Nitrosative Stress–Induced <i>S</i>-Glutathionylation of Protein Disulfide Isomerase Leads to Activation of the Unfolded Protein Response

Townsend, Danyelle M.; Manevich, Yefim; He, Lin; Xiong, Ying; Bowers, Robert R.; Hutchens, Steven; Tew, Kenneth D.

doi:10.1158/0008-5472.can-09-0493

Cited by 120 publications

(137 citation statements)

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“…associate with various pathologies, such as diabetes, atherosclerosis, inflammatory, and cancer [11,[14][15][16]. In the present study, serum S-glutathionylated proteins were significantly increased in patients with CS, suggesting an imbalance of the redox state and protein thiols in the serum.…”

Section: Altered Levels Of S-glutathionylated Proteins Have Been Recementioning

confidence: 50%

“…Recent studies have demonstrated that S-glutathionylation can produce discrete modulatory effects on protein function [12,13]. Therefore, S-glutathionylated proteins have been actively investigated with reference to problems of biological interest and as potential biomarkers of human diseases associated with oxidative stress [11,[14][15][16]. Nakamoto M,et al page 4 In this study, we developed an antibody to specifically recognize the S-glutathionylated proteins, and then we investigated whether the serum S-glutathionylated proteins increased in patients with different stages of CS.…”

Section: Introductionmentioning

confidence: 99%

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Serum S-glutathionylated proteins as a potential biomarker of carotid artery stenosis

Nakamoto

Hirose

Kawakatsu

et al. 2012

Clinical Biochemistry

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Section: Altered Levels Of S-glutathionylated Proteins Have Been Recementioning

confidence: 50%

Section: Introductionmentioning

confidence: 99%

Serum S-glutathionylated proteins as a potential biomarker of carotid artery stenosis

Nakamoto

Hirose

Kawakatsu

et al. 2012

Clinical Biochemistry

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“…In addition, the application of peroxynitrite (ONOO -) or Snitrosoglutathione (GSNO, 10-500 lM) to induce S-glutathionylation is also found in the literature (12,38,125,129). The application of peroxynitrite is of high physiological relevance but as peroxynitrite can also induce other modification including S-nitrosylation, additional experiments should be performed to further dissect the exact modification mechanism.…”

Section: Induction Of S-glutathionylationmentioning

confidence: 99%

“…After that, the cells are lysed and streptavidinconjugated agarose beads (or magnetic beads) are used to pull down the BioGEE-conjugated protein complex, and the protein of interest is detected by the protein-specific antibodies (145). Alternatively, the BioGEE-protein complex could be immunoprecipitated (IP) first with specific antibodies against the protein of interest and then immunoblotted (IB) with streptavidin or anti-biotin antibody (125). A variation of this experiment is to avoid using BioGEE.…”

Section: Biochemical Testsmentioning

confidence: 99%

S-Glutathionylation of Ion Channels: Insights into the Regulation of Channel Functions, Thiol Modification Crosstalk, and Mechanosensing

Yang

Jin²,

Jiang³

2014

Antioxidants & Redox Signaling

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Significance: Ion channels control membrane potential, cellular excitability, and Ca ++ signaling, all of which play essential roles in cellular functions. The regulation of ion channels enables cells to respond to changing environments, and post-translational modification (PTM) is one major regulation mechanism. Recent Advances: Many PTMs (e.g., S-glutathionylation, S-nitrosylation, S-palmitoylation, S-sulfhydration, etc.) targeting the thiol group of cysteine residues have emerged to be essential for ion channels regulation under physiological and pathological conditions. Critical Issues: Under oxidative stress, S-glutathionylation could be a critical PTM that regulates many molecules. In this review, we discuss S-glutathionylation-mediated structural and functional changes of ion channels. Criteria for testing S-glutathionylation, methods and reagents used in ion channel S-glutathionylation studies, and thiol modification crosstalk, are also covered. Mechanotransduction, and S-glutathionylation of the mechanosensitive K ATP channel, are discussed. Future Directions: Further investigation of the ion channel S-glutathionylation, especially the physiological significance of S-glutathionylation and thiol modification crosstalk, could lead to a better understanding of the thiol modifications in general and the ramifications of such modifications on cellular functions and related diseases. Antioxid. Redox Signal. 20, 937-951.

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“…Other substrates for PDI that also have their intermediates identified are lysozyme (4 disulfides) (van den and 2 modified RNases, RNaseT1 (2 disulfides) and glutathionylated RNAseT1, (Ruoppolo and Freedman, 1995;Ruoppolo et al, 1996). Reduced RNaseT1 behaves in the assay as reduced RNase, while the glutathionylated substrate has to be deglutathionylated in the first step, which may also be mediated by PDI Townsend et al, 2009). Transposition of oxidative refolding assays to biological samples relies on the same difficulties as those of isomerase activity discussed previously.…”

Section: An Overview Of Pdi Activity Assaysmentioning

confidence: 99%

Medidas das atividades da Dissulfeto Isomerase Proteica: uma análise crítica

Watanabe¹

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AgradecimentosÀ Denise de Castro Fernandes pela orientação, inspiração, compreensão e apoio em todos os momentos nessa fase, exemplo de pessoa que sempre irei me inspirar.Ao Prof. Francisco Laurindo pelo apoio e as conversas científicas, que me inspiraram sobre o que é realmente fazer ciência.À minha família (Cecília, Eduardo, Marcela, Yoshio e Ytiro) pelo apoio e compreensão incondicional.Ao Danilo por estar ao meu lado, com carinho e compreensão, nesta etapa que certamente será importante para futuras etapas em nossa vida.Ao João Wosniak Jr pelo apoio e ajuda cultivo celular, na otimização de condições experimentais e em todas as minhas apresentações.À Maria Bertoline, que sempre me ajudou no HPLC e pela carinhosa companhia no laboratório.Aos colegas de laboratório: Ana Moretti, Angélica, Carol, Daniela, Jéssyca, Júlia, Laura, Leonora, Luciana, Raquel, Renata, Phelipe, Thais, Thalita, Vanda, Victor. substantially from in vitro studies using purified PDI and chimeras. In these experimental scenarios, PDI reductase and chaperone are readily approachable. LISTA DE ABREVIATURASHowever, isomerase activity, the hallmark of PDI family, is significantly complex.Assessment of PDI roles in cells and tissues mainly relies on gain-or loss-of-function experiments. However, there is limited information regarding correlation of these results with PDI activities. In this manuscript, we put together the main methods described for measuring the four PDI activities: thiol reductase, thiol oxidase, thiol isomerase and chaperone, with emphasis on controls and critical interferents, such as detergentcontaining buffers. We also discuss the transposition of these methods from purified PDI to cellular or in vivo samples, with critical thoughts about the interpretation of results.Keywords: Protein disulfide isomerase, Chaperone, Isomerization, Oxidation. INTRODUÇÃO Estrutura da Dissulfeto Isomerase ProteicaA Dissulfeto Isomerase Proteíca -PDI (também denominada PDIA1 ou no genoma humano, gene P4HB) é uma chaperona redox pertencente ao grupo de ditiol-proteínas da superfamília da tiorredoxina ( Fig. 1 A PDI é uma proteína de 55 kDa formada por quatro domínios tiorredoxina (denominados a-b-b'-a '), sendo que os sítios catalíticos contém 2 cisteínas (motivo WCGHC) e estão presentes nos dois domínios a e a' (Fig. 1 Estudos de cristalização da PDI de levedura realizados em diferentes temperaturas (4°C versus 22°) (Tian e col., 2006; Tian e col., 2008) descreveram uma proteína altamente flexível, que pode portanto, ajustar sua estrutura para ligar substratos de diferentes tamanhos e conformações, de tal forma que permite a acessibilidade dos sítios redox da PDI para tióis críticos dos substratos. Nestes trabalhos observou-se que a PDI de levedura pode apresentar duas distintas conformações, dependendo da temperatura de cristalização: i) uma forma em "U", na qual os dois sítios catalíticos estão frente a frente e os resíduos hidrofóbicos estão na base rígida do "U" (Fig. 3) ou ii) uma forma aberta, denominada "forma de barco". Além disso, ...

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Nitrosative Stress–Induced S-Glutathionylation of Protein Disulfide Isomerase Leads to Activation of the Unfolded Protein Response

Abstract: The rapid proliferation of cancer cells mandates a high protein turnover. The endoplasmic reticulum (ER) is intimately involved in protein processing.

Cited by 120 publications

References 39 publications

Serum S-glutathionylated proteins as a potential biomarker of carotid artery stenosis

Serum S-glutathionylated proteins as a potential biomarker of carotid artery stenosis

S-Glutathionylation of Ion Channels: Insights into the Regulation of Channel Functions, Thiol Modification Crosstalk, and Mechanosensing

Medidas das atividades da Dissulfeto Isomerase Proteica: uma análise crítica

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