Nε-carboxymethyllysine-mediated endoplasmic reticulum stress promotes endothelial cell injury through Nox4/MKP-3 interaction

Lee, Wen‐Jane; Sheu, Wayne Huey‐Herng; Liu, Shing‐Hwa; Yi, Yu-Chiao; Chen, Wei-Chih; Lin, Shih‐Yi; Liang, Kae‐Woei; Shen, Chin-Chang; Yeh, Hsiang-Yu; Lin, Li-Yun; Tsai, Yi-Ching; Tien, Hsing-Ru; Lee, Maw-Rong; Yang, Tzung-Jie; Sheu, Meei-Ling

doi:10.1016/j.freeradbiomed.2014.06.015

Cited by 15 publications

(3 citation statements)

References 27 publications

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“…Furthermore, CML had no effect on the myeloperoxidase (MPO) activity in the colitis groups, suggesting that injury was mediated by neutrophil-independent mechanisms. CML induces endoplasmic reticulum stress injuring cells via different pathways that could partly explain this phenomenon [4]. Moreover, the study revealed that weight change inversely correlated with food intake by mice, consistent with metabolic changes associated with chronic consumption of CML, supported by an in vitro study [5] in which CML impaired basal glucose uptake while enhancing lipid accumulation in adipocytes.…”

supporting

confidence: 57%

Modulation of Gut Microbiota by Maillard Reaction Products in Intestinal Inflammation: Are We What We Eat?

Fabisiak

2017

Dig Dis Sci

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supporting

confidence: 57%

Modulation of Gut Microbiota by Maillard Reaction Products in Intestinal Inflammation: Are We What We Eat?

Fabisiak

2017

Dig Dis Sci

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“…LPS-associated myocardial damage could be attenuated by MKP-1 through reducing inflammatory response [63]. Oxidative stress-mediated endothelial cell injury was associated with ER stress due to a loss of MKP-1 activity [64,65]. Overexpression of MKP-1 reduced ER stress, resulting in increased neural cell survival [66].…”

Section: Discussionmentioning

confidence: 99%

[Retracted] MKP‐1 Overexpression Reduces Postischemic Myocardial Damage through Attenuation of ER Stress and Mitochondrial Damage

Hou¹,

Li²,

Chen

et al. 2021

Oxidative Medicine and Cellular Longevity

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Mitochondrial dysfunction and endoplasmic reticulum (ER) stress contribute to postischemic myocardial damage, but the upstream regulatory mechanisms have not been identified. In this study, we analyzed the role of mitogen-activated protein kinase (MAPK) phosphatase 1 (MKP-1) in the regulation of mitochondrial function and ER stress in hypoxic cardiomyocytes. Our results show that MKP-1 overexpression sustains viability and reduces hypoxia-induced apoptosis among H9C2 cardiomyocytes. MKP-1 overexpression attenuates ER stress and expression of ER stress genes and improves mitochondrial function in hypoxia-treated H9C2 cells. MKP-1 overexpression also increases ATP production and mitochondrial respiration and attenuates mitochondrial oxidative damage in hypoxic cardiomyocytes. Moreover, our results demonstrate that ERK and JNK are the downstream signaling targets of MKP-1 and that MKP-1 overexpression activates ERK, while it inhibits JNK. Inhibition of ERK reduces the ability of MKP-1 to preserve mitochondrial function and ER homeostasis in hypoxic cardiomyocytes. These results show that MKP-1 plays an essential role in the regulation of mitochondrial function and ER stress in hypoxic H9C2 cardiomyocytes through normalization of the ERK pathway and suggest that MKP-1 may serve as a novel target for the treatment of postischemic myocardial injury.

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“…Collagen‐binding CML that infect umbilical cord blood endothelial cells was found to significantly trigger endothelial cell injury via a pathway of tyrosine phosphatase Src homology phosphatase‐1‐regulated VEGFR‐2 dephosphorylation . Another study conducted by Lee et al showed that, through the NADPH oxidase 4 (Nox4)/mitogen‐activated protein kinase phosphatase 3, CML‐collagen made cells vulnerable to endoplasmic reticulum stress and endothelial cell apoptosis.…”

Section: Introductionmentioning

confidence: 99%

Studies on mechanism of free Nε‐(carboxymethyl)lysine‐induced toxic injury in mice

Wang

Hao

Liu

et al. 2019

J Biochem & Molecular Tox

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Nε‐(carboxymethyl)lysine (CML), which is a compound produced when food is processed, has aroused concern in recent years because of its potentially dangerous effects. This study aimed to investigate the mechanism of free CML‐induced toxic injury in mice. The inflammatory cytokine tumor necrosis factor‐α, transforming growth factor‐β, vascular cell adhesion molecule‐1 mRNA expression levels of CML‐infected mice liver and kidney tissues significantly increased. While CML receptor—receptor for advanced glycation end products (RAGE) protein expression in male mice liver tissue had a more significant change than the control group, there was no significant difference in other dose groups compared with the control group. In conclusion, the foodborne free CML can be induced by oxidative stress and immune response to liver and kidney tissue injury in mice. Additionally, the free CML may also bind to RAGE, which activates the downstream inflammatory pathway.

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Nε-carboxymethyllysine-mediated endoplasmic reticulum stress promotes endothelial cell injury through Nox4/MKP-3 interaction

Cited by 15 publications

References 27 publications

Modulation of Gut Microbiota by Maillard Reaction Products in Intestinal Inflammation: Are We What We Eat?

Modulation of Gut Microbiota by Maillard Reaction Products in Intestinal Inflammation: Are We What We Eat?

[Retracted] MKP‐1 Overexpression Reduces Postischemic Myocardial Damage through Attenuation of ER Stress and Mitochondrial Damage

Studies on mechanism of free Nε‐(carboxymethyl)lysine‐induced toxic injury in mice

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