Direct methods for detection of protein S-nitrosylation

Devarie‐Baez, Nelmi O.; Zou, Dehui; Li, Sheng; Whorton, A. R.; Xian, Ming

doi:10.1016/j.ymeth.2013.04.018

Cited by 32 publications

(18 citation statements)

References 39 publications

(38 reference statements)

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“…An analysis of a wide variety of RSNO measurement techniques, including the biotin switch, has established that artifacts are common when measuring RSNOs and it is not always possible to identify which thiols have been S-nitrosated (Giustarini et al, 2003). Newer techniques have become available in recent years (Chen et al, 2013; Devarie-Baez et al, 2013), such as tandem mass spectrometry (MS/MS) of S-nitrosated protein thiols (Murray et al, 2012; Ulrich et al, 2013), that are highly quantitative. Beyond the problem of quantitation, it has been proposed that other thiol modifications such as dithiol/disulfide exchange, S-glutathionylation, and oxidation, may affect signaling more readily than do RSNOs (Lancaster, 2008), and should be investigated along with S-nitrosation.…”

Section: Gsnor: Health and Diseasementioning

confidence: 99%

The role of S-nitrosoglutathione reductase (GSNOR) in human disease and therapy

Barnett

Buxton

2017

Critical Reviews in Biochemistry and Molecular Biology

119

101

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S-nitrosoglutathione reductase (GSNOR), or ADH5, is an enzyme in the alcohol dehydrogenase (ADH) family. It is unique when compared to other ADH enzymes in that primary short-chain alcohols are not its principle substrate. GSNOR metabolizes S-nitrosoglutathione (GSNO), S-hydroxymethylglutathione (the spontaneous adduct of formaldehyde and glutathione), and some alcohols. GSNOR modulates reactive nitric oxide (•NO) availability in the cell by catalyzing the breakdown of GSNO, and indirectly regulates S-nitrosothiols (RSNOs) through GSNO-mediated protein S-nitrosation. The dysregulation of GSNOR can significantly alter cellular homeostasis, leading to disease. GSNOR plays an important regulatory role in smooth muscle relaxation, immune function, inflammation, neuronal development, and cancer progression, among many other processes. In recent years, the therapeutic inhibition of GSNOR has been investigated to treat asthma, cystic fibrosis and interstitial lung disease (ILD). The direct action of •NO on cellular pathways, as well as the important regulatory role of protein S-nitrosation, are closely tied to GSNOR regulation and define this enzyme as an important therapeutic target.

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Section: Gsnor: Health and Diseasementioning

confidence: 99%

The role of S-nitrosoglutathione reductase (GSNOR) in human disease and therapy

Barnett

Buxton

2017

Critical Reviews in Biochemistry and Molecular Biology

119

101

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“…However, with the MALDI source the peptides bearing this mass addition are decomposed upon laser ionization, which makes their identification difficult (Kaneko and Wada, 2003 ). The ESI source is most commonly used to probe this mass increase and has been addressed in some recent reviews (Foster, 2012 ; Chen et al, 2013 ; Devarie-Baez et al, 2013 ; Chicooree et al, 2014 ). For instance, peroxiredoxin II E (PrxII E) was shown to undergo S-nitrosylation in A. thaliana leaves infected with an avirulent strain of the bacterial pathogen Pseudomonas syringae pv.…”

Section: Identification Of Plant S-nitrosylated Proteins: Methodologimentioning

confidence: 99%

Protein S-nitrosylation: specificity and identification strategies in plants

et al. 2015

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The role of nitric oxide (NO) as a major regulator of plant physiological functions has become increasingly evident. To further improve our understanding of its role, within the last few years plant biologists have begun to embrace the exciting opportunity of investigating protein S-nitrosylation, a major reversible NO-dependent post-translational modification (PTM) targeting specific Cys residues and widely studied in animals. Thanks to the development of dedicated proteomic approaches, in particular the use of the biotin switch technique (BST) combined with mass spectrometry, hundreds of plant protein candidates for S-nitrosylation have been identified. Functional studies focused on specific proteins provided preliminary comprehensive views of how this PTM impacts the structure and function of proteins and, more generally, of how NO might regulate biological plant processes. The aim of this review is to detail the basic principle of protein S-nitrosylation, to provide information on the biochemical and structural features of the S-nitrosylation sites and to describe the proteomic strategies adopted to investigate this PTM in plants. Limits of the current approaches and tomorrow's challenges are also discussed.

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“…Therefore, there is still a great need to develop novel chemo-selective SNO labeling reagents to facilitate specific labeling and for more effective enrichment and profiling of SNOs in complex samples. 125, 126 Similarly, the development of dimedone-based probes is another example of a method which enables specific detection of SOH-modified proteins even at the proteome level. 5093 As with the case for SNO, the overall sensitivity for detecting endogenous levels of SOH modifications is still quite low and a large amount of starting material (e.g., 30 mg) is necessary.…”

Section: Perspective and Outlookmentioning

confidence: 99%

Quantitative proteomic characterization of redox-dependent post-translational modifications on protein cysteines

2017

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Protein thiols play a crucial role in redox signaling, in the regulation of enzymatic activity and protein function, and in maintaining redox homeostasis in living systems. The unique chemical reactivity of the thiol group makes protein cysteines susceptible to reactions with reactive oxygen and nitrogen species that form various reversible and irreversible post-translational modifications (PTMs). The reversible PTMs in particular are major components of redox signaling and are involved in the regulation of various cellular processes under physiological and pathological conditions. The biological significance of these redox PTMs in both healthy and disease states has been increasingly recognized. Herein, we review recent advances in quantitative proteomic approaches for investigating redox PTMs in complex biological systems, including general considerations of sample processing, chemical or affinity enrichment strategies, and quantitative approaches. We also highlight a number of redox proteomic approaches that enable effective profiling of redox PTMs for specific biological applications. Although technical limitations remain, redox proteomics is paving the way to a better understanding of redox signaling and regulation in both healthy and disease states.

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Direct methods for detection of protein S-nitrosylation

Cited by 32 publications

References 39 publications

The role of S-nitrosoglutathione reductase (GSNOR) in human disease and therapy

The role of S-nitrosoglutathione reductase (GSNOR) in human disease and therapy

Protein S-nitrosylation: specificity and identification strategies in plants

Quantitative proteomic characterization of redox-dependent post-translational modifications on protein cysteines

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