Cited by 151Endoplasmic Reticulum Stress and DiseasePancreatic function and diabetesIon Channels and Receptors

The DOI matches its Crossref record; 54 of the 55 references it cites were found in a registry or an index.

Endoplasmic Reticulum Stress and Diabetes Mellitus.

Open access

ARAKI, Eiichi, OYADOMARI, Seiichi, MORI, Masataka·2003·Internal Medicine

Open this paper in CoChat — free account Open PDF

Abstract

Pancreatic beta-cells are strongly engaged in protein secretion and have highly developed endoplasmic reticulum (ER). Proper folding of polypeptide into a three-dimensional structure is essential for cellular function and protein malfolding can threaten cell survival. Various conditions can perturb the protein folding in the ER, which is collectively called ER stress. In order to adapt ER stress conditions, the cells respond in three distinct ways such as transcriptional induction of ER chaperones, translational attenuation, and ER-associated degradation (ERAD). However, when ER functions are severely impaired, the cell is eliminated by apoptosis via transcriptional induction of CHOP/GADD153, the activation of cJUN NH2-terminal kinase, and/or the activation of caspase-12. Recent studies have revealed that beta-cell is one of the most susceptible cells for ER stress, and ER stress-mediated apoptosis in beta-cells can be a cause of diabetes. A comprehensive understanding of the impact of the ER stress pathway in beta-cells and how it relates to the development of diabetes may contribute to provide new targets for the prevention and treatment of this disease.

Integrity signals

Registry

Crossref · 10.2169/internalmedicine.42.7

Cites

54 of 54 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

We couldn’t retrieve this paper’s full text, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Regulated Translation Initiation Controls Stress-Induced Gene Expression in Mammalian Cells
Harding, H. P., Novoa, I., Zhang, Y., Zeng, H., Wek, R. C., Schapira, M., & Ron, D. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)00108-8 · Cited by 3,344
Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-β
Nakagawa, T., Zhu, H., Morishima, N., Li, E., Xu, J., Yankner, B. A., & Yuan, J. (2000) · Nature · doi:10.1038/47513 · Cited by 3,292
Coupling of stress in the ER to activation of JNK protein kinases by transmembrane protein kinase IRE1.
Urano, F., Wang, X.-Z., Bertolotti, A., Zhang, Y.-H., Chung, P., Harding, H., & Ron, D. (2000) · Science · doi:10.1126/science.287.5453.664 · Cited by 3,081
Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases
Bucciantini, M., Giannoni, E., Chiti, F., Baroni, F., Formigli, L., Zurdo, J., Taddei, N., Ramponi, G., Dobson, C. M., & Stefani, M. (2002) · Nature · doi:10.1038/416507a · Cited by 2,434
CHOP is implicated in programmed cell death in response to impaired function of the endoplasmic reticulumPreprint
Zinszner, H., Kuroda, M., Wang, X., Batchvarova, N., Lightfoot, R. T., Remotti, H. E., Stevens, J. L., & Ron, D. (1998) · Genes & Development · doi:10.1101/gad.12.7.982 · Cited by 2,039
Gadd153 Sensitizes Cells to Endoplasmic Reticulum Stress by Down-Regulating Bcl2 and Perturbing the Cellular Redox State
McCullough, K. D., Martindale, J. L., Klotz, L., Aw, T. Y., & Holbrook, N. J. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.4.1249-1259.2001 · Cited by 1,945
Aggresomes, inclusion bodies and protein aggregation
Kopito, R. R. (2000) · Trends in Cell Biology · doi:10.1016/s0962-8924(00)01852-3 · Cited by 1,942
ASK1 is essential for endoplasmic reticulum stress-induced neuronal cell death triggered by expanded polyglutamine repeatsPreprint
Nishitoh, H., Matsuzawa, A., Tobiume, K., Saegusa, K., Takeda, K., Inoue, K., Hori, S., Kakizuka, A., & Ichijo, H. (2002) · Genes & Development · doi:10.1101/gad.992302 · Cited by 1,372
Translational Control Is Required for the Unfolded Protein Response and In Vivo Glucose Homeostasis
Scheuner, D. L., Song, B., McEwen, E. L., Liu, C., Laybutt, D. R., Gillespie, P. J., Saunders, T. L., Bonner‐Weir, S., & Kaufman, R. J. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00265-9 · Cited by 1,355
Diabetes Mellitus and Exocrine Pancreatic Dysfunction in Perk−/− Mice Reveals a Role for Translational Control in Secretory Cell Survival
Harding, H. P., Zeng, H., Zhang, Y., Jungries, R., Chung, P., Plesken, H., Sabatini, D. D., & Ron, D. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00264-7 · Cited by 1,217

Show all 55 references

Sorted by citations

Type 2 diabetes as an inflammatory disease
Donath, M. Y., & Shoelson, S. E. (2011) · Nature Reviews Immunology · doi:10.1038/nri2925 · Cited by 3,737
Roles of CHOP/GADD153 in endoplasmic reticulum stress
Oyadomari, S., & Mori, M. (2003) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401373 · Cited by 2,879
“infant diabetes due to pancreatic hypoplasia and a reduced number of b-cells.(77,78) eIF2a knockin mice have more severe b-cell deficiency as seen in 16.”
BackgroundSelf-citation
Endoplasmic reticulum stress: cell life and death decisions
Xu, C. (2005) · Journal of Clinical Investigation · doi:10.1172/jci26373 · Cited by 2,291
Cell death and endoplasmic reticulum stress: disease relevance and therapeutic opportunities
Kim, I., Xu, W., & Reed, J. C. (2008) · Nature Reviews Drug Discovery · doi:10.1038/nrd2755 · Cited by 1,840
“Moreover, PERK gene mutations in association with infant-onset diabetes have been described in humans with the autosomal recessive disorder Wolcott–Rallison syndrom”
Background
ER stress and diseases
Yoshida, H. (2007) · The FEBS Journal · doi:10.1111/j.1742-4658.2007.05639.x · Cited by 1,086
Decreased beta-cell mass in diabetes: significance, mechanisms and therapeutic implications
Donath, M. Y., & Halban, P. A. (2004) · Diabetologia · doi:10.1007/s00125-004-1336-4 · Cited by 430
“One such signal might be increased ER-stress [35, 36, 37].”
BackgroundInfluential
A review of the mammalian unfolded protein response
Chakrabarti, A., Chen, A. W., & Varner, J. D. (2011) · Biotechnology and Bioengineering · doi:10.1002/bit.23282 · Cited by 428
“[PubMed: 11389192] LaFerla F. Calcium dyshomeostasis and intracellular signalling in Alzheimer's disease.”
BackgroundInfluential
Mechanisms of β-Cell Death in Type 2 Diabetes
Donath, M. Y., Ehses, J. A., Maedler, K., Schumann, D. M., Ellingsgaard, H., Eppler, E., & Reinecke, M. (2005) · Diabetes · doi:10.2337/diabetes.54.suppl_2.s108 · Cited by 444
Biology of Endoplasmic Reticulum Stress in the Heart
Groenendyk, J., Sreenivasaiah, P. K., Kim, D. H., Agellon, L. B., & Michalak, M. (2010) · Circulation Research · doi:10.1161/circresaha.110.227033 · Cited by 319
Arabidopsis Ubiquitin Conjugase UBC32 Is an ERAD Component That Functions in Brassinosteroid-Mediated Salt Stress Tolerance
Cui, F., Liu, L., Zhao, Q., Zhang, Z., Li, Q., Lin, B., Wu, Y., Tang, S., & Xie, Q. (2012) · The Plant Cell · doi:10.1105/tpc.111.093062 · Cited by 269
“When prolonged ER stress extensively impairs the homeostasis of the ER, apoptosis is activated by the induction of CHOP (encoding the CCAAT/ enhancer binding protein homologous protein) (Araki et al., 2003).”
Background
Endoplasmic Reticulum Stress Stimulates the Expression of Cyclooxygenase-2 through Activation of NF-κB and pp38 Mitogen-activated Protein Kinase
Hung, J., Su, I., Lei, H.-Y., Wang, H.-C., Lin, W.-C., Chang, W., Huang, W., Chang, W., Chang, Y.-S., Chen, C., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m403568200 · Cited by 261
Endoplasmic Reticulum Stress in the Heart
Glembotski, C. C. (2007) · Circulation Research · doi:10.1161/circresaha.107.161273 · Cited by 230
The integrated stress response prevents demyelination by protecting oligodendrocytes against immune-mediated damage
Lin, W., Bailey, S. L., Ho, H., Harding, H. P., Ron, D., Miller, S. D., & Popko, B. (2007) · Journal of Clinical Investigation · doi:10.1172/jci29571 · Cited by 201
“While it has been shown that the apoptotic program controlled by the ER stress response plays an important role in the pathogenesis of various diseases such as diabetes mellitus and neurodegenerative diseases (40, 41), several lines of evidence suggest that a modest ER stress response that does not cause severe cell i…”
Background
Evaluation of the effects of anthocyanins in type 2 diabetes
Sancho, R. A. S., & Pastore, G. M. (2011) · Food Research International · doi:10.1016/j.foodres.2011.11.021 · Cited by 196
Stress and the inflammatory process: a major cause of pancreatic cell death in type 2 diabetes
Novials, A., Montané, J., & Cadavez, L. (2014) · Diabetes Metabolic Syndrome and Obesity · doi:10.2147/dmso.s37649 · Cited by 164
“Procaspase-12 is localized to ER membranes and undergoes cleavage during ER stress in murine cells, promoting the downstream cleaving of caspase-3, the last effector caspase of the apoptotic cascade.(68,69) Pharmacologically induced ER stress has given additional insight into mechanisms by which ER stress may promote…”
Background
The endoplasmic reticulum-associated degradation is necessary for plant salt tolerance
Liu, L., Cui, F., Li, Q., Yin, B., Zhang, H., Lin, B., Wu, Y., Xia, R., Tang, S., & Xie, Q. (2010) · Cell Research · doi:10.1038/cr.2010.181 · Cited by 151
RyR2 and Calpain-10 Delineate a Novel Apoptosis Pathway in Pancreatic Islets
Johnson, J. D., Han, Z., Otani, K., Ye, H., Zhang, Y., Wu, H., Horikawa, Y., Misler, S., Bell, G. I., & Polonsky, K. S. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m401216200 · Cited by 145
PERK (EIF2AK3) Regulates Proinsulin Trafficking and Quality Control in the Secretory Pathway
Gupta, S., McGrath, B. C., & Cavener, D. R. (2010) · Diabetes · doi:10.2337/db09-1064 · Cited by 139
“Initially, it was proposed that increased -cell death was the cause of the dominant Akita phenotype (28,29).”
Background
Type 2 diabetes mellitus as a conformational disease.
Hayden, M. R., Tyagi, S. C., Kerklo, M. M., & Nicolls, M. R. (2005) · PubMed · Cited by 120
O-GlcNAc signaling attenuates ER stress-induced cardiomyocyte death
Ngoh, G. A., Hamid, T., Prabhu, S. D., & Jones, S. P. (2009) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00553.2009 · Cited by 121
Imatinib Mesylate Reduces Endoplasmic Reticulum Stress and Induces Remission of Diabetes in db/db Mice
Han, M. S., Chung, K. W., Cheon, H. G., Rhee, S. D., Yoon, C., Lee, M., Kim, K., & Lee, M. (2009) · Diabetes · doi:10.2337/db08-0080 · Cited by 117
“We next studied pancreatic -cell changes because pancreatic -cells have adaptive capacity to changing insulin resistance and -cell failure is the ultimate cause of diabetes (30,31).”
Background
β cell ER stress and the implications for immunogenicity in type 1 diabetes
Marré, M. L., James, E. A., & Piganelli, J. D. (2015) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2015.00067 · Cited by 115
“…stress. β cells, like all professional secretory cells, naturally undergo high levels of ER stress as a result of their normal secretory physiology (Araki et al., 2003a; Lipson et al., 2006a,b; Wu and Kaufman, 2006; Fonseca et al., 2007; Ortsäter and Sjöholm, 2007; Eizirik et al., 2008; Volchuk…”
Background
CHOP plays a pivotal role in the astrocyte death induced by oxygen and glucose deprivation
Benavides, A., Pastor, M. D., Santos, P., Tranque, P., & Calvo, S. (2005) · Glia · doi:10.1002/glia.20242 · Cited by 108
“…online 6 July 2005 in Wiley InterScience (www.interscience. wiley.com). mediated apoptosis seems to be involved in some human diseases like diabetes (Oyadomari et al., 2002; Araki et al., 2003) and neurodegenerative diseases (Milhavet et al., 2002; Kogel et al., 2003; Holtz and O’Malley, 2003).”
Background
Reactive Oxygen Species Promote Caspase-12 Expression and Tubular Apoptosis in Diabetic Nephropathy
Brezniceanu, M.-L., Lau, C. J., Godin, N., Chénier, I., Duclos, A. J., Ethier, J. H., Filep, J. G., Ingelfinger, J. R., Zhang, S., & Chan, J. S. D. (2010) · Journal of the American Society of Nephrology · doi:10.1681/asn.2009030242 · Cited by 107
Astragalus polysaccharides decreased the expression of PTP1B through relieving ER stress induced activation of ATF6 in a rat model of type 2 diabetes
Wang, N., Deling, Z., Mao, X., Zou, F., Jin, H., & Ouyang, J. (2009) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2009.03.001 · Cited by 106
“Accumulating evidences from recent esearcheshadproved that ER stresswas a central feature of periphral insulin resistance and T2DM at the molecular, cellular, and rganismal levels (Eiichi et al., 2003; Muoio and Newgard, 2008; izirik et al., 2008; Özcan et al., 2004).”
PERK-opathies: An Endoplasmic Reticulum Stress Mechanism Underlying Neurodegeneration
Bell, M. C., Meier, S. E., Ingram, A., & Abisambra, J. F. (2015) · Current Alzheimer Research · doi:10.2174/1567205013666151218145431 · Cited by 104
“Secretory cells, such as islet β-cells that are integral for insulin production, produce high levels of PERK [35, 36].”
BackgroundInfluential
Modifying Enzymes Are Elicited by ER Stress, Generating Epitopes That Are Selectively Recognized by CD4+ T Cells in Patients With Type 1 Diabetes
Marré, M. L., McGinty, J. W., Chow, I., DeNicola, M., Beck, N. W., Kent, S. C., Powers, A. C., Bottino, R., Harlan, D. M., Greenbaum, C. J., et al. (2018) · Diabetes · doi:10.2337/db17-1166 · Cited by 92
Inherent ER stress in pancreatic islet β cells causes self-recognition by autoreactive T cells in type 1 diabetes
Marré, M. L., Profozich, J., Coneybeer, J., Geng, X., Bertera, S., Ford, M., Trucco, M., & Piganelli, J. D. (2016) · Journal of Autoimmunity · doi:10.1016/j.jaut.2016.04.009 · Cited by 84
Endoplasmic Reticulum Stress-activated C/EBP Homologous Protein Enhances Nuclear Factor-κB Signals via Repression of Peroxisome Proliferator-activated Receptor γ
Park, S., Choi, H. J., Yang, H. J., Do, K. H., Kim, J., Lee, D. W., & Moon, Y. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.136259 · Cited by 87
The Group VIA Calcium-Independent Phospholipase A2 Participates in ER Stress-Induced INS-1 Insulinoma Cell Apoptosis by Promoting Ceramide Generation via Hydrolysis of Sphingomyelins by Neutral Sphingomyelinase
Lei, X., Zhang, S., Bohrer, A., Bao, S. S., Song, H., & Ramanadham, S. (2007) · Biochemistry · doi:10.1021/bi700017z · Cited by 82
Too much of a good thing: why it is bad to stimulate the beta cell to secrete insulin
Aston‐Mourney, K., Proietto, J., Morahan, G., & Andrikopoulos, S. (2008) · Diabetologia · doi:10.1007/s00125-008-0930-2 · Cited by 79
“Studies have shown that the beta cell is one of the most susceptible cells to ER stress, and furthermore, ER stress-mediated apoptosis in the beta cell has been suggested as having an important role in the development of type 2 diabetes [28, 29].”
T Cell Epitopes and Post-Translationally Modified Epitopes in Type 1 Diabetes
McGinty, J. W., Marré, M. L., Bajzik, V., Piganelli, J. D., & James, E. A. (2015) · Current Diabetes Reports · doi:10.1007/s11892-015-0657-7 · Cited by 77
Immune recognition of citrullinated epitopes
Nguyen, H. Q. T., & James, E. A. (2016) · Immunology · doi:10.1111/imm.12640 · Cited by 73
Misfolded Proinsulin Affects Bystander Proinsulin in Neonatal Diabetes
Hodish, I., Liu, M. R., Rajpal, G., Larkin, D. D., Holz, R. W., Adams, A. M., Liu, L., & Arvan, P. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.038042 · Cited by 72
Apoptosis of pancreatic β-cells in Type 1 diabetes
Tomita, T. (2017) · Biomolecules and Biomedicine · doi:10.17305/bjbms.2017.1961 · Cited by 78
“stress [50], leading to β-cell exhaustion and eventual apop-”
Background
Honokiol abrogates chronic restraint stress-induced cognitive impairment and depressive-like behaviour by blocking endoplasmic reticulum stress in the hippocampus of mice
Jangra, A., Dwivedi, S., Sriram, C. S., Gurjar, S. S., Kwatra, M., Sulakhiya, K., Baruah, C. C., & Lahkar, M. (2015) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2015.11.047 · Cited by 71
“If the damage is too severe to repair, C/EBP-homologous protein (CHOP) and other factors are activated and induce cell apoptosis (Araki et al., 2003).”
Background
Insulin-Like Growth Factor (IGF)-I/IGF-Binding Protein-3 Complex: Therapeutic Efficacy and Mechanism of Protection against Type 1 Diabetes
Chen, W., Salojin, K. V., Mi, Q., Grattan, M., Meagher, T. C., Zucker, P., & Delovitch, T. L. (2003) · Endocrinology · doi:10.1210/en.2003-1274 · Cited by 69
Prolonged Endoplasmic Reticulum Stress Induces Apoptotic Cell Death in an Experimental Model of Chronic Cyclosporine Nephropathy
Han, S. W., Li, C., Ahn, K. O., Lim, S. W., Song, H. G., Jang, Y. S., Cho, Y. M., Jang, Y. M., Ghee, J. Y., Kim, J. Y., et al. (2008) · American Journal of Nephrology · doi:10.1159/000127432 · Cited by 68
“However, when ER stress is excessive and/or prolonged, the initiation of apoptotic processes is promoted [ , ,”
Background
A Point Mutation in Sec61α1 Leads to Diabetes and Hepatosteatosis in Mice
Lloyd, D. J., Wheeler, M. C., & Gekakis, N. (2009) · Diabetes · doi:10.2337/db08-1362 · Cited by 71
ER Stress in Adipocytes Inhibits Insulin Signaling, Represses Lipolysis, and Alters the Secretion of Adipokines Without Inhibiting Glucose Transport
Xu, L., Spinas, G. A., & Nießen, M. (2010) · Hormone and Metabolic Research · doi:10.1055/s-0030-1255034 · Cited by 71
RING-finger type E3 ubiquitin ligase inhibitors as novel candidates for the treatment of rheumatoid arthritis
Yagishita, N., Aratani, S., Leach, C. A., Amano, T., Yamano, Y., Nakatani, K., Nishioka, K., & Nakajima, T. (2012) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2012.1129 · Cited by 68
“Accordingly, RING E3 ligases have been linked to the control of multiple cellular processes and to many human diseases such as diabetes mellitus, polygluta-mine disease, and Parkinson's diseases (24-26).”
Genetic inactivation of PERK signaling in mouse oligodendrocytes: Normal developmental myelination with increased susceptibility to inflammatory demyelination
Hussien, Y., Cavener, D. R., & Popko, B. (2014) · Glia · doi:10.1002/glia.22634 · Cited by 61
“It has been shown that the disruption of protein translation in the secretory pathway plays an important role in the pathogenesis of various diseases, such as diabetes mellitus, neurodegenerative disorders, and hypomyelinating diseases (Araki et al., 2003; Bauer et al., 2002; Fogli et al., 2004; Leegwater et al., 2001…”
Background
Chapter 2 The Structure and Function of Insulin
Weiss, M. A. (2009) · Vitamins and hormones · doi:10.1016/s0083-6729(08)00602-x · Cited by 59
“This hypothesis is supported by the observation of a human mutation associated with neonatal diabetes mellitus that recapitulates a classical diabetes-associated mutation in the mouse (the Akita mouse; Araki et al., 2003; Oyadomari et al., 2002; Ron, 2002) in which Cys is substituted by Tyr.”
Influential
Neuroprotective Effect of Ginkgolide B on Bupivacaine-Induced Apoptosis in SH-SY5Y Cells
Li, L., Zhang, Q., Lai, L., Wen, X., Zheng, T., Cheung, C.-W., Zhou, S., & Xu, S. (2013) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2013/159864 · Cited by 56
Metformin differentially activates ER stress signaling pathways without inducing apoptosis
Quentin, T., Steinmetz, M., Poppe, A., & Thoms, S. (2011) · Disease Models & Mechanisms · doi:10.1242/dmm.008110 · Cited by 58
“…diseases, metabolic disorders such as insulin resistance and type 2 diabetes, and cardiovascular diseases such as cardiac hypertrophy, heart failure, atherosclerosis and ischemic heart disease (Araki et al., 2003; Kim et al., 2008; Minamino and Kitakaze, 2010; Thoms et al., 2009).”
Altered Retinoic Acid Metabolism in Diabetic Mouse Kidney Identified by 18O Isotopic Labeling and 2D Mass Spectrometry
Starkey, J. M., Zhao, Y., Sadygov, R. G., Haidacher, S. J., LeJeune, W. S., Dey, N., Luxon, B. A., Kane, M. A., Napoli, J. L., Denner, L. A., et al. (2010) · PLoS ONE · doi:10.1371/journal.pone.0011095 · Cited by 50
“Numerous biochemical and metabolic pathways have emerged as predominant pathophysiological mechanisms for diabetes-induced renal injury [2–11].”
Background
Toxoplasma gondiiinduce apoptosis of neural stem cells via endoplasmic reticulum stress pathway
Wang, T., Zhou, J. H. S., Gan, X., Wang, H., Ding, X., Chen, L., Wang, Y., Du, J., Shen, J., & Yu, L. (2014) · Parasitology · doi:10.1017/s0031182014000183 · Cited by 47
“Caspase-12, an ER-localized cysteine protease, is only activated by ER stress, but not by death receptor-mediated or mitochondria-targeted apoptotic signals (Nakagawa et al. 2000; Araki et al. 2003).”
Background
A gene-environment interaction analysis of plasma selenium with prevalent and incident diabetes: The Hortega study
Galán-Chilet, I., Grau-Pérez, M., de Marco, G., Güallar, E., Martín-Escudero, J. C., Dominguez-Lucas, A., González-Manzano, I., López‐Izquierdo, R., Briongos-Figuero, L. S., Redón, J., et al. (2017) · Redox Biology · doi:10.1016/j.redox.2017.04.022 · Cited by 49
“Interestingly, ER in the pancreatic beta cells has an important role in insulin secretion [54].”
Background
Unfolded protein response prevents blastocyst formation during preimplantation embryo development in vitro
Başar, M., Bozkurt, I., Guzeloglu‐Kayisli, O., Sözen, B., Tekmen, I., Schatz, F., Arici, A. M., Lockwood, C. J., & Kayisli, U. A. (2014) · Fertility and Sterility · doi:10.1016/j.fertnstert.2014.09.004 · Cited by 45
Endoplasmic Reticulum Stress-Mediated Apoptotic Pathway Is Involved in Corpus Luteum Regression in Rats
Yang, Y., Sun, M., Yuanyuan, S., Zheng, X., Ma, H., Ma, W., Wang, Z., Pei, X., & Wang, Y. (2014) · Reproductive Sciences · doi:10.1177/1933719114553445 · Cited by 45
“Several studies have shown that the ATF6a-CHOP pathway existed in cellular apoptosis.(23,43) Caspase 12 mediates ERS-specific apoptosis(44) and is activated in the ERS-induced apoptosis.”
Background
Cellular responses of novel human pancreatic β-cell line, 1.1B4 to hyperglycemia
Vasu, S., McClenaghan, N. H., McCluskey, J. T., & Flatt, P. R. (2013) · Islets · doi:10.4161/isl.26184 · Cited by 45
Thapsigargin induces apoptosis in adrenocortical carcinoma by activating endoplasmic reticulum stress and the JNK signaling pathway: an in vitro and in vivo study
Wu, L., Huang, X., Kuang, Y., Xing, Z., Deng, X., & Luo, Z. (2019) · Drug Design Development and Therapy · doi:10.2147/dddt.s209947 · Cited by 43
“The third pathway involves caspase-12.(39,40) Mutations occurring in the JNK signaling pathway (eg, MAP3K1, MAP2K4, and MAP2K7) are implicated in the pathology of breast cancer.”
Background
A link between endoplasmic reticulum stress‐induced β ‐cell apoptosis and the group VIA Ca 2+ ‐independent phospholipase A 2 (iPLA 2 β )
Lei, X., Zhang, S., Emani, B., Barbour, S. E., & Ramanadham, S. (2010) · Diabetes Obesity and Metabolism · doi:10.1111/j.1463-1326.2010.01270.x · Cited by 44
“Additionally, ER stress is thought to play a role in the autoimmune destruction of β-cells during the development of T1DM [17,30–34].”
Background
Environmental Factors Contribute to β Cell Endoplasmic Reticulum Stress and Neo-Antigen Formation in Type 1 Diabetes
Marré, M. L., & Piganelli, J. D. (2017) · Frontiers in Endocrinology · doi:10.3389/fendo.2017.00262 · Cited by 47
Swimming Differentially Affects T2DM-Induced Skeletal Muscle ER Stress and Mitochondrial Dysfunction Related to MAM
Zhang, Z., Cui, D., Zhang, T., Sun, Y., & Ding, S. (2020) · Diabetes Metabolic Syndrome and Obesity · doi:10.2147/dmso.s243024 · Cited by 39
The Role of Endoplasmic Reticulum Stress in Autoimmune-Mediated Beta-Cell Destruction in Type 1 Diabetes
Zhong, J., Rao, X., Xu, J.-F., Yang, P. C., & Wang, C. (2012) · Experimental Diabetes Research · doi:10.1155/2012/238980 · Cited by 38
“For example, loss of EIF2AK3 (the gene encodes PERK) develops Wolcott-Rallison syndrome, an autosomal recessive disorder characterized by early infancy insulin-dependent diabetes and multisystemic manifestations including growth retardation, hepatic/renal dysfunction, mental retardation, and cardiovascular abnormaliti…”
Background
O-GlcNAcylation under hypoxic conditions and its effects on the blood-retinal barrier in diabetic retinopathy
Xu, C. B., Liu, G., Liu, X., & Wang, F. (2013) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2013.1597 · Cited by 39
“During the later stages of the disease (24 and 32 weeks), it is not only distributed in the aforementioned layers but also in the inner plexiform layer.”
Differential molecular and cellular responses of GLP-1 secreting L-cells and pancreatic alpha cells to glucotoxicity and lipotoxicity
Vasu, S., Moffett, R. C., McClenaghan, N. H., & Flatt, P. R. (2015) · Experimental Cell Research · doi:10.1016/j.yexcr.2015.05.022 · Cited by 37
“Chronic oxidative stress or prolonged activation of ER stress response induces apoptosis pathways [1],[54].”
Background
Considerations for Defining Cytokine Dose, Duration, and Milieu That Are Appropriate for Modeling Chronic Low-Grade Inflammation in Type 2 Diabetes
Nunemaker, C. S. (2016) · Journal of Diabetes Research · doi:10.1155/2016/2846570 · Cited by 41
High Glucose Exposure Promotes Activation of Protein Phosphatase 2A in Rodent Islets and INS-1 832/13 β-Cells by Increasing the Posttranslational Carboxylmethylation of Its Catalytic Subunit
Arora, D. K., Machhadieh, B., Matti, A., Wadzinski, B. E., Ramanadham, S., & Kowluru, A. (2013) · Endocrinology · doi:10.1210/en.2013-1773 · Cited by 36
Oxidative stress induces unfolding protein response and inflammation in nasal polyposis
Jeanson, L., Kelly, M., Coste, A., Guerrera, I. C., Fritsch, J., Nguyen‐Khoa, T., Baudouin-Legros, M., Papon, J., Zadigue, P., Prulière-Escabasse, V., et al. (2011) · Allergy · doi:10.1111/j.1398-9995.2011.02769.x · Cited by 36
Tracking cellular stress with labeled FMAU reflects changes in mitochondrial TK2
Tehrani, O. S., Douglas, K. A., Lawhorn‐Crews, J. M., & Shields, A. F. (2008) · European Journal of Nuclear Medicine and Molecular Imaging · doi:10.1007/s00259-008-0738-9 · Cited by 36
Glucose regulated proteins 78 protects insulinoma cells (NIT-1) from death induced by streptozotocin, cytokines or cytotoxic T lymphocytes
Wang, M., Zhao, X., Wang, P., Li, L., Dai, Y. D., Huang, H., Lei, P., Zhu, H., & Shen, G. (2007) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2007.05.022 · Cited by 35
The Role of β‐Cell Dysfunction in the Cardiometabolic Syndrome
Lastra, G., Manrique, C. M., & Hayden, M. R. (2006) · Journal of the CardioMetabolic Syndrome · doi:10.1111/j.0197-3118.2006.05458.x · Cited by 38
Melatonin ameliorates myocardial apoptosis by suppressing endoplasmic reticulum stress in rats with long‑term diabetic cardiomyopathy
Xiong, F., Tang, S., Su, H., Tang, H., Jiang, P., Zhou, Q., Wang, Y., & Zhu, H. (2017) · Molecular Medicine Reports · doi:10.3892/mmr.2017.7841 · Cited by 33
Comparison of the effect of individual saturated and unsaturated fatty acids on cell growth and death induction in the human pancreatic β-cell line NES2Y
Němcová‐Fürstová, V., Kopska, T., James, R. F. L., & Kovár̆, J. (2008) · Life Sciences · doi:10.1016/j.lfs.2007.12.023 · Cited by 34
Toxoplasma gondii prevalent in China induce weaker apoptosis of neural stem cells C17.2 via endoplasmic reticulum stress (ERS) signaling pathways
Zhou, J. H. S., Gan, X., Wang, Y., Zhang, X., Ding, X., Chen, L., Du, J., Luo, Q., Wang, T., Shen, J., et al. (2015) · Parasites & Vectors · doi:10.1186/s13071-015-0670-3 · Cited by 34
“12, which is activated by ER stress, but apparently not by death receptor-mediated or mitochondria -targeted apoptotic signals [58,59].”
Background
Emerging Roles for Mesencephalic Astrocyte-Derived Neurotrophic Factor (MANF) in Pancreatic Beta Cells and Diabetes
Danilova, T., & Lindahl, M. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.01457 · Cited by 32
Bioinformatics Methodologies to Identify Interactions Between Type 2 Diabetes and Neurological Comorbidities
Rahman, M. H., Peng, S., Hu, X., Chen, C., Uddin, S., Quinn, J. M. W., & Moni, M. A. (2019) · IEEE Access · doi:10.1109/access.2019.2960037 · Cited by 30
Rosiglitazone counteracts palmitate-induced β-cell dysfunction by suppression of MAP kinase, inducible nitric oxide synthase and caspase 3 activities
Abaraviciene, S. M., Lundquist, I., & Salehi, A. A. (2008) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-008-8100-8 · Cited by 30
The Expanding Role of Oxidative Stress, Renin Angiotensin System, and β-Cell Dysfunction in the Cardiometabolic Syndrome and Type 2 Diabetes Mellitus
Lastra, G., & Manrique, C. M. (2007) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.1615 · Cited by 30
Is cystic fibrosis-related diabetes an apoptotic consequence of ER stress in pancreatic cells?
Ali, B. R. (2008) · Medical Hypotheses · doi:10.1016/j.mehy.2008.07.058 · Cited by 29
“Furthermore, failure to cope with nitric oxide-mediated ER stress led to apoptosis of pancreatic b-cells through transcriptional induction of CHOP/GADD153, the activation of c-JUN NH2-terminal kinase, and/or the activation of caspase-12 [21,1].”
BackgroundInfluential
Administration of mulberry leaves maintains pancreatic β-cell mass in obese/type 2 diabetes mellitus mouse model
Suthamwong, P., Minami, M., Okada, T., Shiwaku, N., Uesugi, M., Yokode, M., & Kamei, K. (2020) · BMC Complementary Medicine and Therapies · doi:10.1186/s12906-020-02933-4 · Cited by 28
Ginkgolide B‑induced AMPK pathway activation protects astrocytes by regulating endoplasmic reticulum stress, oxidative stress and energy metabolism induced by Aβ1‑42
Wang, J., Ding, Y., Zhuang, L., Wang, Z., Xiao, W., & Zhu, J. (2021) · Molecular Medicine Reports · doi:10.3892/mmr.2021.12096 · Cited by 30
“Previous studies on patients with AD and the brain tissues of animal models demonstrate that Aβ seriously disturbs the functions of ER, leading to excessive generation of Aβ, ERS activation (19,20) and finally cell dysfunction and apoptosis (21).”
Estradiol Prevents High Glucose-Induced β-cell Apoptosis by Decreased BTG2 Expression
Kooptiwut, S., Kaewin, S., Semprasert, N., Sujjitjoon, J., Junking, M., Suksri, K., & Yenchitsomanus, P. (2018) · Scientific Reports · doi:10.1038/s41598-018-30698-x · Cited by 28
Oxidative and nitrosative stress in β-cell apoptosis: their contribution to β-cell lossin type 1 diabetes mellitus
Watson, D., & Loweth, A. C. (2009) · British Journal of Biomedical Science · doi:10.1080/09674845.2009.11730278 · Cited by 27
Hyperglycemia magnifies bupivacaine‐induced cell apoptosis triggered by mitochondria dysfunction and endoplasmic reticulum stress
Li, L., Ye, X. Y., Lu, A., Zhou, S., Liu, H., Liu, Z., Jiang, S., & Xu, S. (2013) · Journal of Neuroscience Research · doi:10.1002/jnr.23216 · Cited by 27
“In agreement with previous studies (Araki et al., 2003; Takada et al., 2012), we found that Grp78 mRNA and protein expression were upregulated in the bupivacaine group and were enhanced by high-level glucose pretreatment.”
Result
Bushen Zhuangjin decoction inhibits TM-induced chondrocyte apoptosis mediated by endoplasmic reticulum stress
LIN, P., Weng, X., LIU, F., Ma, Y., Chen, H., SHAO, X., ZHENG, W., Liu, X., Ye, H., & Li, X. (2015) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2015.2387 · Cited by 25
“To confirm the inhibitory effects of BZD on ER stress-mediated chondrocyte apoptosis, we measured the expression levels of established the ER stress-associated markers (24), Bip, Xbp1, Chop and Atf4.”
The endoplasmic reticulum stress response in disease pathogenesis and pathophysiology
Manalo, R. V. M., & Medina, P. M. B. (2017) · Egyptian Journal of Medical Human Genetics · doi:10.1016/j.ejmhg.2017.07.004 · Cited by 25
“Eventually, UPR promotes attenuation of protein synthesis, which would lead to a downregulation of insulin production and eventually the depleted Ca promoted by hyperglycemia would cause b-cell exhaustion and ER-induced apoptosis [66,71].”
Background
Involvement of ER stress in apoptosis induced by sialic acid-binding lectin (leczyme) from bullfrog eggs
Tatsuta, T., Hosono, M., MIURA, Y., Sugawara, S., Kariya, Y., Hakomori, S., & Nitta, K. (2013) · International Journal of Oncology · doi:10.3892/ijo.2013.2128 · Cited by 25
“Association of ER stress-mediated apoptosis to some pathology such as Alzheimer (16), Parkinson (17), and diabetes (18) has been reported as well as the involvement of the cytotoxic mechanism in the medicinal drugs such as Bortezomib (19) and Nelfinavir (20).”
Background
Ribosomal Alteration-Derived Signals for Cytokine Induction in Mucosal and Systemic Inflammation: Noncanonical Pathways by Ribosomal Inactivation
Moon, Y. (2014) · Mediators of Inflammation · doi:10.1155/2014/708193 · Cited by 25
“Moreover, upper airway inflammation such as intranasal neutrophilic”
Background
Protective Effect of Gomisin N against Endoplasmic Reticulum Stress-Induced Hepatic Steatosis
Jang, M.-K., Yun, Y., Kim, S. H., Kim, J. H., & Jung, M. H. (2016) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.b15-01020 · Cited by 25
The flavoheme reductase Ncb5or protects cells against endoplasmic reticulum stress-induced lipotoxicity
Zhang, Y., Larade, K., Jiang, Z.-G., Ito, S., Wang, W., Zhu, H., & Bunn, H. F. (2009) · Journal of Lipid Research · doi:10.1194/jlr.m900146-jlr200 · Cited by 25
Effects of lipotoxicity on a novel insulin-secreting human pancreatic β-cell line, 1.1B4
Vasu, S., McClenaghan, N. H., McCluskey, J. T., & Flatt, P. R. (2013) · Biological Chemistry · doi:10.1515/hsz-2013-0115 · Cited by 25
“Functions of the ER include post-translational modifications, folding and protein trafficking and the provision of cellular Ca 2 + (Araki et al. , 2003 ). Any disturbances in the normal function would therefore cause β cell stress. Cunha et al. (2008) observed that fatty acids such as palmitate deplete ER Ca 2 + store…”
Background
Soluble and insoluble protein aggregates, endoplasmic reticulum stress, and vascular dysfunction in Alzheimer’s disease and cardiovascular diseases
Waigi, E. W., Webb, R. C., Moss, M. A., Uline, M. J., McCarthy, C. G., & Wenceslau, C. F. (2023) · GeroScience · doi:10.1007/s11357-023-00748-y · Cited by 26
The immunosuppressive and protective ability of glucose-regulated protein 78 for improvement of alloimmunity in β cell transplantation
Wang, M., Wang, P., Liu, Y. Q., Peng, J.-B., Zhao, X., Wu, S., He, F. R., Wen, X., Li, Y., & Shen, G. (2007) · Clinical & Experimental Immunology · doi:10.1111/j.1365-2249.2007.03525.x · Cited by 23
Baldspot/ELOVL6 is a conserved modifier of disease and the ER stress response
Palu, R. A. S., & Chow, C. Y. (2018) · PLoS Genetics · doi:10.1371/journal.pgen.1007557 · Cited by 23
The altered expression of glucose-regulated proteins 78 in different phase of streptozotocin-affected pancreatic beta-cells
Wang, M., Wang, P., Peng, J., Wu, S., Zhao, X., Li, L., & Shen, G. (2008) · Cell Stress and Chaperones · doi:10.1007/s12192-008-0053-1 · Cited by 21
“Recent studies suggest that endoplasmic reticulum (ER) stress plays an important role in the loss of beta-cells (Oyadomari et al 2002a; Araki et al 2003; Laybutt et al 2007).”
Background
D4S234E, a novel p53-responsive gene, induces apoptosis in response to DNA damage
Kudoh, T., Kimura, J., Lu, Z., Miki, Y., & Yoshida, K. (2010) · Experimental Cell Research · doi:10.1016/j.yexcr.2010.06.025 · Cited by 20
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
“high-level insulin secretion, β-cells undergo highly developed ER stress [305].”
Background
Palmatine Inhibits Up-Regulation of GRP78 and CALR Protein in an STZ-Induced Diabetic Rat Model
Okechukwu, P. N., Ekeuku, S. O., Chan, H. K., Eluri, K., & Froemming, G. R. A. (2020) · Current Pharmaceutical Biotechnology · doi:10.2174/1389201021666200730124208 · Cited by 19
PERK in POMC neurons connects celastrol with metabolism
He, Z., Lieu, L., Dong, Y., Afrin, S., Chau, D., Kabahizi, A., Wallace, B., Cao, J., Hwang, E., Yao, T. S., et al. (2021) · JCI Insight · doi:10.1172/jci.insight.145306 · Cited by 19
Mitochondria maintain maturation and secretion of lipoprotein lipase in the endoplasmic reticulum
Osibow, K., Frank, S., Malli, R., Zechner, R., & Graier, W. F. (2006) · Biochemical Journal · doi:10.1042/bj20060099 · Cited by 18
Endoplasmic Reticulum Overcrowding as a Mechanism of β-Cell Dysfunction in Diabetes
Despa, F. (2010) · Biophysical Journal · doi:10.1016/j.bpj.2009.12.4295 · Cited by 18
Dilation of the endoplasmic reticulum in beta cells due to molecular overcrowding?
Despa, F. (2008) · Biophysical Chemistry · doi:10.1016/j.bpc.2008.12.003 · Cited by 18
Analysis of cellular response to protein overexpression
Raden, D. L., Hildebrandt, S., Xu, P., Bell, E., Doyle, F. J., & Robinson, A. S. (2005) · Systems Biology · doi:10.1049/ip-syb:20050048 · Cited by 19
Proteomic and Functional Analyses Reveal the Potential Involvement of Endoplasmic Reticulum Stress and α-CP1 in the Anticancer Activities of Oridonin in HepG2 Cells
Wang, H., Ye, Y., Chu, J., Zhu, G., Fong, W. F., & Yu, Z. (2010) · Integrative Cancer Therapies · doi:10.1177/1534735410383171 · Cited by 17
“To survive under ER stress, cells activate a self-protective mechanism against ER stress termed UPR, which involves the upregulation of genes encoding ER chaperone proteins.(18) The chaperone protein Grp78 is central to the coordinated activation of UPR.”
Background
On the role of IRS2 in the regulation of functional β-cell mass
Nießen, M. (2006) · Archives of Physiology and Biochemistry · doi:10.1080/13813450600711409 · Cited by 17
“The ER is known to play a pivotal role in b-cells, and ER-stress-dependent apoptosis in islets has been described in a number of studies (Kaufman et al., 2002; Araki et al., 2003).”
Background
Protective Mechanism of KIOM‐4 in Streptozotocin‐Induced Pancreatic β ‐Cells Damage Is Involved in the Inhibition of Endoplasmic Reticulum Stress
Zhang, R., Kim, J. S., Kang, K. A., Piao, M. J., Kim, K. C., & Hyun, J. W. (2010) · Evidence-based Complementary and Alternative Medicine · doi:10.1155/2011/231938 · Cited by 16
“Hindawi Publishing Corporation Evidence-Based Complementary and Alternative Medicine Volume 2011, Article ID 231938, 10 pages doi:10.1155/2011/231938”
BackgroundInfluential
Proteomic identification of carboxypeptidase E connects lipid-induced β-cell apoptosis and dysfunction in type 2 diabetes
Johnson, J. D. (2009) · Cell Cycle · doi:10.4161/cc.8.1.7343 · Cited by 16

Authors: ARAKI, E., OYADOMARI, S., & MORI, M.
Affiliations: Kumamoto University (JP)
ORCID: ARAKI, Eiichi
OYADOMARI, Seiichi
MORI, Masataka
Venue: Internal Medicine
Publisher: Japanese Society of Internal Medicine
Published: 2003
Volume: 42
Issue: 1
Pages: 7-14
ISSN: 0918-2918 (ISSN-L)
1349-7235
DOI: 10.2169/internalmedicine.42.7
OpenAlex: W2056689556
Cited by: 151
References: 55
Citations by year: 2025: 1 · 2024: 2 · 2023: 2 · 2022: 4 · 2021: 4 · 2020: 4 · 2019: 2 · 2018: 8 · 2017: 7 · 2016: 4 · 2015: 10 · 2014: 8 · 2013: 8 · 2012: 10
FWCI: 0.37
Type: journal article
Language: en
Open access: bronze
doi.org
Locations: Internal Medicine (publishedVersion)
PubMed (publishedVersion)
Funders: Ministry of Education, Culture, Sports, Science and Technology
Japan Society for the Promotion of Science (14370339)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Endoplasmic Reticulum Stress and Disease
Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Pancreatic function and diabetes
Life Sciences › Neuroscience › Sensory Systems › Ion Channels and Receptors
Keywords: endoplasmic reticulum stress, diabetes mellitus, pancreatic beta cells, protein folding, ER-associated degradation, CHOP/GADD153, c-Jun N-terminal kinase, caspase-12, beta-cell apoptosis, ER chaperones, translational attenuation
MeSH terms: Amyloid, Animals, Diabetes Mellitus, Endoplasmic Reticulum, Humans, Islets of Langerhans, Mice, Mutant Strains, Models, Biological, Nitric Oxide, Eukaryotic Initiation Factor-2, Apoptosis, Protein Folding, eIF-2 Kinase, Mice

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Endoplasmic Reticulum Stress and Diabetes Mellitus.

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks