded protein response signaling impacts macrophage polarity to modulate breast cancer cell clearance and melanoma immune checkpoint therapy responsiveness
Soto‐Pantoja, D. R., Wilson, A. S., Clear, K. Y. J., Westwood, B. M., Triozzi, P. L., & Cook, K. L. (2017) · Oncotarget · doi:10.18632/oncotarget.19849 · Cited by 43 · see citing works
Dickkopf Homolog 3 Induces Stem Cell Differentiation into Smooth Muscle Lineage via ATF6 Signalling
Wang, X., Karamariti, E., Simpson, R., Wang, W., & Xu, Q. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.641415 · Cited by 41 · see citing works
Catestatin improves insulin sensitivity by attenuating endoplasmic reticulum stress: In vivo and in silico validation
Dasgupta, A., Bandyopadhyay, G. K., Ray, I., Bandyopadhyay, K., Chowdhury, N., De, R. K., & Mahata, S. K. (2020) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2020.02.005 · Cited by 41 · see citing works
ER Protein Quality Control and the Unfolded Protein Response in the Heart
Arrieta, A., Blackwood, E. A., & Glembotski, C. C. (2017) · Current topics in microbiology and immunology · doi:10.1007/82_2017_54 · Cited by 39 · see citing works
Intercepting IRE1 kinase‐FMRP signaling prevents atherosclerosis progression
Yıldırım, Z., Baboo, S., Hamid, S. M., Atici, A. E., Tufanlı, Ö., Robichaud, S., Emerton, C., Diedrich, J. K., Vatandaslar, H., Nikolos, F., et al. (2022) · EMBO Molecular Medicine · doi:10.15252/emmm.202115344 · Cited by 35 · see citing works
Unfolded protein response in cardiovascular disease
Kubra, K., Akhter, M. S., Uddin, M. A., & Barabutis, N. (2020) · Cellular Signalling · doi:10.1016/j.cellsig.2020.109699 · Cited by 36 · see citing works
The Impact of Intermittent and Repetitive Cold Stress Exposure on Endoplasmic Reticulum Stress and Instability of Atherosclerotic Plaques
Dai, M.-X., Xiao-hui, Z., Yu, J. M., Yin, T., Ma, M., Zhang, L., Liu, M., Ma, Y., Liu, L., Gao, X., et al. (2014) · Cellular Physiology and Biochemistry · doi:10.1159/000363008 · Cited by 34 · see citing works
Atorvastatin attenuates atherosclerotic plaque destabilization by inhibiting endoplasmic reticulum stress in hyperhomocysteinemic mice
JIA, F., Wu, C., Zhenyue, C., Lü, G., & Sun, J. (2016) · Molecular Medicine Reports · doi:10.3892/mmr.2016.4975 · Cited by 34 · see citing works
Protein-rich foods, sea foods, and gut microbiota amplify immune responses in chronic diseases and cancers – Targeting PERK as a novel therapeutic strategy for chronic inflammatory diseases, neurodegenerative disorders, and cancer
Saaoud, F., Lu, Y., Xu, K., Shao, Y., Praticò, D., Vázquez-Padrón, R. I., Wang, H., & Yang, X. (2024) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2024.108604 · Cited by 33 · see citing works
Hypoxia triggers endothelial endoplasmic reticulum stress and apoptosis via induction of VLDL receptor
Yang, D., Gao, L., Wang, T., Qiao, Z., Liang, Y., & Zhang, P. (2014) · FEBS Letters · doi:10.1016/j.febslet.2014.09.046 · Cited by 31 · see citing works
Toll-Like Receptor 4: A Macrophage Cell Surface Receptor Is Activated By Trimethylamine-N-Oxide.
Hakhamaneshi, M. S., Abdolahi, A., Vahabzadeh, Z., Abdi, M., & Andalibi, P. (2021) · PubMed Central · doi:10.22074/cellj.2021.7849 · Cited by 29 · see citing works
A Deficiency of Herp, an Endoplasmic Reticulum Stress Protein, Suppresses Atherosclerosis in ApoE Knockout Mice by Attenuating Inflammatory Responses
Shinozaki, S., Chiba, T., Kokame, K., Miyata, T., Kaneko, E., & Shimokado, K. (2013) · PLoS ONE · doi:10.1371/journal.pone.0075249 · Cited by 28 · see citing works
Sphingosine-1-Phosphate Receptor 1, Expressed in Myeloid Cells, Slows Diet-Induced Atherosclerosis and Protects against Macrophage Apoptosis in Ldlr KO Mice
González, L., Qian, A. S., Tahir, U., Yu, P., & Trigatti, B. L. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18122721 · Cited by 28 · see citing works
8-Chloroadenosine induces apoptosis in human coronary artery endothelial cells through the activation of the unfolded protein response
Tang, V., Fu, S., Rayner, B. S., & Hawkins, C. L. (2019) · Redox Biology · doi:10.1016/j.redox.2019.101274 · Cited by 28 · see citing works
Activation of the unfolded protein response downregulates cardiac ion channels in human induced pluripotent stem cell-derived cardiomyocytes
Liu, M., Shi, G., Zhou, A., Rupert, C. E., Coulombe, K. L. K., & Dudley, S. C. (2018) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2018.02.011 · Cited by 26 · see citing works
Self-citation
Endoplasmic reticulum stress in perivascular adipose tissue promotes destabilization of atherosclerotic plaque by regulating GM-CSF paracrine
Ying, R., Li, S., Chen, J., Zhang, H., Yang, Y., Gu, Z.-J., Chen, Y., & Wang, J. (2018) · Journal of Translational Medicine · doi:10.1186/s12967-018-1481-z · Cited by 26 · see citing works
Rosuvastatin protects against endothelial cell apoptosis in vitro and alleviates atherosclerosis in ApoE‑/‑ mice by suppressing endoplasmic reticulum stress
Geng, J., Xu, H., Fu, W., Yu, X., Xu, G., Cao, H., Lin, G., & Sui, D. (2020) · Experimental and Therapeutic Medicine · doi:10.3892/etm.2020.8733 · Cited by 26 · see citing works
Trimethylamine N-oxide promotes PERK-mediated endothelial-mesenchymal transition and apoptosis thereby aggravates atherosclerosis
Wang, B., Jun, Q., Bingyang, L., Xi, Y., Jianqing, Z., & Jiangfang, L. (2024) · International Immunopharmacology · doi:10.1016/j.intimp.2024.113209 · Cited by 25 · see citing works
Endoplasmic Reticulum Membrane Homeostasis and the Unfolded Protein ResponsePreprint
Ernst, R., Renne, M. F., Jain, A., & von der Malsburg, A. (2024) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a041400 · Cited by 25 · see citing works
Ca2+ Flux: Searching for a Role in Efferocytosis of Apoptotic Cells in Atherosclerosis
Tajbakhsh, A., Kovanen, P. T., Rezaee, M., Banach, M., & Sahebkar, A. (2019) · Journal of Clinical Medicine · doi:10.3390/jcm8122047 · Cited by 24 · see citing works
Ethanol extract of propolis protects macrophages from oxidized low density lipoprotein-induced apoptosis by inhibiting CD36 expression and endoplasmic reticulum stress-C/EBP homologous protein pathway
Tian, H., Sun, H., Zhang, J., Zhang, X., Zhao, L., Guo, S., Li, Y., Jiao, P., Wang, H., Qin, S.-C., et al. (2015) · BMC Complementary and Alternative Medicine · doi:10.1186/s12906-015-0759-4 · Cited by 24 · see citing works
The Modulation of Endoplasmic Reticulum Stress by Chemical Chaperone Upregulates Immune Negative Cytokine IL-35 in Apolipoprotein E-Deficient Mice
Wang, B., Dai, S., Dong, Z., Sun, Y., Song, X., Guo, C., Zhu, F., Wang, Q., & Zhang, L. (2014) · PLoS ONE · doi:10.1371/journal.pone.0087787 · Cited by 23 · see citing works
Atherosclerosis in HIV Patients: What Do We Know so Far?
Poznyak, A. V., Bezsonov, E. E., Borisov, E. E., Grechko, A. V., Kartuesov, A. G., & Orekhov, A. N. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23052504 · Cited by 22 · see citing works
Pharmacological evidence for a role of the transient receptor potential canonical 3 (TRPC3) channel in endoplasmic reticulum stress-induced apoptosis of human coronary artery endothelial cells
Ampem, P. T., Smedlund, K., & Vázquez, G. (2015) · Vascular Pharmacology · doi:10.1016/j.vph.2015.07.011 · Cited by 22 · see citing works
Aging and Hypercholesterolemia Differentially Affect the Unfolded Protein Response in the Vasculature of ApoE −/− Mice
Zhou, Y., Wan, X., Seidel, K., Zhang, M., Goodman, J. B., Seta, F., Hamburg, N. M., & Han, J. (2021) · Journal of the American Heart Association · doi:10.1161/jaha.120.020441 · Cited by 21 · see citing works
Berberine Attenuates Macrophages Infiltration in Intracranial Aneurysms Potentially Through FAK/Grp78/UPR Axis
Quan, K., Li, S., Wang, D., Shi, Y., Yang, Z., Song, J., Tian, Y., Liu, Y., Fan, Z., & Zhu, W. P. (2018) · Frontiers in Pharmacology · doi:10.3389/fphar.2018.00565 · Cited by 20 · see citing works
GANAB and N-Glycans Substrates Are Relevant in Human Physiology, Polycystic Pathology and Multiple Sclerosis: A Review
De Masi, R., & Orlando, S. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23137373 · Cited by 20 · see citing works
“Moreover, in the atherosclerotic plaques, there is evidence of UPR activation [419].”
Background
AIP1-Mediated Stress Signaling in Atherosclerosis and Arteriosclerosis
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Brain Endoplasmic Reticulum Stress Mechanistically Distinguishes the Saline-Intake and Hypertensive Response to Deoxycorticosterone Acetate–Salt
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Salubrinal attenuated retinal neovascularization by inhibiting CHOP-HIF1α-VEGF pathways
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Overexpression of CREB protein protects from tunicamycin-induced apoptosis in various rat cell types
Balogh, A., Németh, M., Koloszár, I., Markó, L., Przybyl, L., Jinno, K., Szigeti, C., Heffer, M., Gebhardt, M., Szeberényi, J., et al. (2014) · Apoptosis · doi:10.1007/s10495-014-0986-z · Cited by 16 · see citing works
Pollen Typhae Total Flavone Inhibits Endoplasmic Reticulum Stress-Induced Apoptosis in Human Aortic-Vascular Smooth Muscle Cells through Down-Regulating PERK-eIF2α-ATF4-CHOP Pathway
Chen, M., Huang, R., Ou, L.-J., Chen, Y., Men, L., Chang, X., Wang, L., Yang, Y., & Zhang, Z. (2019) · Chinese Journal of Integrative Medicine · doi:10.1007/s11655-019-3052-4 · Cited by 16 · see citing works
Atherosclerosis: A Pathologist’s Perspective
Verbóová, Ľ., Nedoroščík, A., Kisková-Šimková, T., Šmirjáková, A., Bohus, P., Kollár, M., Virag, M., Mazarova, K., & Závacká, M. (2026) · Journal of Cardiovascular Development and Disease · doi:10.3390/jcdd13020085 · Cited by 15 · see citing works
Dietary compound α‐asarone alleviates ER stress‐mediated apoptosis in 7β‐hydroxycholesterol‐challenged macrophages
Park, S., Kang, M., Choi, Y. J., Kim, Y., Antika, L. D., Lim, S. S., & Kang, Y. (2016) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201500750 · Cited by 15 · see citing works
Astragaloside IV protects against C/EBP homologous protein-mediated apoptosis in oxidized low-density lipoprotein-treated macrophages by promoting autophagy
Tian, H., Wang, T., Zhang, Y., Pan, T., Yao, S., Yu, H., Ma, K., & Wang, S. (2022) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2022.174912 · Cited by 14 · see citing works
Genome-wide census of ATF4 binding sites and functional profiling of trait-associated genetic variants overlapping ATF4 binding motifs
Örd, T., Örd, D., Adler, P., & Örd, T. (2023) · PLoS Genetics · doi:10.1371/journal.pgen.1011014 · Cited by 14 · see citing works
High‐throughput profiling reveals perturbation of endoplasmic reticulum stress‐related genes in atherosclerosis induced by high‐cholesterol diet and the protective role of vitamin E
Bozaykut, P., Ekren, R., Sezerman, O. U., Gladyshev, V. N., & Özer, N. K. (2020) · BioFactors · doi:10.1002/biof.1635 · Cited by 14 · see citing works
Purple Perilla Extracts Allay ER Stress in Lipid-Laden Macrophages
Park, S., Shin, D., Lim, S. S., Lee, J., & Kang, Y. (2014) · PLoS ONE · doi:10.1371/journal.pone.0110581 · Cited by 14 · see citing works
Developmental endothelial locus 1: the present and future of an endogenous factor in vessels
Jiang, D., Yue, H., Liang, W., & Wu, Z. (2024) · Frontiers in Physiology · doi:10.3389/fphys.2024.1347888 · Cited by 13 · see citing works
How Similar Are Proteins and Origami?
Azulay, H., Lutaty, A., & Qvit, N. (2022) · Biomolecules · doi:10.3390/biom12050622 · Cited by 13 · see citing works
Ab initio protein structure prediction: the necessary presence of external force field as it is delivered by Hsp40 chaperone
Roterman, I., Stąpor, K., & Konieczny, L. (2023) · BMC Bioinformatics · doi:10.1186/s12859-023-05545-0 · Cited by 13 · see citing works
Oleanolic Acid@SPIONs Alleviates Lipid-Oxidative Stress Injury of Zebrafish Blood Vessels via Regulating the Expression of JNK and MAPK Signaling Pathways in Vascular Endothelial Cells
Gao, H., Liu, T., Liu, J., Yang, L., Liu, L., Cui, Z., Du, X., Gu, Y., & Huang, P. (2025) · Drug Design Development and Therapy · doi:10.2147/dddt.s512752 · Cited by 11 · see citing works
PPARβ/δ activation protects against corticosterone-induced ER stress in astrocytes by inhibiting the CpG hypermethylation of microRNA-181a
Ji, J., Zeng, X., Cao, L., Zhang, L., Zhao, Z., Yang, D., & Sun, X. (2016) · Neuropharmacology · doi:10.1016/j.neuropharm.2016.10.022 · Cited by 11 · see citing works
Coordinating Organismal Metabolism During Protein Misfolding in the ER Through the Unfolded Protein Response
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Apocynin protects endothelial cells from endoplasmic reticulum stress-induced apoptosis via IRE1α engagement
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Integrated Stress Response Inhibition in Atherosclerosis
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Methylglyoxal stimulates endoplasmic reticulum stress in vascular smooth muscle cells
Kırça, M., & Yeşilkaya, A. (2021) · Journal of Receptors and Signal Transduction · doi:10.1080/10799893.2021.1918167 · Cited by 10 · see citing works
X-box Binding Protein 1: An Adaptor in the Pathogenesis of Atherosclerosis
Wang, T., Zhou, J., Zhang, X., Wu, Y., Jin, K., Wang, Y., Xu, R., Yang, G., Li, W., & Jiao, L. (2022) · Aging and Disease · doi:10.14336/ad.2022.0824 · Cited by 9 · see citing works
Promoting athero-protective immunity by vaccination with low density lipoprotein-derived antigens
Nilsson, J. Å., & Shah, P. K. (2021) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2021.08.033 · Cited by 8 · see citing works
Cholesterol enriched diet suppresses ATF6 and PERK and upregulates the IRE1 pathways of the unfolded protein response in spontaneously hypertensive rats: Relevance to pathophysiology of atherosclerosis in the setting of hypertension
Tumanovska, L. V., Swanson, R. J., Serebrovska, Z. O., Portnichenko, G. V., Goncharov, S. V., Kysilov, B., Moibenko, O. O., & Dosenko, V. (2019) · Pathophysiology · doi:10.1016/j.pathophys.2019.05.005 · Cited by 8 · see citing works
The Unfolded Protein Response in the Immune Cell Development: Putting the Caretaker in the Driving Seat
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Small molecules as modulators of the proteostasis machinery: Implication in cardiovascular diseases
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IRE1α: from the function to the potential therapeutic target in atherosclerosis
Zhou, Z., Wu, L., Liu, Y., Tang, M.-Y., Tang, J., Deng, Y.-Q., Liu, L., Nie, B.-B., Zou, Z.-K., & Huang, L. (2023) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-023-04780-6 · Cited by 6 · see citing works
Changes of Bax, Bcl-2, CCR-2, MCP-1, and TGF-β1 genes in the left ventricle of spontaneously hypertensive rat after losartan treatment
Lee, H., Kim, K. C., & Hong, Y. M. (2018) · Korean Journal of Pediatrics · doi:10.3345/kjp.2018.06856 · Cited by 4 · see citing works
In Silico Modeling of COVID-19 Pandemic Course Differentiation Using the FOD Model
Roterman, I., Stąpor, K., Fabian, P., & Konieczny, L. (2022) · Coronaviruses · doi:10.2174/2666796703666220602155421 · Cited by 4 · see citing works
The Joint Link of the rs1051730 and rs1902341 Polymorphisms and Cigarette Smoking to Peripheral Artery Disease and Atherosclerotic Lesions of Different Arterial Beds
Zhabin, S. N., Lazarenko, V. A., Azarova, I. E., Klyosova, E. Y., Быканова, М. А., Chernousova, S. S., Bashkatov, D., Gneeva, E., Polonikova, A. A., Churnosov, M. I., et al. (2023) · Life · doi:10.3390/life13020496 · Cited by 4 · see citing works
CURRENT APPROACHES TO THE IDENTIFICATION OF CELLULAR MARKERS OF ENDOTHELIAL DYSFUNCTION
Bogdanov, L. A., Koshelev, V. A., Mukhamadiyarov, R. А., Kanonykina, A., Lazebnaya, A. A., Андреевич, К. Е., Stepanov, A. D., & Кутихин, А. Г. (2024) · Complex Issues of Cardiovascular Diseases · doi:10.17802/2306-1278-2024-13-3s-191-207 · Cited by 3 · see citing works
NR4A1 deficiency promotes carotid plaque vulnerability by activating integrated stress response via targeting Bcat1
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ATF3 and EGR2 gene expression levels in sdLDL-treated macrophages of patients with coronary artery stenosis
Hosseini‐Fard, S. R., Khosravi, M., Yarnazari, A., Hassanpour, P., Amirfarhangi, A., Tajik, N., Faezeh, N.-G., & Najafi, M. (2018) · Journal of Laboratory Medicine · doi:10.1515/labmed-2017-0138 · Cited by 3 · see citing works
The role of lipoxins in cardiometabolic physiology and disease
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Mechanisms of ER Stress-Induced Apoptosis in Atherosclerosis
Scull, C. M., & Tabas, I. A. (2011) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.111.224881 · Cited by 197 · see citing works
Self-citation
The Role of Endoplasmic Reticulum Stress in the Progression of Atherosclerosis
Tabas, I. (2010) · Circulation Research · doi:10.1161/circresaha.110.224766 · Cited by 480 · see citing works
Self-citation
Role of Endoplasmic Reticulum Stress in Atherosclerosis and Its Potential as a Therapeutic Target
Yang, S., Wu, M., Li, X., Zhao, R., Zhao, Y., Liu, L., & Wang, S. (2020) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2020/9270107 · Cited by 68 · see citing works
Endoplasmic Reticulum Stress and Atherosclerosis
Zhou, H., Sun, L., Xiao, J., Zhang, L., Li, X., Studer, E. J., Pandak, W. M., & Hylemon, P. B. (2010) · Current Hypertension Reviews · doi:10.2174/157340210790231744 · Cited by 6 · see citing works
A reporter for tracking the UPR in vivo reveals patterns of temporal and cellular stress during atherosclerotic progression
Thorp, E. B., Iwawaki, T., Miura, M., & Tabas, I. A. (2011) · Journal of Lipid Research · doi:10.1194/jlr.d012492 · Cited by 24 · see citing works
Self-citation

Authors: Zhou, A. X., & Tabas, I.
Affiliations: Columbia University Irving Medical Center (US)
Columbia University (US)
Corresponding author: Zhou, Alex X.
ORCID: Tabas, Ira
Venue: Seminars in Immunopathology
Publisher: Springer Science and Business Media LLC
Published: 2013-04-04
Volume: 35
Issue: 3
Pages: 321-332
ISSN: 1863-2297 (ISSN-L)
1863-2300
DOI: 10.1007/s00281-013-0372-x
PMC: PMC3967405
OpenAlex: W2023441054
Cited by: 121
References: 91
Citations by year: 2026: 5 · 2025: 5 · 2024: 7 · 2023: 8 · 2022: 9 · 2021: 7 · 2020: 6 · 2019: 11 · 2018: 11 · 2017: 12 · 2016: 12 · 2015: 11 · 2014: 14 · 2013: 3
FWCI: 1.53
Type: journal article
Language: en
Open access: green
europepmc.org
Licence: www.springer.com/tdm (tdm)
Locations: Seminars in Immunopathology (publishedVersion)
PubMed (publishedVersion)
Europe PMC (PubMed Central) (acceptedVersion)
PubMed Central (acceptedVersion)
Funders: National Institutes of Health
National Heart, Lung, and Blood Institute (R01HL106019, P01HL087123, R01HL075662, R01HL107497)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Endoplasmic Reticulum Stress and Disease
Life Sciences › Immunology and Microbiology › Immunology › Atherosclerosis and Cardiovascular Diseases
Life Sciences › Neuroscience › Sensory Systems › Ion Channels and Receptors
Keywords: unfolded protein response, atherosclerosis, endoplasmic reticulum stress, PERK pathway, ATF6 pathway, endothelial cells, vascular smooth muscle cells, macrophages, apoptosis, plaque vulnerability, inflammation, macrophage differentiation
MeSH terms: Animals, Cell Differentiation, Humans, Inflammation, Macrophages, Apoptosis, Atherosclerosis, Unfolded Protein Response, Endoplasmic Reticulum Stress

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