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Alzheimer’s disease, Parkinson’s disease and its animals models, cystic fibrosis, asthma, lung diseases, myocardial malfunction, stroke, amyotrophic lateral sclerosis (ALS), chronic hepatitis, cirrhosis, diabetes, etc. [68,69]. Formation of 3-nitrotyrosine in proteins is considered to be a post-translational modification with important pathophysiological consequences and is one of the early markers of nitrosative stress that have been revealed in multiple sclerosis. Elevated contents of nitrates, nitrites, and free nitrotyrosine were found in the cerebrospinal fluid of subjects and have been proposed as functional biomarkers of neurodegeneration [70]. Approximately 1 to 10 residues of tyrosine per 100,000 (10–100 μmol 3-NT/mol of tyrosine) are found to be nitrated in plasma proteins under inflammatory conditions such as in cardiovascular disease [71], although up to 10 times more 3-NT can be detected in tissues [19]. Studies have found a strong correlation between 3-NT plasma levels and coronary artery disease (CAD), identifying the elevated levels of 3-NT as an emerging cardiovascular risk factor [72] (Table 2). Among the many technologies available, the most efficient and dependable approach for the quantification of 3-NT are gas chromatography-mass spectrometry (GC–MS/MS) and liquid chromatography-mass spectrometry (LC–MS/MS) (Table 3). GC–MS/ MS and LC–MS/MS based methods reveal that the concentration of 3-NT in human plasma is on the threshold of the pico mole (pM) to nano mole (nM) range and changes only very little upon disease or intervention. These important findings are suitable to serve as the gold standard and as a measure to test the reliability of alternative techniques, such as GC–MS, high performance liquid chromatography (HPLC) with electrochemical detection, or immunological assays. The various antibody assays also need to be validated by these GC–MS/ MS or LC–MS/MS methods [73]. Protein Nitrating agent Technique or Method* References Bovine serum albumin (BSA) Tetranitromethane MALDI, MS Creatine Kinase (CK) Peroxynitrite MS Cytochrome c (cyt c) Peroxynitrite MALDI-TOF Cytochromes P450s (CYP2B6, CYP2E1) Peroxynitrite Hemoglobin (Hb), human Nitrite/hydrogen peroxide MS Human Serum albumin (HSA) Peroxynitrite, Tetranitromethane HPLC, MS, MALDI-TOF Low density lipoprotein (LDL) apoB100 Peroxynitrite Phosphorylase b Peroxynitrite MS MS Tsikas (2012), Radi et al (2001), Abello et al (2009), Duncan (2003). *MALDI, Matrix-Assisted Laser Desorption Ionization; MS, Mass Spectroscopy; HPLC, High Performance Liquid Chromatography, MALDI-TOF, Matrix-assisted laser desorption/ionisation-time of flight mass spectroscopy. Table 3: Measurement of tyrosine nitrated proteins by different methods. In tissue-based proteomics of diseases, more than 100 nitrated proteins have been identified using mass spectrometric methods or Western blot analysis following fractionation of samples with 2- dimensional (2D) Polyacrylamide gel electrophoresis (PAGE) or immunoprecipitation from tissues, such as brains afflicted with neurodegenerative diseases or atherosclerotic blood vessels. Protein nitration occurs in various diseases with biological selectivity and site specificity [3]. There are many reports on nitrated proteins in various diseases, identified by current proteomic methods such as 2D-PAGE or LC-MS/MS [3,12]. The biological functions and the subcellular locations of identified nitrated proteins are classified into multiple categories. Of the identified nitrated proteins in in vivo disease models, 25%, 20%, 28% are derived from mitochondria, extracellular, and cytoplasm or intracellular, respectively. Since, various active redox reactions occur in mitochondria, it is expected to be the center of nitration. The major nitrated proteins identified are shown to be involved in energy metabolism (20%), which includes many redox reactions. Among the nitrated proteins, the active roles of tau, α-syn and LDL have extensively been studied in pathogenesis of Alzheimer’s disease, Parkinson’s disease and atherosclerosis, respectively [74]. Therefore, the presence of 3-NT in biological samples indicates that reactive NO-derived species are produced in vivo, leading to various pathophysiological conditions [67,75,76]. Nitric oxide is known to participate as a cytotoxic effector molecule or a pathogenic mediator when overexpressed by either inflammatory stimuli-induced nitric oxide synthase (iNOS) or over stimulation of the constitutive forms of NOS (eNOS). The autologous proteins may become immunogenic if they are structurally modified post-translationally under physiological and pathological conditions. These chemical modifications reactions include transglutamination, deamidation, glycosylation, oxidation, nitration and proteolytic cleavage. The consequence of these protein modifications may be generation or unmasking of new antigenic epitopes, which will stimulate relevant B cells and/or T cells, thus leading to the breakdown or bypass of tolerance. The protein tyrosine nitration is widely recognized as a hallmark of inflammation that is associated with the up-regulation of iNOS and is not affected by exogenous sources of nitrate/nitrite (NO 3 /NO 2 ) or serum thiols [77-80]. MS Varieties of post-translationally modified nitrated proteins have been shown to accumulate in apoptotic or inflamed tissues [81]. Hence, the accumulation of nitrotyrosine-containing proteins in tissues that appear as foreign to the immune system might induce an autoimmune response and sustain a chronic inflammatory reaction [82]. Elevated levels of anti-nitrotyrosine antibodies have been measured in the synovial fluid of patients with RA and OA [76], serum of patients with systemic lupus erythematosus (SLE) [83] and after acute lung injury [84]. It has been suggested that alteration in amino acid structure or sequence may generate neoepitopes on self-proteins, leading to an immune attack. Furthermore, autologous proteins may also become immunogenic if they are structurally modified. The modifications may generate or mask antigenic epitopes and stimulate relevant B cells and/or T cells, leading to breakdown or bypass of tolerance [77]. Approaches directed at inhibiting the oxidative modification of proteins caused by RNS may be useful in understanding the pathology of inflammatory, neurodegenerative and autoimmune diseases [85]. Acknowledgment The author wishes to thank co-researchers and co-authors, Dr. Fahim Khan and Dr. Rizwan Ahmad, who have been associated with studies on various aspects of free radical biochemistry. References 1. Ischiropoulos H (1998) Biological tyrosine nitration: a pathophysiological function of nitric oxide and reactive oxygen species. Arch Biochem Biophys 356: 1-11. OMICS Group eBooks 006
2. Souza JM, Daikhin E, Yudkoff M, Raman CS, Ischiropoulos H (1999) Factors determining the selectivity of protein tyrosine nitration. Arch Biochem Biophys 371: 169-78. 3. Ischiropoulos H (2003) Biological selectivity and functional aspects of protein tyrosine nitration. Biochem Biophys Res Commun 305: 776-83. 4. Kyte J, Doolittle RF (1982) A simple method for displaying the hydropathic character of a protein. J Mol Biol 157: 105-32. 5. Abello N, Kerstjens HA, Postma DS, Bischoff R (2009) Protein tyrosine nitration: selectivity, physicochemical and biological consequences, denitration, and proteomics methods for the identification of tyrosine-nitrated proteins. J Proteome Res 8: 3222- 3238. 6. Clementi C, Carloni P, Maritan A (1999) Protein design is a key factor for subunit-subunit association. Proc Natl Acad Sci U.S.A 96: 9616-9621. 7. Jiao K, Mandapati S, Skipper PL, Tannenbaum SR, Wishnok JS (2001) Site-selective nitration of tyrosine in human serum albumin by peroxynitrite. Anal Biochem 293: 43-52. 8. Greis KD, Zhu S, Matalon S (1996) Identification of nitration sites on surfactant protein A by tandem electrospray mass spectrometry. Arch Biochem Biophys 335: 396-402. 9. Batthyany C, Souza JM, Duran R, Cassina A, Cervenansky C, Radi R (2005) Time course and site(s) of cytochrome c tyrosine nitration by peroxynitrite. Biochemistry 44: 8038-8046. 10. Lennon CW, Cox HD, Hennelly SP, Chelmo SJ, McGuirl MA (2007) Probing structural differences in prion protein isoforms by tyrosine nitration. Biochemistry 46: 4850-4860. 11. Yamaguchi Y, Nasu F, Harada A, Kunitomo M (2007) Oxidants in the gas phase of cigarette smoke pass through the lung alveolar wall and raise systemic oxidative stress. J Pharmacol Sci 103: 275-82. 12. Yeo WS, Lee SJ, Lee JR, Kim KP (2008) Nitrosative protein tyrosine modifications: biochemistry and functional significance. BMB Rep 41: 194-203. 13. Beckman JS, Beckman TW, Chen J, Marshall PA, Freeman BA (1990) Apparent hydroxyl radical production by peroxynitrite: implications for endothelial injury from nitric oxide and superoxide. Proc Natl Acad Sci USA 87: 1620-1624. 14. Sokolovsky M, Riordan JF, Vallee BL (1966) Tetranitromethane. A reagent for the nitration of tyrosyl residues in proteins. Biochemistry 5: 3582-3589. 15. Ischiropoulos H, Zhu L, Chen J, Tsai M, Martin JC, et al. (1992) Peroxynitrite-mediated tyrosine nitration catalyzed by superoxide dismutase. Arch Biochem Biophys 298: 431-437. 16. Zhan X, Desiderio DM (2006) Nitroproteins from a human pituitary adenoma tissue discovered with a nitrotyrosine affinity column and tandem mass spectrometry. Anal Biochem 354: 279-289. 17. Quint P, Reutzel R, Mikulski R, McKenna R, Silverman DN (2006) Crystal structure of nitrated human manganese superoxide dismutase: mechanism of inactivation. Free Radic Biol Med 40: 453-8. 18. Yamakura F, Taka H, Fujimura T, Murayama K (1998) Inactivation of human manganese-superoxide dismutase by peroxynitrite is caused by exclusive nitration of tyrosine 34 to 3-nitrotyrosine. J Biol Chem 273: 14085-14089. 19. Brennan ML, Wu W, Fu X, Shen Z, Song W, et al. (2002) A tale of two controversies: defining both the role of peroxidases in nitrotyrosine formation in vivo using eosinophil peroxidase and myeloperoxidase-deficient mice, and the nature of peroxidasegenerated reactive nitrogen species. J Biol Chem 277: 17415-17427. 20. Klebanoff SJ (1993) Reactive nitrogen intermediates and antimicrobial activity: role of nitrite. Free Radic Biol Med 14: 351-360. 21. Shao B, Bergt C, Fu X, Green P, Voss JC (2005) Tyrosine 192 in apolipoprotein A-I is the major site of nitration and chlorination by myeloperoxidase, but only chlorination markedly impairs ABCA1-dependent cholesterol transport. J Biol Chem 280: 5983-5993. 22. Thomas DD, Espey MG, Vitek MP, Miranda KM, Wink DA (2002) Protein nitration is mediated by heme and free metals through Fenton-type chemistry: an alternative to the NO/O2- reaction. Proc Natl Acad Sci U.S.A 99: 1269-76. 23. Bian K, Gao Z, Weisbrodt N, Murad F (2003) The nature of heme/iron-induced protein tyrosine nitration. Proc Natl Acad Sci U.S.A 100: 5712-5217. 24. Roncone R, Barbieri M, Monzani E, Casella L (2006) Reactive nitrogen species generated by heme proteins: Mechanism of formation and targets. Coord Chem Rev 250: 1286-1293. 25. Halliwell B (1997) What nitrates tyrosine? Is nitrotyrosine specific as a biomarker of peroxynitrite formation in vivo. FEBS Lett 411: 157-60. 26. Radi R (2004) Nitric oxide, oxidants, and protein tyrosine nitration. Proc Natl Acad Sci U.S.A 101(12): 4003-4008. 27. Peluffo G, Radi R (2007) Biochemistry of protein tyrosine nitration in cardiovascular pathology. Cardiovasc Res 75: 291-302. 28. Schopfer FJ, Baker PR, Freeman BA (2003) NO-dependent protein nitration: a cell signaling event or an oxidative inflammatory response? Trends Biochem Sci 28: 646-54. 29. Grzelak A, Balcerczyk A, Mateja A, Bartosz G (2001) Hemoglobin can nitrate itself and other proteins. Biochim Biophys Acta 1528: 97-100. 30. Kilinc K, Kilinc A, Wolf RE, Grisham MB (2001) Myoglobin-mediated tyrosine nitration: no need for peroxynitrite. Biochem Biophys Res Commun 285: 273-276. 31. Lu N, Zhang Y, Gao Z (2009) Nitrite-glucose-glucose oxidase system directly induces rat heart homogenate oxidation and tyrosine nitration: effects of some flavonoids. Toxicol In vitro 23: 627-33. 32. Ceriello A, Mercuri F, Quagliaro L, Assaloni R, Motz E, et al. (2001) Detection of nitrotyrosine in diabtetic plasma: evidence of oxidative stress. Diabetologia 44: 834. 33. Wang N, Lia D, Lu NH, Yi L, Huang XW, et al. (2010) Peroxynitrite and hemoglobin-mediated nitrative/oxidative modification of human plasma protein: effects of some flavonoids. J Asian Nat Prod Res 12: 257-264. OMICS Group eBooks 007
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Proteins and Peptides- Reemergence
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Coming years will witness increasin
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Advances in Protein Chemistry Chapt
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purification methodology and laid t
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