S-Nitrosation of thioredoxin in the nitrogen monoxide/superoxide system activates apoptosis signal-regulating kinase 1

Yasinska, Inna M.; Kozhukhar, Anna; Sumbayev, Vadim V.

doi:10.1016/j.abb.2004.06.004

Cited by 32 publications

(20 citation statements)

References 26 publications

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“…In this study, we also show that Cys 32 and Cys 35 , which are in the active site of Trx1, were not nitrosylated by GSNO but became oxidized to a disulfide bond. This finding is in accordance with previous reports (33).…”

Section: Discussionsupporting

confidence: 53%

Regulation of the Catalytic Activity and Structure of Human Thioredoxin 1 via Oxidation and S-Nitrosylation of Cysteine Residues

Hashemy¹,

Holmgren

2008

Journal of Biological Chemistry

173

146

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Section: Discussionsupporting

confidence: 53%

Regulation of the Catalytic Activity and Structure of Human Thioredoxin 1 via Oxidation and S-Nitrosylation of Cysteine Residues

Hashemy¹,

Holmgren

2008

Journal of Biological Chemistry

173

146

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“…First, the AT 1 receptor-stretch regulation of cardiac Kv4.3 expression could be activated in response to physiological and pathological changes in blood pressure. Second, because ASK1 is activated by a variety of ROS, 16,19 different ROS sources could trigger destabilization of Kv4.3 mRNA. For example, cardiac mitochondria generate ROS after reperfusion following ischemia.…”

Section: Discussionmentioning

confidence: 99%

Angiotensin II and Stretch Activate NADPH Oxidase to Destabilize Cardiac Kv4.3 Channel mRNA

Zhou

Ziegler

Birder

et al. 2006

Circulation Research

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Abstract-Pathological and physiological hypertrophy of the heart is associated with decreased expression of the Kv4.3 transient outward current (I to ) channel. The downregulation of channel mRNA and protein, which may be proarrhythmic, is recapitulated with cultured neonatal rat ventricular myocytes treated with angiotensin II (Ang II). Here we show that the 4.9 kb 3Ј untranslated region (3Ј UTR) of the Kv4.3 channel transcript confers Ang II sensitivity to a promoter-reporter construct. In contrast, Kv4.2 and Kv1.5 3Ј-UTR sequences are insensitive to Ang II. Both Kv4.3 3Ј-UTR reporter mRNA and activity are decreased in Ang II-treated cardiac myocytes, in accordance with a decrease in mRNA stability. This regulation is mediated by Ang II type 1 (AT 1 ) receptors and abolished by NADPH oxidase inhibitors and dominant negative rac. The Ang II effect is also blocked by expression of superoxide dismutase (SOD) Key Words: potassium channel Ⅲ angiotensin Ⅲ stretch Ⅲ NADPH oxidase Ⅲ ROS Ⅲ mRNA stability C ardiac hypertrophy, caused by congestive heart failure, hypertension, and pregnancy, is associated with a decrease in the transient outward current (I to ) in ventricular cardiac myocytes. 1,2 The suppression of ventricular I to is thought to promote calcium influx and myocyte contraction in the early adaptive phase of hypertrophy but may eventually induce calcium overloading of the sarcoplasmic reticulum, leading to arrhythmic firing and sudden death. 3,4 The reduction of I to is likely related to the downregulation of Kv4.3 mRNA and protein that occurs with congestive heart failure in humans and hypertension in animals. 5,6 The finding that the latter effect is blocked by angiotensin converting enzyme (ACE) inhibition implicated angiotensin II (Ang II) in the control of cardiac Kv4.3 gene expression. 7 Follow-up experiments have shown that Ang II acts directly on cultured neonatal rat ventricular myocytes via Ang II type 1 (AT 1 ) receptors to decrease Kv4.3 mRNA and protein. 8 However, the onset of the effect was more rapid than the turnover of the channel mRNA, and Ang II did not act on the Kv4.3 promoter. 8 This indirect evidence led to the proposal that Ang II destabilizes Kv4.3 mRNA in cardiac myocytes. In contrast, the ␣ 1 -adrenergic receptor agonist phenylephrine downregulated Kv4.3 promoter activity, 8 suggesting that G q -mediated signaling shared by AT 1 receptors and ␣ 1 -adrenergic receptors might not be involved in this Ang II effect on mRNA stability.,It has been recently demonstrated that AT 1 receptors can act via the small G protein rac to stimulate NADPH oxidase in cardiac myocytes. 9,10 NADPH oxidase produces superoxide, which serves as a physiological reactive oxygen species (ROS) messenger within the cell. Separate studies have also shown that AT 1 receptors, rac and ROS production are activated by mechanical stretch of cardiac myocytes. 11-13 Thus, we hypothesized that Ang II and stretch can act via the AT 1 receptor-NADPH oxidase pathway to regulate cardiac myocyte Kv4.3 mRNA stability. Here...

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“…At later stages, S-nitrosation of ASK1 also takes place (Sumbayev 2008b). S-nitrosation of ASK1 could lead to a decrease in its catalytic activity (Park et al 2004;Yasinska et al 2004). Therefore, these two mechanisms (the PI3K pathway and S-nitrosation) possibly influence the activity of ASK1, allowing its pro-inflammatory function but preventing the enzyme from inducing apoptosis.…”

Section: Biochemical Mechanisms Leading To the Accumulation/ Activatimentioning

confidence: 99%

Hypoxia-inducible Factor 1 as one of the “Signaling Drivers” of Toll-like Receptor-Dependent and Allergic Inflammation

Sumbayev

Nicholas

2010

Arch. Immunol. Ther. Exp.

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Hypoxia-inducible factor 1 (HIF-1) is a heterodimeric transcription complex which plays a crucial role in cellular adaptation to low oxygen availability. In the last years there has been increasing evidence about the role of this factor in inflammatory/innate immune reactions. It has also been found to contribute to different types of allergic inflammation. In this review the current knowledge about the accumulation and role of HIF-1 in Toll-like receptor-mediated and allergic inflammation is summarized. Differential biochemical mechanisms employed to stabilize the protein in different cases are discussed.

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S-Nitrosation of thioredoxin in the nitrogen monoxide/superoxide system activates apoptosis signal-regulating kinase 1

Cited by 32 publications

References 26 publications

Regulation of the Catalytic Activity and Structure of Human Thioredoxin 1 via Oxidation and S-Nitrosylation of Cysteine Residues

Regulation of the Catalytic Activity and Structure of Human Thioredoxin 1 via Oxidation and S-Nitrosylation of Cysteine Residues

Angiotensin II and Stretch Activate NADPH Oxidase to Destabilize Cardiac Kv4.3 Channel mRNA

Hypoxia-inducible Factor 1 as one of the “Signaling Drivers” of Toll-like Receptor-Dependent and Allergic Inflammation

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