Quantitative and comparative liquid chromatography-electrospray ionization-mass spectrometry analyses of hydrogen sulfide and thiol metabolites derivaitized with 2-iodoacetanilide isotopologues

Lee, Der-Yen; Huang, Wei-Chieh; Gu, Ting‐Jia; Chang, Geen-Dong

doi:10.1016/j.chroma.2018.04.008

Cited by 28 publications

(19 citation statements)

References 32 publications

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“…In the same context, commercially available 2‐iodoacetanilide (IAN) and 13 C 6 ‐IAN were also used for the determination of hydrogen sulfide and thiol metabolites (cysteine, homocysteine, and GSH) in a cellular extract. The derivatization reaction was accomplished at 65°C, yielding stable derivatives (Lee, Huang, Gu, & Chang, ).…”

Section: Isotope‐coded Derivatization Reagents For Lc–ms Analysismentioning

confidence: 99%

Current trends in isotope‐coded derivatization liquid chromatographic‐mass spectrometric analyses with special emphasis on their biomedical application

El-Maghrabey

Kishikawa

Kuroda

2020

Biomedical Chromatography

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Currently, LC–MS has various applications in different areas such as metabolomics, pharmacokinetics, and pathological studies. Yet, matrix effects resulting from co‐existing constituents remain a major problem for LC–MS [or LC–tandem mass spectrometry (LC–MS/MS)]. Moreover, technical problems and instrumental drifts may lead to ion abundance variance. Thus, an internal standard (IS) is required to guarantee the accuracy and precision of the method. Because of their limited number, isotope‐coded derivatization (ICD) has been recently introduced to overcome this problem. For ICD, a stable heavy isotope‐coded moiety is used for labeling the standard or the control sample and the formed products can act as ISs. A light form of the reagent is used for labeling the sample. Then, both are mixed and analyzed by LC–MS(/MS). This strategy permits the identification of different unknown analytes including potential metabolites and disease biomarkers. All these attributes lead to persistent growth in the applications of ICD LC–MS(/MS) in various biomedical branches. In this article we review the ICD methods published in the last eight years for biomedical applications as well as briefly summarize other applications for environmental and food analyses as some of their used ICD reagents were further applied for analyzing biological specimens or have the potential for that.

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Section: Isotope‐coded Derivatization Reagents For Lc–ms Analysismentioning

confidence: 99%

Current trends in isotope‐coded derivatization liquid chromatographic‐mass spectrometric analyses with special emphasis on their biomedical application

El-Maghrabey

Kishikawa

Kuroda

2020

Biomedical Chromatography

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“…Chromatographic methods used in H 2 S analysis include: GC coupled to different detectors as electrochemical [132] , electron capture [133] , flame photometry [134] , mass spectrometry [135] , [136] , ion mobility spectrometry [137] . LC coupled to different detectors as spectrophotometry [138] , spectrofluorimetry [139] , atomic fluorescence spectrometry [140] , mass spectrometry [141] , and electrochemical [142] . …”

Section: Introductionmentioning

confidence: 99%

“…LC coupled to different detectors as spectrophotometry [138] , spectrofluorimetry [139] , atomic fluorescence spectrometry [140] , mass spectrometry [141] , and electrochemical [142] .…”

Section: Introductionmentioning

confidence: 99%

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Emerging analytical tools for the detection of the third gasotransmitter H2S, a comprehensive review

Ibrahim

Serag

Farag

2021

Journal of Advanced Research

100

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“…the formation of mixed disulfide bonds between small thiol‐containing compounds and protein cysteinyl thiol groups. Within the field of oxidative stress, mass spectrometry has been used to detect protein thiol oxidations such as to sulfenic acid, 20–23 sulfinic acid, 24 sulfonic acid, 25–27 S‐thiolation by coenzyme A, 28 hydrogen sulfide, 29 cysteine perthiosulfenic acid, 30 S‐nitrosylation, 31–34 cysteine 35,36 and glutathionylation, 37–40 and to a lesser extent protein S‐thiolation by HcySH 41,42 …”

Section: Introductionmentioning

confidence: 99%

Investigating protein thiol chemistry associated with dehydroascorbate, homocysteine and glutathione using mass spectrometry

Ahuie

Gagnon

Pace

et al. 2020

Rapid Comm Mass Spectrometry

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Rationale:Oxidative stress is an imbalance between reactive free radical oxygen species and antioxidant defenses. Its consequences can lead to numerous pathologies. Regulating oxidative stress is the complex interplay between antioxidant recycling and thiol-containing regulatory proteins. Understanding these regulatory mechanisms is important for preventing onset of oxidative stress. The aim of this study was to investigate S-thiol protein chemistry associated with oxidized vitamin C (dehydroascorbate, DHA), homocysteine (HcySH) and glutathione (GSH) using mass spectrometry. Methods:Glutaredoxin-1 (Grx-1) was incubated with DHA, with and without GSH and HcySH. Disulfide formation was followed by electrospray ionization mass spectrometry (ESI-MS) of intact proteins and by LC/ESI-MS/MS of peptides from protein tryptic digestions. The mechanism of DHA-mediated S-thiolation was investigated using two synthetic peptides: AcFHACAAK and AcFHACE. Three proteins, i.e. human hemoglobin (HHb), recombinant peroxiredoxin 2 (Prdx2) andGrx-1, were S-homocysteinylated followed by S-transthiolyation with GSH and investigated by ESI-MS and ESI-MS/MS. Results: ESI-MS analysis reveals that DHA mediates disulfide formation andS-thiolation by HcySH as well as GSH of Grx-1. LC/ESI-MS/MS analysis allows identification of Grx-1 S-thiolated cysteine adducts. The mechanism by which DHA mediates S-thiolation of heptapeptide AcFHACAAK is shown to be via initial formation of a thiohemiketal adduct. In addition, ESI-MS of intact proteins shows that GSH can S-transthiolate S-homocysteinylated Grx-1, HHb and Prdx2.The GS-S-protein adducts over time dominate the ESI-MS spectrum profile. Conclusions:Mass spectrometry is a unique analytical technique for probing complex reaction mechanisms associated with oxidative stress. Using model proteins, ESI-MS reveals the mechanism of DHA-facilitated S-thiolation, which consists of thiohemiketal formation, disulfide formation or S-thiolation. Furthermore, protein S-thiolation by HcySH can be reversed by reversible GSH thiol exchange. The use of mass spectrometry with in vitro models of protein S-thiolation in oxidative stress may provide significant insight into possible mechanisms of action occurring in vivo.

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Quantitative and comparative liquid chromatography-electrospray ionization-mass spectrometry analyses of hydrogen sulfide and thiol metabolites derivaitized with 2-iodoacetanilide isotopologues

Cited by 28 publications

References 32 publications

Current trends in isotope‐coded derivatization liquid chromatographic‐mass spectrometric analyses with special emphasis on their biomedical application

Current trends in isotope‐coded derivatization liquid chromatographic‐mass spectrometric analyses with special emphasis on their biomedical application

Emerging analytical tools for the detection of the third gasotransmitter H2S, a comprehensive review

Investigating protein thiol chemistry associated with dehydroascorbate, homocysteine and glutathione using mass spectrometry

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