Thioredoxin-dependent redox regulation of the antioxidant responsive element (ARE) in electrophile response

Kim, Yong-Chul; Yamaguchi, Yoshimi; Kondo, Norihiko; Masutani, Hiroshi; Yodoi, Junji

doi:10.1038/sj.onc.1206369

Cited by 122 publications

(74 citation statements)

References 26 publications

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“…Moreover, a growing amount of data demonstrates that the reduced state of specific cysteines of several transcription factors is maintained by proteins such as Trx1 to ensure the DNA binding capability (8). The nuclear erythroid factor 2-related factor 2 (Nrf2) is a typical activator of antioxidantresponsive elements (AREs) (9) that, once activated, induces the antioxidant and detoxifying response (10,11). Nrf2 is normally sequestered in the cytoplasm in an inactive complex with kelchlike ECH-associated protein 1 (Keap1), which, upon oxidation of critical cysteines, dissociates from Nrf2, leading to its translocation into the nucleus (12).…”

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confidence: 99%

Redox Mechanisms Involved in the Selective Activation of Nrf2-mediated Resistance Versus p53-dependent Apoptosis in Adenocarcinoma Cells

Piccirillo

Filomeni

Brüne

et al. 2009

Journal of Biological Chemistry

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We have investigated the role of reactive oxygen species and thiol-oxidizing agents in the induction of cell death and have shown that adenocarcinoma gastric (AGS) cells respond differently to the oxidative challenge according to the signaling pathways activated. In particular, apoptosis in AGS cells is induced via the mitochondrial pathway upon treatment with thiol-oxidizing agents, such as diamide. Apoptosis is associated with persistent oxidative damage, as evidenced by the increase in carbonylated proteins and the expression/activation of DNA damage-sensitive proteins histone H2A.X and DNA-dependent protein kinase. Resistance to hydrogen peroxide is instead associated with Keap1 oxidation and rapid translocation of Nrf2 into the nucleus. Sensitivity to diamide and resistance to hydrogen peroxide are correlated with GSH redox changes, with diamide severely increasing GSSG, and hydrogen peroxide transiently inducing protein-GSH mixed disulfides. We show that p53 is activated in response to diamide treatment by the oxidative induction of the Trx1/p38 MAPK signaling pathway. Similar results were obtained with another carcinoma cell line, CaCo2, indicating that these findings are not limited to AGS cells. Our data suggest that thiol-oxidizing agents could be exploited as inducers of apoptosis in tumor histotypes resistant to ROS-producing chemotherapeutics.

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confidence: 99%

Redox Mechanisms Involved in the Selective Activation of Nrf2-mediated Resistance Versus p53-dependent Apoptosis in Adenocarcinoma Cells

Piccirillo

Filomeni

Brüne

et al. 2009

Journal of Biological Chemistry

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“…Ref-1, a redox factor of AP1, was previously demonstrated to reduce a conserved cysteine residue in the DNA binding domains of AP1 family members and enhances their binding to the AP1 binding sequence (1,74). Ref-1 was also shown to be activated during oxidative stress, at least in part, by the mechanism of enhanced nuclear translocation of Ref-1 itself (4, 63) or thioredoxin (30,34). In this study, we showed that Ref-1 is localized in both the nucleus and cytoplasm in K562 cells and that hemin as well as t-BHQ treatment induced nuclear accumulation of Ref-1 (Fig.…”

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confidence: 99%

Hemin-Mediated Regulation of an Antioxidant-Responsive Element of the Human Ferritin H Gene and Role of Ref-1 during Erythroid Differentiation of K562 Cells

Iwasaki

Mackenzie

Hailemariam

et al. 2006

Molecular and Cellular Biology

101

108

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“…It is a critical factor in the activation of several redox-sensitive transcription factors, including NF-kappaB and AP1 complexes, which are important participants regulating oxidative status [Gauss et al 2007;Hirota et al 1999;Manea et al 2007;Nordberg and Arnér 2001]. Moreover, TXN gene expression is dependent on oxidative status [Kim et al 2003;Levy et al 2009;Um et al 2011]. Thus, TXN may be used as indicative of both the cellular and the organismal antioxidant system's activation state and the oxidative status stabilization capacity.…”

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confidence: 99%

Oxidative status shifts in uterine cervical incompetence patients

Zolotukhin

Александрова

Goncharova

et al. 2013

Systems Biology in Reproductive Medicine

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Uterine cervical incompetence (UCI) is a pregnancy complication affecting about 10% of the pregnancies in the western world. Studying the etiology of the UCI requires a specific approach adequate for this highly heterogenous syndrome. Oxidative status disorders are associated with various pathologies, including pregnancy complications. As such, general oxidative status profiling is a promising methodology to treat UCI. We aimed at assaying the closely interrelated oxidative status markers in the uterine cervical incompetence patients by means of the systems biology-oriented approach. Chemiluminescent assay, circulating thioredoxin 1 protein, uric acid, and homocysteine level measurements were used to assess the character of the oxidative status regulation in the UCI patients. We found UCI to be associated with the atypical plasma oxidative status deregulation; UCI plasma samples demonstrated lowered proneness to the pro-oxidative processes, and this was not due to the excessive antioxidant activity. There were neither signs of oxidative stress nor destructive pro-oxidant feedforward circuit locking in the UCI group. We also report increased circulating levels of uric acid in the UCI patients.

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Thioredoxin-dependent redox regulation of the antioxidant responsive element (ARE) in electrophile response

Cited by 122 publications

References 26 publications

Redox Mechanisms Involved in the Selective Activation of Nrf2-mediated Resistance Versus p53-dependent Apoptosis in Adenocarcinoma Cells

Redox Mechanisms Involved in the Selective Activation of Nrf2-mediated Resistance Versus p53-dependent Apoptosis in Adenocarcinoma Cells

Hemin-Mediated Regulation of an Antioxidant-Responsive Element of the Human Ferritin H Gene and Role of Ref-1 during Erythroid Differentiation of K562 Cells

Oxidative status shifts in uterine cervical incompetence patients

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