Chromatographic and mass spectrometric methods for quantitative determination of 3-nitrotyrosine in biological samples and their application to human samples

Ryberg, Henrik; Caidahl, Kenneth

doi:10.1016/j.jchromb.2007.02.001

Cited by 77 publications

(77 citation statements)

References 110 publications

(153 reference statements)

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“…Because 3NT is a low-abundance PTM, issues with ion suppression and false-positive identification arise (Ryberg andCaidahl 2007 , Li et al 2011 ). A conservative set of guidelines has been proposed to increase confidence in the identification of 3NT-modified proteins as follows: accurate peptide charge state and mass, detection of the 3NT immonium ion fragment peak (m/z 181.1), validation of 3NT peptide chromatographic retention (in comparison to unmodified peptide), and limitation of unassigned fragment peaks (Li et al 2011 ) which can be adopted by any laboratory.…”

Section: Enrichmentmentioning

confidence: 99%

“…High-performance liquid chromatography is a popular separation technique to measure free 3NT because of its versatile coupling to a wide variety of detectors (Tsikas and Caidahl 2005 ) such as UV-visible (Vis) Halliwell 1994 , Sucu et al 2003 ) and fluorescence detectors (Sharov et al 2008, Dremina et al 2011. Electrochemical detection of proteinbound 3NT (Sugiura et al 2004 ) and free 3NT (Kaur et al 1998, Halejcia -Delophont et al 2001, Ryberg and Caidahl 2007, Nuriel et al 2008 ) is 100 × more sensitive than UV-Vis or fluorescence detection (Nuriel et al 2008 ). Detection limits of 3 attomole [limit of quantification (LOQ) 0.6 pm] of 3NT have been reported with MS (Tsikas 2012 ).…”

Section: Introductionmentioning

confidence: 99%

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Proteomics quantification of protein nitration

Robinson

2013

Reviews in Analytical Chemistry

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Protein tyrosine nitration is a post-translational modification (PTM) that can occur in biological systems under conditions of oxidative stress. This PTM can impact protein structure and function and has been linked to diseases such as Alzheimer ' s disease, cardiomyopathy, and arthritis. In order to understand the role that 3-nitrotyrosine (3NT) plays in disease states, a better understanding at the macromolecular level is necessary. Proteomics is a powerful approach that can simultaneously measure hundreds to thousands of proteins in normal or diseased states and thus can be helpful in the analysis of 3NT-modified proteins. Recently, some attention has been focused on the development of proteomic workflows that provide enrichment, characterization, and relative quantification of 3NT-modified proteins. These approaches rely on gel electrophoresis, liquid chromatography, and mass spectrometry (MS) techniques. This review provides an overview of current proteomics approaches for 3NT-modified proteins and highlights current MS-based methods for quantification of this PTM.

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Section: Enrichmentmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Proteomics quantification of protein nitration

Robinson

2013

Reviews in Analytical Chemistry

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“…Several methods have been developed to detect protein nitration. [12][13][14][15][16] Immunodetection with antibodies directed against nitrotyrosine is one of the most commonly used methods. 12) Many highperformance liquid chromatography (HPLC)-based methods with ultraviolet, 13) electrochemical, 14) and fluorescent detection 15) have also been reported.…”

Section: · ϫmentioning

confidence: 99%

“…However, these methods are based on the detection and/or quantification of free nitrotyrosine, either in plasma or generated after the cleavage of the peptide bond by enzymatic or acidic hydrolysis. 16) These methods yield quantitative data only regarding the changes in nitration levels in whole tissues or whole proteins, and do not identify the sites of NO 2 -Tyr in proteins.…”

Section: · ϫmentioning

confidence: 99%

Efficient Identification and Quantification of Peptides Containing Nitrotyrosine by Matrix-Assisted Laser Desorption/Ionization Time-of-Flight Mass Spectrometry after Derivatization

Tsumoto

Taguchi

Kohda

2010

CHEMICAL & PHARMACEUTICAL BULLETIN

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Protein nitration at tyrosine residues leading to 3-nitrotyrosine (NO 2 -Tyr) is one of the nonenzymatic post-translational modifications that can occur in cells under conditions of nitrosative stress.1) There are two main pathways of protein nitration. One is the generation of peroxynitrite (ONOO Ϫ ) by the reaction of nitric oxide ( · NO) with superoxide (O 2 · Ϫ ) and the subsequent reaction of ONOO Ϫ with CO 2 , which leads to the generation of nitrogen dioxide ( · NO 2 ) and the carbonate radical (CO 3 · Ϫ).2) The other is the generation of · NO 2 by the reaction of nitrite (NO 2 Ϫ ) with hydrogen peroxide (H 2 O 2 ) in the presence of heme proteins, such as myeloperoxidase.3) Tyrosine nitration can alter protein structure and function by forming NO 2 -Tyr, partly because of the shift in the pK a value of the tyrosine hydroxyl group from 10.1 to 7.2. 4) Tyrosine nitration may also prevent tyrosine phosphorylation, which is important in signal transduction. 5)Increased levels of protein nitration have been observed in various diseases, [6][7][8][9][10][11][12] such as cardiovascular disease , 9) Alzheimer's disease, 10,12) and Parkinson's disease. 11) Because protein nitration is associated with both physiological and pathological conditions, it is necessary to develop efficient methods to identify the nitration sites and quantify the nitration levels in proteins.NO 2 -Tyr is a sufficiently stable modification to be used as a biomarker of · NO/ONOO Ϫ -related damage. Several methods have been developed to detect protein nitration.12-16) Immunodetection with antibodies directed against nitrotyrosine is one of the most commonly used methods.12) Many highperformance liquid chromatography (HPLC)-based methods with ultraviolet, 13) electrochemical, 14) and fluorescent detection 15) have also been reported. However, these methods are based on the detection and/or quantification of free nitrotyrosine, either in plasma or generated after the cleavage of the peptide bond by enzymatic or acidic hydrolysis.16) These methods yield quantitative data only regarding the changes in nitration levels in whole tissues or whole proteins, and do not identify the sites of NO 2 -Tyr in proteins.Recently, mass spectrometry (MS)-based methods have been developed as an important technique for the identification of nitrated proteins and nitrated sites in proteins. Mass spectrometers with matrix-assisted laser desorption/ionization (MALDI) [17][18][19] or electrospray ionization (ESI) [20][21][22][23][24][25] have been widely used in these studies. The application of tandem mass spectrometry (MS/MS) makes it possible to identify nitrated sites in proteins. [20][21][22][23][24][25] In the MALDI analysis of nitrotyrosine-containing peptides, the characteristic mass pattern derived from nitrotyrosine has mass values lower than that of [MϩH] ϩ by 16 Da and 32 Da. These ions correspond to the loss of one and two oxygen atoms, respectively, from the nitro group (-NO 2 ), and are generated during the ionization process with laser irradiat...

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“…3-NT, a stable product of nitration of tyrosine residues, has been measured as a biomarker of protein damage induced by peroxynitrite and other RNS [23,24,25,26,27,28,29,30,31,32,33]. Human plasma proteins such as plasminogen, fibrinogen and superoxide dismutase, mitochondrial antoxidant enzymehave been demonstrated to be nitrated [23,25,26,27,28].…”

Section: Introductionmentioning

confidence: 99%

Oxidative and Nitrosative Stress Markers in Patients on Hemodialysis and Peritoneal Dialysis

Köse¹,

Seziş

Akçiçek

et al. 2011

Blood Purif

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Aim: The aim of this study was to evaluate the effects of hemodialysis (HD) and peritoneal dialysis (PD) treatments on oxidative and nitrosative stress markers comparatively. Methods: Twenty HD and 20 PD patients as well as 20 healthy individuals were included in this study. Plasma advanced oxidation protein products, myeloperoxidase, thiol group and 3-nitrotyrosine (3-NT) levels were measured in all subjects. Results: Plasma advanced oxidation protein products and myeloperoxidase levels were elevated by HD and PD treatments when compared to the control group. Conversely, plasma thiol group levels were decreased in HD and PD patients. 3-NT levels were increased by HD treatment only. Conclusions: The elevated plasma 3-NT levels in pre-HD and post-HD patients suggest that those patients have a considerably increased risk for nitrosative tissue injury. However, similar 3-NT levels of the control and PD groups support the advantage of PD therapy in terms of nitrosative tissue injury.

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Chromatographic and mass spectrometric methods for quantitative determination of 3-nitrotyrosine in biological samples and their application to human samples

Cited by 77 publications

References 110 publications

Proteomics quantification of protein nitration

Proteomics quantification of protein nitration

Efficient Identification and Quantification of Peptides Containing Nitrotyrosine by Matrix-Assisted Laser Desorption/Ionization Time-of-Flight Mass Spectrometry after Derivatization

Oxidative and Nitrosative Stress Markers in Patients on Hemodialysis and Peritoneal Dialysis

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