Endoplasmic Reticulum Stress Links Oxidative Stress to Impaired Pancreatic Beta-Cell Function Caused by Human Oxidized LDL

Plaisance, Valérie; Brajkovic, Saska; Tenenbaum, Mathie; Favre, D.; Ezanno, Hélène; Bonnefond, Amélie; Bonner, Caroline; Gmyr, Valéry; Kerr–Conte, Julie; Gauthier, Benoit R.; Widmann, Christian; Waeber, Gérard; Pattou, François; Froguel, Philippe; Abderrahmani, Amar

doi:10.1371/journal.pone.0163046

Cited by 81 publications

(58 citation statements)

References 41 publications

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“…Recent studies support the view that ER protein folding pathways are highly correlated with ROS production [4,87]. In ER, redox homeostasis is crucial for the protein folding process and disulfide bond formation [89].…”

Section: Vicious Sequence Of Events Between Endoplasmic Reticulum mentioning

confidence: 90%

Endoplasmic Reticulum Stress and Oxidative Stress: A Vicious Nexus Implicated in Bowel Disease Pathophysiology

Chong

Shastri

Eri

2017

IJMS

238

127

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The endoplasmic reticulum (ER) is a complex protein folding and trafficking organelle. Alteration and discrepancy in the endoplasmic reticulum environment can affect the protein folding process and hence, can result in the production of misfolded proteins. The accumulation of misfolded proteins causes cellular damage and elicits endoplasmic reticulum stress. Under such stress conditions, cells exhibit reduced functional synthesis, and will undergo apoptosis if the stress is prolonged. To resolve the ER stress, cells trigger an intrinsic mechanism called an unfolded protein response (UPR). UPR is an adaptive signaling process that triggers multiple pathways through the endoplasmic reticulum transmembrane transducers, to reduce and remove misfolded proteins and improve the protein folding mechanism, in order to improve and maintain endoplasmic reticulum homeostasis. An increasing number of studies support the view that oxidative stress has a strong connection with ER stress. During the protein folding process, reactive oxygen species are produced as by-products, leading to impaired reduction-oxidation (redox) balance conferring oxidative stress. As the protein folding process is dependent on redox homeostasis, the oxidative stress can disrupt the protein folding mechanism and enhance the production of misfolded proteins, causing further ER stress. It is proposed that endoplasmic reticulum stress and oxidative stress together play significant roles in the pathophysiology of bowel diseases.

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Section: Vicious Sequence Of Events Between Endoplasmic Reticulum mentioning

confidence: 90%

Endoplasmic Reticulum Stress and Oxidative Stress: A Vicious Nexus Implicated in Bowel Disease Pathophysiology

Chong

Shastri

Eri

2017

IJMS

238

127

View full text Add to dashboard Cite

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“…These sensors signal and initiate transcriptional and translational programs related to amelioration of the stress, including silencing of most protein synthesis and augmenting the synthesis of chaperone molecules, promoting proteasome‐mediated degradation. In cases where these unfolding protein response elements (UPREs: PERK, IRE1 and ATF6) are unable to overcome the stress, apoptotic pathways are activated . Chemical inhibition of sEH and genetic deletion has been demonstrated to decrease ER stress .…”

Section: Discussionmentioning

confidence: 99%

“…PERK, IRE1 and ATF6) are unable to overcome the stress, apoptotic pathways are activated. [48][49][50][51][52][53] Chemical inhibition of sEH and genetic deletion has been demonstrated to decrease ER stress. [53][54][55] The cardioprotective effect of sEH inhibitors in this model could therefore be due to mitigation of ER stress.…”

Section: Treatment With Seh Inhibitors Decreases Endothelial Dysfunmentioning

confidence: 99%

Inhibitors of soluble epoxide hydrolase minimize ischemia‐reperfusion‐induced cardiac damage in normal, hypertensive, and diabetic rats

Islam

Patil

Goswami

et al. 2017

Cardiovascular Therapeutics

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Aim We designed a study to evaluate the cardioprotective effect of two soluble epoxide hydrolase (sEH) inhibitors, 1-(1-propanoylpiperidin-4-yl)-3-(4-trifluoromethoxy)phenyl)urea (TPPU) and trans-4-{4-[3-(4-trifluoromethoxyphenyl)-ureido]cyclohexyloxy}benzoic acid (t-TUCB), in ischemia-reperfusion (IR) model. Methods Cardioprotective effects of the sEH inhibitors were evaluated against IR-induced myocardial damage in hearts from normal, hypertensive and diabetic rats using Langendorff’s apparatus. In addition, the effect of sEH inhibitors on endothelial function was evaluated in vitro and ex vivo using isolated rat thoracic aorta. Results IR increased the myocardial damage in hearts from normal rats. IR-induced myocardial damage was augmented in hearts isolated from hypertensive and diabetic rats. Myocardial damage as evident from increase in the activities of lactate dehydrogenase (LDH) and creatine kinase-MB (CK-MB) in heart perfusate was associated with significant decrease in the heart rate and developed tension, and increase in the resting tension in isolated heart. Both sEH inhibitors protected the heart in normal, hypertensive and diabetic rats subjected to IR injury. The sEH inhibitor t-TUCB relaxed phenylephrine pre-contracted aorta from normal rats. Relaxant effect of acetylcholine (ACh) was reduced in aortas from diabetic and hypertensive rats compared to normal rats. Pre-treatment of sEH inhibitors to diabetic and hypertensive rats increased relaxant effect of ACh on aortas isolated from these rats. Conclusions Prophylactic treatment with sEH inhibitors decreased myocardial damage due to IR, hypertension and diabetes, and decreased endothelial dysfunction created by diabetes and hypertension. Therefore, inhibitors of sEH are useful probes to study cardiovascular pathology and inhibition of the sEH is a potential approach in the management of IR-induced cardiac damage and endothelial dysfunction related cardiovascular disorders.

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“…Recent studies have suggested that ER signalling pathways correlate with ROS production. 26,45,46 In response to ERS, the activation of CHOP was shown to promote ROS production and to indirectly disturb reduction-oxidation (redox) homeostasis causing further induction of oxidative stress. 47,48 In addition, ROS has also been reported to induce ERS that is involved in the CHOP-Wnt pathway.…”

Section: Discussionmentioning

confidence: 99%

Long non‐coding RNA MEG3 knockdown attenuates endoplasmic reticulum stress‐mediated apoptosis by targeting p53 following myocardial infarction

Zhao

Chen

et al. 2019

J Cellular Molecular Medi

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Mounting evidence has indicated that long non‐coding RNA maternally expressed gene 3 (lncRNA MEG3) regulates cell apoptosis, and is involved in a variety of diseases. However, its exact role in myocardial infarction (MI) has not been fully elucidated. In the present study, we firstly observed that the expression levels of the lncRNA MEG3 in infarct hearts and hypoxic neonatal mice ventricular myocytes (NMVMs) were up‐regulated by quantitative real‐time PCR (qRT‐PCR). Then, we knocked down lncRNA MEG3 by lentiviral delivery in the myocardial border region following multipoint injection. Following 28 days of MI, the lncRNA MEG3 knockdown mice indicated better cardiac function, and less cardiac remodelling by ultrasonic cardiogram and histological analysis. In addition, we indicated that lncRNA MEG3 knockdown reduced myocyte apoptosis and reactive oxygen species production in MI mice model and hypoxic NMVMs. Furthermore, we revealed that knockdown of lncRNA MEG3 protected against endoplasmic reticulum stress (ERS)‐mediated myocardial apoptosis including the induction of PERK‐eIF2α and caspase 12 pathways. At last, we provided evidence that p53 was identified as a protein target of lncRNA MEG3 to regulate NF‐κB‐ and ERS‐associated apoptosis. Taken collectively, our findings demonstrated that lncRNA MEG3 knockdown exerted cardioprotection by reducing ERS‐mediated apoptosis through targeting p53 post‐MI.

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Endoplasmic Reticulum Stress Links Oxidative Stress to Impaired Pancreatic Beta-Cell Function Caused by Human Oxidized LDL

Cited by 81 publications

References 41 publications

Endoplasmic Reticulum Stress and Oxidative Stress: A Vicious Nexus Implicated in Bowel Disease Pathophysiology

Endoplasmic Reticulum Stress and Oxidative Stress: A Vicious Nexus Implicated in Bowel Disease Pathophysiology

Inhibitors of soluble epoxide hydrolase minimize ischemia‐reperfusion‐induced cardiac damage in normal, hypertensive, and diabetic rats

Long non‐coding RNA MEG3 knockdown attenuates endoplasmic reticulum stress‐mediated apoptosis by targeting p53 following myocardial infarction

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