Detection of S-nitrosothiols

Diers, Anne R.; Keszler, Ágnes; Hogg, Neil

doi:10.1016/j.bbagen.2013.07.026

Cited by 45 publications

(37 citation statements)

References 73 publications

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“…200 Several methods have been developed for detection of protein and low-molecular-weight nitrosothiols; however, these techniques are challenging and prone to artifacts. 201 These measurements can be affected by light, reducing agents, and pH because of an effect on nitrosothiol stability. Chung et al 202 offer a comprehensive review on the utility of Cys tandem mass tag (cysTMT) to detect and determine the reactivity of an individual Cys’s reactivity for S -nitrosylation.…”

Section: Oxidative Modification Of Proteinsmentioning

confidence: 99%

“…This approach has facilitated the identification and quantification of Cys oxidative modifications in cardiovascular cells and tissue. 202 Other major methods of nitrosothiol detection include chemiluminescence-based methods and switch-based methods, 201 and recently, nitrosothiol-specific antibodies have been developed. 203,204 …”

Section: Oxidative Modification Of Proteinsmentioning

confidence: 99%

See 1 more Smart Citation

Measurement of Reactive Oxygen Species, Reactive Nitrogen Species, and Redox-Dependent Signaling in the Cardiovascular System

Griendling¹,

Touyz²,

Zweíer³

et al. 2016

Circulation Research

332

247

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Reactive oxygen species and reactive nitrogen species are biological molecules that play important roles in cardiovascular physiology and contribute to disease initiation, progression, and severity. Because of their ephemeral nature and rapid reactivity, these species are difficult to measure directly with high accuracy and precision. In this statement, we review current methods for measuring these species and the secondary products they generate and suggest approaches for measuring redox status, oxidative stress, and the production of individual reactive oxygen and nitrogen species. We discuss the strengths and limitations of different methods and the relative specificity and suitability of these methods for measuring the concentrations of reactive oxygen and reactive nitrogen species in cells, tissues, and biological fluids. We provide specific guidelines, through expert opinion, for choosing reliable and reproducible assays for different experimental and clinical situations. These guidelines are intended to help investigators and clinical researchers avoid experimental error and ensure high-quality measurements of these important biological species.

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Section: Oxidative Modification Of Proteinsmentioning

confidence: 99%

Section: Oxidative Modification Of Proteinsmentioning

confidence: 99%

Measurement of Reactive Oxygen Species, Reactive Nitrogen Species, and Redox-Dependent Signaling in the Cardiovascular System

Griendling¹,

Touyz²,

Zweíer³

et al. 2016

Circulation Research

332

247

View full text Add to dashboard Cite

show abstract

“…Despite recent progress in characterizing protein nitrosylation and denitrosylation, the dynamic cellular nitrosoproteome remains relatively unexplored, particularly under physiologically relevant conditions. This may be in part because of methodological challenges inherent to the proteomic analysis of S-nitrosylation and denitrosylation (See Discussion and (15)(16)(17)). …”

mentioning

confidence: 99%

A Substrate Trapping Approach Identifies Proteins Regulated by Reversible S-nitrosylation

Ben-Lulu

Ziv

Admon

et al. 2014

Molecular & Cellular Proteomics

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Protein S-nitrosylation, the nitric oxide-mediated posttranslational modification of cysteine residues, has emerged as an important regulatory mechanism in diverse cellular processes. Yet, knowledge about the Snitrosoproteome in different cell types and cellular contexts is still limited and many questions remain regarding the precise roles of protein S-nitrosylation and denitrosylation. Here we present a novel strategy to identify reversibly nitrosylated proteins. Our approach is based on nitrosothiol capture and enrichment using a thioredoxin trap mutant, followed by protein identification by mass spectrometry. Employing this approach, we identified more than 400 putative nitroso-proteins in S-nitrosocysteinetreated human monocytes and about 200 nitrosylation substrates in endotoxin and cytokine-stimulated mouse macrophages. The large majority of these represent novel nitrosylation targets and they include many proteins with key functions in cellular homeostasis and signaling. Biochemical and functional experiments in vitro and in cells validated the proteomic results and further suggested a role for thioredoxin in the denitrosylation and activation of inducible nitric oxide synthase and the protein kinase MEK1. Our findings contribute to a better understanding of the macrophage S-nitrosoproteome and the role of thioredoxin-mediated denitrosylation in nitric oxide signaling. The approach described here may prove generally useful for the identification and exploration of nitrosoproteomes under various physiological and pathophysiological conditions. Molecular & Cellular

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“…A significant advancement was made with the development of the biotin switch assay that allows identification of protein S-nitrosothiols using a combination of thiol-blocking, RSNO-reducing strategies: immunoblotting with LC-MS-based protein identification (45). Several method-focused texts about the pros and cons of the biotin switch assay have been compiled and thus not discussed in this review (19,55). We would like to underscore, however, how this approach can be used, in combination with quantitative approaches outlined above, to determine the position of an RSNO on a protein, and the amount of this modification.…”

Section: No and H 2 S Measurementsmentioning

confidence: 99%

Working with nitric oxide and hydrogen sulfide in biological systems

Yuan

Patel

Kevil

2015

American Journal of Physiology-Lung Cellular and Molecular Phys

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(H 2S) are gasotransmitter molecules important in numerous physiological and pathological processes. Although these molecules were first known as environmental toxicants, it is now evident that that they are intricately involved in diverse cellular functions with impact on numerous physiological and pathogenic processes. NO and H 2S share some common characteristics but also have unique chemical properties that suggest potential complementary interactions between the two in affecting cellular biochemistry and metabolism. Central among these is the interactions between NO, H 2S, and thiols that constitute new ways to regulate protein function, signaling, and cellular responses. In this review, we discuss fundamental biochemical principals, molecular functions, measurement methods, and the pathophysiological relevance of NO and H 2S. thiol; oxidation; redox; pulmonary; cardiovascular HISTORICALLY CONSIDERED ONLY as industrial pollutants, nitric oxide (NO) and hydrogen sulfide (H 2 S) are now appreciated as two key physiologically produced signaling molecules that control multiple cellular functions. Appreciation that dysfunction in how these solvated gases affect these functions, through either deficient formation or downstream reactivity, has opened up new therapeutic avenues for a host of diseases in all major organ systems including the lung. Our understanding of NO homeostasis mechanisms are relatively advanced compared with H 2 S, primarily because of the latter's discovery as a biologically relevant entity being postdated by a decade or more compared with NO. Although they are chemically distinct, there are intriguing parallel mechanisms/concepts in NO and H 2 S biology that include overlapping functions, technical challenges in how each of these gases are measured in biological milieu, appreciation of the mechanisms and factors that modulate how metabolism of each of these is regulated, and therapeutic potential for either inhibiting or repleting NO or H 2 S. In this article, and within the framework outlined above, we provide a general overview of NO and H 2 S biology. Nitric Oxide Formation: Enzymatic and Nonenzymatic SourcesEnzymatic sources. Nitric oxide is synthesized by one of three different isoforms of nitric oxide synthase (NOS) that differ in enzymatic activity, in how they are regulated (transcriptional, translational, and posttranslational mechanisms), and in how they are expressed/compartmentalized in tissues as well as the subcellular level. These are called NOS I, II, and III, corresponding to the inducible (iNOS), neuronal (nNOS), and endothelial (eNOS) isoforms, typically with high, mid, and low activities, respectively. In the systemic and pulmonary vasculature, eNOS plays a key role in controlling blood flow and maintaining an antithrombotic and anti-inflammatory luminal surface. On the other hand, iNOS is induced by inflammatory stimuli in leukocytes, airway epithelial cells, and alveolar macrophages to mediate pathogen killing. However, production of NO at higher concentrations in ...

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Detection of S-nitrosothiols

Cited by 45 publications

References 73 publications

Measurement of Reactive Oxygen Species, Reactive Nitrogen Species, and Redox-Dependent Signaling in the Cardiovascular System

Measurement of Reactive Oxygen Species, Reactive Nitrogen Species, and Redox-Dependent Signaling in the Cardiovascular System

A Substrate Trapping Approach Identifies Proteins Regulated by Reversible S-nitrosylation

Working with nitric oxide and hydrogen sulfide in biological systems

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