Hanyang Med Rev.  2013 May;33(2):110-117. 10.7599/hmr.2013.33.2.110.

Mass Spectrometry Analysis for Nitration of Proteins

Affiliations
  • 1Department of Molecular Biotechnology, Konkuk University, Seoul, Korea. kpkim@konkuk.ac.kr

Abstract

Various proteomics and immunological methods including mass spectrometry combined with both liquid and 2-D PAGE, and immunodetection have been employed to identify and characterize nitrated proteins from pathological samples. Nitrosative modifications regulate cellular signal transduction and pathogenesis of inflammatory responses and neurodegenerative diseases. Nitric oxide generates reactive nitrosative species, such as peroxynitrite (ONOO-) that may be involved in a number of diseases. ONOO- can mediate protein tyrosine nitration which causes structural changes of affected proteins and leads to their inactivation. Protein tyrosine nitration is a biomarker of oxidative stress and also influences protein structure and function. Recent advances in mass spectrometry have made it possible to identify modified proteins and specific modified amino acid residues. This review focuses on the significance of protein tyrosine nitration and the progress achieved in analytical methods. Although mass spectrometry of nitrated peptides has become a powerful tool for the analysis of nitrated peptides, the low stoichiometry of protein tyrosine nitration clearly demands the use of affinity chromatography to enrich modified proteins (or peptides).

Keyword

Proteomics; Mass Spectrometry; Nitric Oxide; Nitration; Chromatography, Affinity

MeSH Terms

Chromatography, Affinity
Mass Spectrometry
Neurodegenerative Diseases
Nitric Oxide
Oxidative Stress
Peptides
Peroxynitrous Acid
Proteins
Proteomics
Signal Transduction
Tyrosine
Nitric Oxide
Peptides
Peroxynitrous Acid
Proteins
Tyrosine

Figure

  • Fig. 1 This paper describes the analysis of PTN. Typical methods for the analysis are divided into antibody based approach and mass-spectrometry based approach. MALDI, Matrix-assisted laser desorption/ionization; LC-MS/MS, Liquid chromatography-tandem mass spectrometry.


Cited by  1 articles

Do Reactive Oxygen Species Cause Aging?
Seong Eon Ryu
Hanyang Med Rev. 2013;33(2):75-76.    doi: 10.7599/hmr.2013.33.2.75.


Reference

1. Reynolds MR, Berry RW, Binder LI. Site-specific nitration and oxidative dityrosine bridging of the tau protein by peroxynitrite: implications for Alzheimer's disease. Biochemistry. 2005; 44:1690–1700.
Article
2. Yeo WS, Lee SJ, Lee JR, Kim KP. Nitrosative protein tyrosine modifications: biochemistry and functional significance. BMB Rep. 2008; 41:194–203.
Article
3. Muntane J, la Mata MD. Nitric oxide and cancer. World J Hepatol. 2010; 2:337–344.
Article
4. MacMillan-Crow LA, Cruthirds DL, Ahki KM, Sanders PW, Thompson JA. Mitochondrial tyrosine nitration precedes chronic allograft nephropathy. Free Radic Biol Med. 2001; 31:1603–1608.
Article
5. Mann M, Hendrickson RC, Pandey A. Analysis of proteins and proteomes by mass spectrometry. Annu Rev Biochem. 2001; 70:437–473.
Article
6. Karas M, Hillenkamp F. Laser desorption ionization of proteins with molecular masses exceeding 10,000 daltons. Anal Chem. 1988; 60:2299–2301.
Article
7. Abello N, Kerstjens HA, Postma DS, Bischoff R. Protein tyrosine nitration: selectivity, physicochemical and biological consequences, denitration, and proteomics methods for the identification of tyrosine-nitrated proteins. J Proteome Res. 2009; 8:3222–3238.
Article
8. Turko IV, Murad F. Mapping sites of tyrosine nitration by matrix-assisted laser desorption/ionization mass spectrometry. Methods Enzymol. 2005; 396:266–275.
Article
9. Tedeschi G, Cappelletti G, Negri A, Pagliato L, Maggioni MG, Maci R, et al. Characterization of nitroproteome in neuron-like PC12 cells differentiated with nerve growth factor: identification of two nitration sites in alpha-tubulin. Proteomics. 2005; 5:2422–2432.
Article
10. Sarver A, Scheffler NK, Shetlar MD, Gibson BW. Analysis of peptides and proteins containing nitrotyrosine by matrix-assisted laser desorption/ionization mass spectrometry. J Am Soc Mass Spectrom. 2001; 12:439–448.
Article
11. Sheeley SA, Rubakhin SS, Sweedler JV. The detection of nitrated tyrosine in neuropeptides: a MALDI matrix-dependent response. Anal Bioanal Chem. 2005; 382:22–27.
Article
12. Petersson AS, Steen H, Kalume DE, Caidahl K, Roepstorff P. Investigation of tyrosine nitration in proteins by mass spectrometry. J Mass Spectrom. 2001; 36:616–625.
Article
13. Salavej P, Spalteholz H, Arnhold J. Modification of amino acid residues in human serum albumin by myeloperoxidase. Free Radic Biol Med. 2006; 40:516–525.
Article
14. Shin YS, Moon JH, Kim MS. Selective screening of tyrosine-nitrated peptides in tryptic mixtures by in-source photodissociation at 355 nm in matrix-assisted laser desorption ionization. Anal Chem. 2011; 83:1704–1708.
Article
15. Butt YK, Lo SC. Detecting nitrated proteins by proteomic technologies. Methods Enzymol. 2008; 440:17–31.
Article
16. Radi R. Nitric oxide, oxidants, and protein tyrosine nitration. Proc Natl Acad Sci U S A. 2004; 101:4003–4008.
Article
17. Yoon SW, Kang S, Ryu SE, Poo H. Identification of tyrosine-nitrated proteins in HT22 hippocampal cells during glutamate-induced oxidative stress. Cell Prolif. 2010; 43:584–593.
Article
18. Cappelletti G, Maggioni MG, Tedeschi G, Maci R. Protein tyrosine nitration is triggered by nerve growth factor during neuronal differentiation of PC12 cells. Exp Cell Res. 2003; 288:9–20.
Article
19. Reed TT, Pierce WM Jr, Turner DM, Markesbery WR, Butterfield DA. Proteomic identification of nitrated brain proteins in early Alzheimer's disease inferior parietal lobule. J Cell Mol Med. 2009; 13:2019–2029.
Article
20. Castegna A, Thongboonkerd V, Klein JB, Lynn B, Markesbery WR, Butterfield DA. Proteomic identification of nitrated proteins in Alzheimer's disease brain. J Neurochem. 2003; 85:1394–1401.
Article
21. Kanski J, Alterman MA, Schoneich C. Proteomic identification of age-dependent protein nitration in rat skeletal muscle. Free Radic Biol Med. 2003; 35:1229–1239.
Article
22. Salzano AM, D'Ambrosio C, Scaloni A. Mass spectrometric characterization of proteins modified by nitric oxide-derived species. Methods Enzymol. 2008; 440:3–15.
Article
23. Fiore G, Di Cristo C, Monti G, Amoresano A, Columbano L, Pucci P, et al. Tubulin nitration in human gliomas. Neurosci Lett. 2006; 394:57–62.
Article
24. Sultana R, Poon HF, Cai J, Pierce WM, Merchant M, Klein JB, et al. Identification of nitrated proteins in Alzheimer's disease brain using a redox proteomics approach. Neurobiol Dis. 2006; 22:76–87.
Article
25. Zhan X, Desiderio DM. Nitroproteins Identified in Human Ex-smoker Bronchoalveolar Lavage Fluid. Aging Dis. 2011; 2:100–115.
26. Zhan X, Desiderio DM. MALDI-induced Fragmentation of Leucine enkephalin, Nitro-Tyr Leucine Enkaphalin, and d(5)-Phe-Nitro-Tyr Leucine Enkephalin. Int J Mass Spectrom. 2009; 287:77–86.
Article
27. Söderling AS, Hultman L, Delbro D, Højrup P, Caidahl K. Reduction of the nitro group during sample preparation may cause underestimation of the nitration level in 3-nitrotyrosine immunoblotting. J Chromatogr B Analyt Technol Biomed Life Sci. 2007; 851:277–286.
Article
28. Koeck T, Fu X, Hazen SL, Crabb JW, Stuehr DJ, Aulak KS. Rapid and selective oxygen-regulated protein tyrosine denitration and nitration in mitochondria. J Biol Chem. 2004; 279:27257–27262.
Article
29. Borges CR, Kuhn DM, Watson JT. Mass mapping sites of nitration in tyrosine hydroxylase: random vs selective nitration of three tyrosine residues. Chem Res Toxicol. 2003; 16:536–540.
Article
30. Ducrocq C, Dendane M, Laprevote O, Serani L, Das BC, Bouchemal-Chibani N, et al. Chemical modifications of the vasoconstrictor peptide angiotensin II by nitrogen oxides (NO, HNO2, HOONO)--evaluation by mass spectrometry. Eur J Biochem. 1998; 253:146–153.
Article
31. Cook SL, Jackson GP. Characterization of tyrosine nitration and cysteine nitrosylation modifications by metastable atom-activation dissociation mass spectrometry. J Am Soc Mass Spectrom. 2011; 22:221–232.
Article
32. Zubarev RA, Horn DM, Fridriksson EK, Kelleher NL, Kruger NA, Lewis MA, et al. Electron capture dissociation for structural characterization of multiply charged protein cations. Anal Chem. 2000; 72:563–573.
Article
33. Kelleher NL, Zubarev RA, Bush K, Furie B, Furie BC, McLafferty FW, et al. Localization of labile posttranslational modifications by electron capture dissociation: the case of gamma-carboxyglutamic acid. Anal Chem. 1999; 71:4250–4253.
Article
34. Jones AW, Mikhailov VA, Iniesta J, Cooper HJ. Electron capture dissociation mass spectrometry of tyrosine nitrated peptides. J Am Soc Mass Spectrom. 2010; 21:268–277.
Article
35. Turko IV, Li L, Aulak KS, Stuehr DJ, Chang JY, Murad F. Protein tyrosine nitration in the mitochondria from diabetic mouse heart. Implications to dysfunctional mitochondria in diabetes. J Biol Chem. 2003; 278:33972–33977.
Article
36. Zhan X, Desiderio DM. Nitroproteins from a human pituitary adenoma tissue discovered with a nitrotyrosine affinity column and tandem mass spectrometry. Anal Biochem. 2006; 354:279–289.
Article
37. Nikov G, Bhat V, Wishnok JS, Tannenbaum SR. Analysis of nitrated proteins by nitrotyrosine-specific affinity probes and mass spectrometry. Anal Biochem. 2003; 320:214–222.
Article
38. Abello N, Barroso B, Kerstjens HA, Postma DS, Bischoff R. Chemical labeling and enrichment of nitrotyrosine-containing peptides. Talanta. 2010; 80:1503–1512.
Article
39. Zhang Q, Qian WJ, Knyushko TV, Clauss TR, Purvine SO, Moore RJ, et al. A method for selective enrichment and analysis of nitrotyrosine-containing peptides in complex proteome samples. J Proteome Res. 2007; 6:2257–2268.
Article
40. Prokai-Tatrai K, Guo J, Prokai L. Selective chemoprecipitation and subsequent release of tagged species for the analysis of nitropeptides by liquid chromatography-tandem mass spectrometry. Mol Cell Proteomics. 2011; 10:M110.002923.
Article
41. Lee JR, Lee SJ, Kim TW, Kim JK, Park HS, Kim DE, et al. Chemical approach for specific enrichment and mass analysis of nitrated peptides. Anal Chem. 2009; 81:6620–6626.
Article
42. Kim JK, Lee JR, Kang JW, Lee SJ, Shin GC, Yeo WS, et al. Selective enrichment and mass spectrometric identification of nitrated peptides using fluorinated carbon tags. Anal Chem. 2011; 83:157–163.
Article
43. Crowley JR, Yarasheski K, Leeuwenburgh C, Turk J, Heinecke JW. Isotope dilution mass spectrometric quantification of 3-nitrotyrosine in proteins and tissues is facilitated by reduction to 3-aminotyrosine. Anal Biochem. 1998; 259:127–135.
Article
44. Ghesquiere B, Colaert N, Helsens K, Dejager L, Vanhaute C, Verleysen K, et al. In vitro and in vivo protein-bound tyrosine nitration characterized by diagonal chromatography. Mol Cell Proteomics. 2009; 8:2642–2652.
Article
45. Larsen TR, Bache N, Gramsbergen JB, Roepstorff P. Identification of nitrotyrosine containing peptides using combined fractional diagonal chromatography (COFRADIC) and off-line nano-LC-MALDI. J Am Soc Mass Spectrom. 2011; 22:989–996.
Article
46. Sharov VS, Dremina ES, Galeva NA, Gerstenecker GS, Li X, Dobrowsky RT, et al. Fluorogenic Tagging of Peptide and Protein 3-Nitrotyrosine with 4-(Aminomethyl)-benzenesulfonic Acid for Quantitative Analysis of Protein Tyrosine Nitration. Chromatographia. 2010; 71:37–53.
Article
47. Wisastra R, Poelstra K, Bischoff R, Maarsingh H, Haisma HJ, Dekker FJ. Antibody-free detection of protein tyrosine nitration in tissue sections. Chembiochem. 2011; 12:2016–2020.
Article
48. Robinson RA, Evans AR. Enhanced sample multiplexing for nitrotyrosine-modified proteins using combined precursor isotopic labeling and isobaric tagging. Anal Chem. 2012; 84:4677–4686.
Article
49. Zhang Y, Yang H, Poschl U. Analysis of nitrated proteins and tryptic peptides by HPLC-chip-MS/MS: site-specific quantification, nitration degree, and reactivity of tyrosine residues. Anal Bioanal Chem. 2011; 399:459–471.
Article
50. Tsumoto H, Taguchi R, Kohda K. Efficient identification and quantification of peptides containing nitrotyrosine by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry after derivatization. Chem Pharm Bull (Tokyo). 2010; 58:488–494.
Article
Full Text Links
  • HMR
Actions
Cited
CITED
export Copy
Close
Share
  • Twitter
  • Facebook
Similar articles
Copyright © 2024 by Korean Association of Medical Journal Editors. All rights reserved.     E-mail: koreamed@kamje.or.kr