Oxidation of proteins: Basic principles and perspectives for blood proteomics

Proteomics - Clinical Applications

Volumn 2, Issue 2, 2008, Pages 142-157

  Barelli, Stefano ^a   Canellini, Giorgia ^a   Thadikkaran, Lynne ^a   Crettaz, David ^a   Quadroni, Manfredo ^b   Rossier, Joël S ^c   Tissot, Jean Daniel ^a   Lion, Niels ^a,d  

^a Service Regional Vaudois de Transfusion Sanguine   (Switzerland)

^b UNIVERSITY OF LAUSANNE   (Switzerland)

^c DiagnoSwiss SA   (Switzerland)

^d EPFL   (Switzerland)

Author keywords

Blood; Oxidation; Oxidative stress; Plasma; Red blood cell

Indexed keywords

3 NITROTYROSINE; AMINO ACID DERIVATIVE; ANTIOXIDANT; CARBONYL DERIVATIVE; FIBRINOGEN; IMMUNOGLOBULIN; REACTIVE NITROGEN SPECIES; REACTIVE OXYGEN METABOLITE; SULFIDE; SUPEROXIDE DISMUTASE; THIOL DERIVATIVE;

ANALYTIC METHOD; BIOINFORMATICS; BLOOD CELL; BLOOD COMPONENT; CHEMICAL ANALYSIS; DEFENSE MECHANISM; ERYTHROCYTE; HUMAN; MASS SPECTROMETRY; OXIDATION REDUCTION REACTION; OXIDATIVE STRESS; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN CROSS LINKING; PROTEIN DEGRADATION; PROTEIN MODIFICATION; PROTEOMICS; REGULATORY MECHANISM; REVIEW; THROMBOCYTE;

EID: 39649083798     PISSN: 18628346     EISSN: None     Source Type: Journal    
DOI: 10.1002/prca.200780009     Document Type: Review

References (197)

1. Grune, T., Reinheckel, T., Davies, K. J. A., Degradation of oxidized proteins in mammalian cells. FASEB J. 1997, 11, 526-534.
2. Grune, T., Merker, K., Sandig, G., Davies, K. J. A., Selective degradation of oxidatively modified protein substrates by the proteasome. Biochem. Biophys. Res. Commun. 2003, 305, 709-718.
3. Claiborne, A., Miller, H., Parsonage, D., Ross, R. P., Protein-sulfenic acid stabilization and function in enzyme catalysis and gene regulation. FASEB J. 1993, 7, 1483-1490.
4. Finkel, T., Redox-dependent signal transduction. FEBS Letters 2000, 476, 52-54.
5. Herrlich, P., Boehmer, F. D., Redox regulation of signal transduction in mammalian cells. Biochem. Pharmacol. 2000, 59, 35-41.
6. Allen, R. G., Tresini, M., Oxidative stress and gene regulation. Free Radic. Biol. Med. 2000, 28, 463-499.
7. Rahman, I., MacNee, W., Regulation of redox glutathione levels and gene transcription in lung inflammation: Therapeutic approaches. Free Radic. Biol. Med. 2000, 28, 1405-1420.
8. Sun, Y., Oberley, L. W., Redox regulation of transcriptional activators. Free Radic. Biol. Med. 1996, 21, 335-348.
9. Morel, Y., Barouki, R., Repression of gene expression by oxidative stress. Biochem. J. 1999, 342, 481-496.
10. Forrester, M. T., Stamler, J. S., A classification scheme for redox-based modifications of proteins. Am. J. Respir. Cell Mol. Biol. 2007, 36, 135-137.
11. Shacter, E., Quantification and significance of protein oxidation in biological samples. Drug Metabol. Rev. 2000, 32, 307-326.
12. Berlett, B. S., Stadtman, E. R., Protein oxidation in aging, disease, and oxidative stress. J. Biol. Chem. 1997, 272, 20313-20316.
13. Levine, R. L., Stadtman, E. R., Oxidative modification of proteins during aging. Exp. Gerontol. 2001, 36, 1495-1502.
14. Sohal, R. S., Role of oxidative stress and protein oxidation in the aging process. Free Radic. Biol. Med. 2002, 33, 37-44.
15. Macario, A. J. L., de Macario, E. C., Sick chaperones, cellular stress, and disease. N. Engl. J. Med. 2005, 353, 1489-1501.
16. Butterfield, D. A., Proteomics: A new approach to investigate oxidative stress in Alzheimer's disease brain. Brain Res. 2004, 1000, 1-7.
17. Butterfield, D. A., Amyloid beta-peptide [1-42]-assosiated free radical-induced oxidative stress and neurodegeneration in Alzheimer's disease brain: Mechanisms and consequences. Curr. Med. Chem. 2003, 10, 2651-2659.
18. Choi, J., Malakowsky, C. A., Talent, J. M., Conrad, C. C., Gracy, R. W., Identification of oxidized plasma proteins in Alzheimer's disease. Biochem. Biophys. Res. Commun. 2002, 293, 1566-1570.
19. Butterfield, D. A., Amyloid beta-peptide (1-42)-induced oxidative stress and neurotoxicity: Implications for neurodegeneration in Alzheimer's disease brain. A review. Free Radic. Res. 2002, 36, 1307-1313.
20. Allan Butterfield, D., Castegna, A., Lauderback, C. M., Drake, J., Evidence that amyloid beta-peptide-induced lipid peroxidation and its sequelae in Alzheimer's disease brain contribute to neuronal death. Neurobiol. Aging 2002, 23, 655-664.
21. Butterfield, D. A., Drake, J., Pocernich, C., Castegna, A., Evidence of oxidative damage in Alzheimer's disease brain: Central role for amyloid beta-peptide. Trends Mol. Med. 2001, 7, 548-554.
22. Varadarajan, S., Yatin, S., Aksenova, M., Butterfield, D. A., Review: Alzheimer's amyloid beta-peptide-associated free radical oxidative stress and neurotoxicity. J. Struct. Biol. 2000, 130, 184-208.
23. Cerutti, P. A., Oxyradicals and cancer. Lancet 1994, 344, 862-863.
24. Cerutti, P. A., Oxidant stress and carcinogenesis. Eur. J. Clin. Invest. 1991, 21, 1-5.
25. Cerutti, P. A., Prooxidant states and tumor promotion. Science 1985, 227, 375-381.
26. Kinnula, V. L., Crapo, J. D., Superoxide dismutases in malignant cells and human tumors. Free Radic. Biol. Med. 2004, 36, 718-744.
27. Baynes, J. W., Role of oxidative stress in development of complications in diabetes. Diabetes 1991, 40, 405-412.
28. Wolff, S. P., Jiang, Z. Y., Hunt, J. V., Protein glycation and oxidative stress in diabetes mellitus and ageing. Free Radic. Biol. Med. 1991, 10, 339-352.
29. Dalle-Donne, I., Giustarini, D., Colombo, R., Rossi, R., Milzani, A., Protein carbonylation in human diseases. Trends Mol. Med. 2003, 9, 169-176.
30. Jurgens, G., Hoff, H. F., Chisolm Iii, G. M., Esterbauer, H., Modification of human serum low density lipoprotein by oxidation - Characterization and pathophysiological implications. Chem. Phys. Lipids 1987, 45, 315-336.
31. Berliner, J. A., Navab, M., Fogelman, A. M., Frank, J. S., et al., Atherosclerosis: Basic mechanisms: Oxidation, inflammation, and genetics. Circulation 1995, 91, 2488-2496.
32. Berliner, J. A., Heinecke, J. W., The role of oxidized lipoproteins in atherogenesis. Free Radic. Biol. Med. 1996, 20, 707-727.
33. Mertens, A. N. N., Holvoet, P., Oxidized LDL and HDL: Antagonists in atherothrombosis. FASEB J. 2001, 15, 2073-2084.
34. Dumaswala, U. J., Zhuo, L., Jacobsen, D. W., Jain, S. K., Sukalski, K. A., Protein and lipid oxidation of banked human erythrocytes: Role of glutathione. Free Radic. Biol. Med. 1999, 27, 1041-1049.
35. Dumaswala, U. J., Wilson, M. J., Wu, Y. L., Wykle, J., et al., Glutathione loading prevents free radical injury in red blood cells after storage. Free Radic. Res. 2000, 33, 517-529.
36. Kriebardis, A. G., Antonelou, M. H., Stamoulis, K. E., Economou-Petersen, E., et al., Membrane protein carbonylation in non-leukodepleted CPDA-preserved red blood cells. Blood Cells Mol. Dis. 2006, 36, 279-282.
37. Tinmouth, A., Fergusson, D., Yee, I. C., Hebert, P. C., Clinical consequences of red cell storage in the critically ill. Transfusion 2006, 46, 201 4-2027,
38. Kriebardis, A. G., Antonelou, M. H., Stamoulis, K. E., Economou-Petersen, E., et al., Progressive oxidation of cytoskeletal proteins and accumulation of denatured hemoglobin in stored red cells. J. Cell. Mol. Med. 2007, 11, 148-155.
39. Stadtman, E. R., Berlett, B. S., Reactive oxygen-mediated protein oxidation in aging and disease. Chem. Res. Toxicol. 1997, 10, 485-494.
40. Stadtman, E. R., Oxidation of free amino acids and amino acid residues in proteins by radiolysis and by metal-catalyzed reactions. Ann. Rev. Biochem. 1993, 62, 797-821.
41. Imlay, J. A., Pathways of Oxidative Damage. Ann. Rev. Microbiol. 2003, 57, 395-418.
42. Hawkins, C. L., Davies, M. J., Generation and propagation of radical reactions on proteins. Biochim. Biophys. Acta 2001, 1504, 196-219.
43. Xu, G., Chance, M. R., Hydroxyl radical-mediated modification of proteins as probes for structural proteomics. Chem. Rev. 2007, 107, 3514-3543.
44. Dalle-Donne, I., Scaloni, A., Butterfield, D. A., Redox Proteomics: From Protein Modifications to Cellular Dysfunction and Diseases, Wiley & Sons, New York 2006.
45. Beckman, J. S., Koppenol, W. H., Nitric oxide, superoxide, and peroxynitrite: The good, the bad, and the ugly. Am. J. Physiol. 1996, 271, 40-45.
46. Stadtman, E. R., Oliver, C. N., Metal-catalyzed oxidation of proteins: Physiological consequences. J. Biol. Chem. 1991, 266, 2005-2008.
47. Stadtman, E. R., Protein oxidation and aging. Free Radic. Res. 2006, 40, 1250-1258.
48. Davies, M. J., The oxidative environment and protein damage. Biochim. Biophys. Acta 2005, 1703, 93-109.
49. Headlam, H. A., Davies, M. J., Markers of protein oxidation: Different oxidants give rise to variable yields of bound and released carbonyl products. Free Radic. Biol. Med. 2004, 36, 1175-1184.
50. Nystrom, T., Role of oxidative carbonylation in protein quality control and senescence. EMBO J. 2005, 24, 1311-1317.
51. Esterbauer, H., Schaur, R. J., Zollner, H., Chemistry and Biochemistry of 4-hydroxynonenal, malonaldehyde and related aidehydes. Free Radic. Biol. Med. 1991, 11, 81-128.
52. Yoritaka, A., Hattori, N., Uchida, K., Tanaka, M., et al., Immunohistochemical detection of 4-hydroxynonenal protein adducts in Parkinson disease. Proc. Natl. Acad. Sci. USA 1996, 93, 2696-2701.
53. Burcham, P. C., Kuhan, Y. T., Introduction of carbonyl groups into proteins by the lipid peroxidation product, malondialdehyde. Biochem. Biophys. Res. Commun. 1996, 220, 996-1001.
54. Uchida, K., Stadtman, E. R., Covalent attachment of 4-hydroxynonenal to glyceraldehyde-3-phosphate dehydrogenase. A possible involvement of intra- and inter-molecular cross- linking reaction. J. Biol. Chem. 1993, 268, 6388-6393.
55. Dalle-Donne, I., Rossi, R., Colombo, R., Giustarini, D., Milzani, A., Biomarkers of oxidative damage in human disease. Clin. Chem. 2006, 52, 601-623.
56. Dalle-Donne, I., Scaloni, A., Giustarini, D., Cavarra, E., et al., Proteins as biomarkers of oxidative/nitrosative stress in diseases: The contribution of redox proteomics. Mass Spectrom. Rev. 2005, 24, 55-99.
57. Rhee, S. G., Bae, Y. S., Lee, S. R., Kwon, J., Hydrogen peroxide: a key messenger that modulates protein phosphorylation through cysteine oxidation. Science STKE 2000, 2000, pe1.
58. Hogg, N., The biochemistry and physiology of S-nitrosothiols. Ann. Rev. Pharmacol. Toxicol. 2002, 42, 585-600.
59. Dalle-Donne, I., Rossi, R., Giustarini, D., Colombo, R., Milzani, A., S-glutathionylation in protein redox regulation. Free Radic. Biol. Med. 2007, 43, 883-898.
60. Bergenhem, N., Carlsson, U., Strid, L., The existence of glutathione and cysteine disulfide-linked to erythrocyte carbonic anhydrase from tiger shark. Biochim. Biophys. Acta 1986, 871, 55-60.
61. Dormann, P., Borchers, T., Korf, U., Hojrup, P., et al., Amino acid exchange and covalent modification by cysteine and glutathione explain isoforms of fatty acid-binding protein occurring in bovine liver. J. Biol. Chem. 1993, 268, 16286-16292.
62. Fratelli, M., Gianazza, E., Ghezzi, P., Redox proteomics: identification and functional role of glutathionylated proteins. Expert Rev. Proteomics 2004, 1, 365-376.
63. Vogt, W., Oxidation of methionyl residues in proteins: Tools, targets, and reversal. Free Radic. Biol. Med. 1995, 18, 93-105.
64. Levine, R. L., Mosoni, L., Berlett, B. S., Stadtman, E. R., Methionine residues as endogenous antioxidants in proteins. Proc. Natl. Acad. Sci. USA 1996, 93, 15036-15040.
65. Levine, R. L., Berlett, B. S., Moskovitz, J., Mosoni, L., Stadtman, E. R., Methionine residues may protect proteins from critical oxidative damage. Mech. Ageing Dev. 1999, 107, 323-332.
66. Stadtman, E. R., Moskovitz, J., Levine, R. L., Oxidation of Methionine Residues of Proteins: Biological Consequences. Antioxid Redox Signal. 2003, 5, 577-582.
67. Stadtman, E. R., Van Remmen, H., Richardson, A., Wehr, N. B., Levine, R. L., Methionine oxidation and aging. Biochim. Biophys. Acta 2005, 1703, 135-140.
68. Beckman, J. S., Beckman, T. W., Chen, J., Marshall, P. A., Freeman, B. A., Apparent hydroxyl radical production by peroxynitrite: Implications for endothelial injury from nitric oxide and superoxide. Proc. Natl. Acad. Sci. USA 1990, 87, 1620-1624.
69. Eiserich, J. P., Patel, R. P., O'Donnell, V. B., Pathophysiology of nitric oxide and related species: Free radical reactions and modification of biomolecules. Mol. Aspects Med. 1998, 19, 221-357.
70. Murphy, M. P., Packer, M. A., Scarlett, J. L., Martin, S. W., Peroxynitrite: A biologically significant oxidant. Gen. Pharmacol. 1998, 31, 179-186.
71. Patel, R. P., McAndrew, J., Sellak, H., White, C. R., et al., Biological aspects of reactive nitrogen species. Biochim. Biophys. Acta - Bioenergetics 1999, 1411, 385-400.
72. Alvarez, B., Radi, R., Peroxynitrite reactivity with amino acids and proteins. Amino Acids 2003, 25, 295-311.
73. Radi, R., Nitric oxide, oxidants, and protein tyrosine nitration. Proc. Natl. Acad. Sci. USA 2004, 101, 4003-4008.
74. Pacher, P., Beckman, J. S., Liaudet, L., Nitric oxide and peroxynitrite in health and disease. Physiolog. Rev. 2007, 87, 315-424.
75. Szabo, C., Ischiropoulos, H., Radi, R., Peroxynitrite: Biochemistry, pathophysiology and development of therapeutics. Nat. Rev. Drug Discov. 2007, 6, 662-680.
76. Lymar, S. V., Hurst, J. K., Radical nature of peroxynitrite reactivity. Chem. Res. Toxicol. 1998, 11, 714-715.
77. Goldstein, S., Czapski, G., Lind, J., Merenyi, G., Tyrosine nitration by simultaneous generation of NO° and O2/°-under physiological conditions. How the radicals do the job. J. Biol. Chem. 2000, 275, 3031-3036.
78. Quijano, C., Romero, N., Radi, R., Tyrosine nitration by superoxide and nitric oxide fluxes in biological systems: Modeling the impact of superoxide dismutase and nitric oxide diffusion. Free Radical Biology and Medicine 2005, 39, 728-741.
79. Shishehbor, M. H., Aviles, R. J., Brennan, M. L., Fu, X., et al., Association of Nitrotyrosine Levels with Cardiovascular Disease and Modulation by Statin Therapy. JAMA 2003, 289, 1675-1680.
80. DiMarco, T., Giulivi, C., Current analytical methods for the detection of dityrosine, a biomarker of oxidative stress, in biological samples. Mass Spectrom. Rev. 2007, 26, 108-120.
81. Fu, X., Mueller, D. M., Heinecke, J. W., Generation of intramolecular and intermolecular sulfenamides, sulfinamides, and sulfonamides by hypochlorous acid: A potential pathway for oxidative cross-linking of low-density lipoprotein by myeloperoxidase. Biochemistry 2002, 41, 1293-1301.
82. Levine, R. L., Williams, J. A., Stadtman, E. R., Shacter, E., Carbonyl assays for determination of oxidatively modified proteins. Methods Enzymol. 1994, 233, 346-357.
83. Reznick, A. Z., Packer, L., Oxidative damage to proteins: Spectrophotometric method for carbonyl assay. Methods Enzymol. 1994, 233, 357-363.
84. Fagan, J. M., Sleczka, B. G., Sohar, I., Quantitation of oxidative damage to tissue proteins. Int. J. Biochem. Cell Biol. 1999, 31, 751-757.
85. Buss, H., Chan, T. P., Sluis, K. B., Domigan, N. M., Winterbourn, C. C., Protein carbonyl measurement by a sensitive ELISA method. Free Radic. Biol. Med. 1997, 23, 361-366.
86. Robinson, C. E., Keshavarzian, A., Pasco, D. S., Frommel, T. O., et al., Determination of protein carbonyl groups by immunoblotting. Anal. Biochem. 1999, 266, 48-57.
87. Alamdari, D. H., Kostidou, E., Paletas, K., Sarigianni, M., et al., High sensitivity enzyme-linked immunosorbent assay (ELISA) method for measuring protein carbonyl in samples with low amounts of protein. Free Radic. Biol, Med. 2005, 39, 1362-1367.
88. Nakamura, A., Goto, S., Analysis of protein carbonyls with 2,4-dinitrophenyl hydrazine and its antibodies by immunoblot in two-dimensional gel electrophoresis. J. Biochem. 1996, 119, 768-774.
89. Yan, L. J., Orr, W. C., Sohal, R. S., Identification of oxidized proteins based on sodium dodecyl sulfate- polyacrylamide gel electrophoresis, immunochemical detection, isoelectric focusing, and microsequencing. Anal. Biochem. 1998, 263, 67-71.
90. Yoo, Y. S., Regnier, F. E., Proteomic analysis of carbonylated proteins in two-dimensional gel electrophoresis using avidin-fluorescein affinity staining. Electrophoresis 2004, 25, 1334-1341.
91. England, K., Cotter, T., Identification of carbonylated proteins by MALDI-TOF mass spectroscopy reveals susceptibility of ER. Biochem. Biophys. Res. Commun. 2004, 320, 123-130.
92. Kristensen, B. K., Askerlund, P., Bykova, N. V., Egsgaard, H., Miller, I. M., Identification of oxidised proteins in the matrix of rice leaf mitochondria by immunoprecipitation and two-dimensional liquid chromatography-tandem mass spectrometry. Phytochemistry 2004, 65, 1839-1851.
93. Soreghan, B. A., Yang, F., Thomas, S. N., Hsu, J., Yang, A. J., High-throughput proteomic-based identification of oxidatively induced protein carbonylation in mouse brain. Pharm. Res. 2003, 20, 1713-1720.
94. Mirzaei, H., Regnier, F., Affinity chromatographic selection of carbonylated proteins followed by identification of oxidation sites using tandem mass spectrometry. Anal. Chem. 2005, 77, 2386-2392.
95. Mirzaei, H., Regnier, F., Creation of allotypic active sites during oxidative stress. J. Proteome Res. 2006, 5, 2159-2168.
96. Temple, A., Yen, T. Y., Gronert, S., Identification of specific protein carbonylation sites in model oxidations of human serum albumin. J. Am. Soc. Mass Spectrom. 2006, 17, 1172-1180.
97. Mirzaei, H., Regnier, F., Identification of yeast oxidized proteins - Chromatographic top-down approach for identification of carbonylated, fragmented and cross-linked proteins in yeast. J. Chromatogr. A 2007, 1141, 22-31.
98. Meany, D. L., Xie, H. W., Thompson, L. V., Arriaga, E. A., Griffin, T. J., Identification of carbonylated proteins from enriched rat skeletal muscle mitochondria using affinity chromatography-stable isotope labeling and tandem mass spectrometry. Proteomics 2007, 7, 1150-1163.
99. Roe, M. R., Xie, H. W., Bandhakavi, S., Griffin, T. J., Proteomic mapping of 4-hydroxynonenal protein modification sites by solid-phase hydrazide chemistry and mass spectrometry. Anal. Chem. 2007, 79, 3747-3756.
100. Mirzaei, H., Regnier, F., Enrichment of carbonylated peptides using Girard P reagent and strong cation exchange chromatography. Anal. Chem. 2006, 78, 770-778.
101. Mirzaei, H., Regnier, F., Identification and quantification of protein carbonylation using light and heavy isotope labeled Girard's P reagent. J. Chromatogr. A 2006, 1134, 122-133.
102. Lee, S., Young, N. L., Whetstone, P. A., Cheal, S. M., et al., Method to site-specificafly identify and quantitate carbonyl end products of protein oxidation using oxidation-dependent element coded affinity tags (O-ECAT) and nanoliquid chromatography Fourier transform mass spectrometry. J. Proteome Res. 2006, 5, 539-547.
103. Eaton, P., Protein thiol oxidation in health and disease: Techniques for measuring disulfides and related modifications in complex protein mixtures. Free Radic. Biol. Med. 2006, 40, 1889-1899.
104. Baty, J. W., Hampton, M. B., Winterbourn, C. C., Proteomic detection of hydrogen peroxide-sensitive thiol proteins in Jurkat cells. Biochem. J. 2005, 389, 785-795.
105. Baty, J. W., Hampton, M. B., Winterbourn, C. C., Detection of oxidant sensitive thiol proteins by fluorescence labeling and two-dimensional electrophoresis. Proteomics 2002, 2, 1261-1266.
106. Laragione, T., Redox regulation of surface protein thiols: Identification of integrin alpha-4 as a molecular target by using redox proteomics. Proc. Natl. Acad. Sci. USA 2003, 100, 14737-14741.
107. Laragione, T., Redox regulation of surface protein thiols: Identification of integrin alpha-4 as a molecular target by using redox proteomics (vol 100, pg 14737, 2003). Proc. Natl. Acad, Sci. USA 2004, 101, 4718-4718.
108. Lind, C., Gerdes, R., Hamnell, Y., Schuppe-Koistinen, I., et al., Identification of S-glutathionylated cellular proteins during oxidative stress and constitutive metabolism by affinity purification and proteomic analysis. Arch. Biochem. Biophys. 2002, 406, 229-240.
109. Hamnell-Pamment, Y., Lind, C., Palmberg, C., Bergman, T., Cotgreave, I. A., Determination of site-specificity of S-glutathionylated cellular proteins. Biochem. Biophys. Res. Commun. 2005, 332, 362-369.
110. Saurin, A. T., Neubert, H., Brennan, J. P., Eaton, P., Wide-spread sulfenic acid formation in tissues in response to hydrogen peroxide. Proc, Natl. Acad. Sci. USA 2004, 101, 17982-17987.
111. Kim, J. R., Yoon, H. W., Kwon, K. S., Lee, S. R., Rhee, S. G., Identification of proteins containing cysteine residues that are sensitive to oxidation by hydrogen peroxide at neutral pH. Anal. Biochem. 2000, 283, 214-221.
112. Suh, S. K., Hood, B. L., Kim, B. J., Conrads, T. P., et al., Identification of oxidized mitochondria proteins in alcohol-exposed human hepatoma cells and mouse liver. Proteomics 2004, 4, 3401-3412.
113. Sethuraman, M., McComb, M. E., Huang, H., Huang, S. Q., et al., Isotope-coded affinity tag (ICAT) approach to redox proteomics: Identification and quantitation of oxidant-sensitive cysteine thiols in complex protein mixtures. J. Proteome Res. 2004, 3, 1228-1233.
114. Sethuraman, M., McComb, M. E., Heibeck, T., Costello, C. E., Cohen, R. A., Isotope-coded affinity tag approach to identify and quantify oxidant-sensitive protein thiols. Mol. Cell. Proteomics 2004, 3, 273-278.
115. Brennan, J. P., Miller, J. I. A., Fuller, W., Wait, R., et al., The utility of N,N-biotinyl glutathione disulfide in the study of protein S-glutathiolation. Mol. Cell. Proteomics 2006, 5, 215-226.
116. Niture, S. K., Velu, C. S., Bailey, N. I., Srivenugopal, K. S., S-Thiolation mimicry: Quantitative and kinetic analysis of redox status of protein cysteines by glutathione-affinity chromatography. Arch. Biochem. Biophys. 2005, 444, 174-184.
117. Jaffrey, S. R., Erdjument-Bromage, H., Ferris, C. D., Tempst, P., Snyder, S. H., Protein S-nitrosylation: A physiological signal for neuronal nitric oxide. Nat. Cell Biol. 2001, 3, 193-197.
118. Aulak, K. S., Koeck, T., Crabb, J. W., Stuehr, D. J., Proteomic method for identification of tyrosine-nitrated proteins. Methods Mol. Biol. 2004, 279, 151-165.
119. ter Steege, J. C. A., Koster-Kamphuis, L., van Straaten, E. A., Forget, P. P., Buurman, W. A., Nitrotyrosine in plasma of celiac disease patients as detected by a new sandwich ELISA. Free Radic. Biol. Med. 1998, 25, 953-963.
120. Zhan, X. Q., Desiderio, D. M., The human pituitary nitroproteome: detection of nitrotyrosyl-proteins with two-dimensional Western blotting, and amino acid sequence determination with mass spectrometry. Biochem. Biophys. Res. Commun. 2004, 325, 1180-1186.
121. Kanski, J., Alterman, M. A., Schoneich, C., Proteomic identification of age-dependent protein nitration in rat skeletal muscle. Free Radic. Biol. Med. 2003, 35, 1229-1239.
122. Zhan, X., Desiderio, D. M., Linear ion-trap mass spectrometric characterization of human pituitary nitrotyrosine-containing proteins. Int. J. Mass Spectrom. 2007, 259, 96-104.
123. Nikov, G., Bhat, V., Wishnok, J. S., Tannenbaum, S. R., Analysis of nitrated proteins by nitrotyrosine-specific affinity probes and mass spectrometry. Anal. Biochem. 2003, 320, 214-222.
124. Zhang, Q., Qian, W. J., Knyushko, T. V., Clauss, T. R. W., et al., A method for selective enrichment and analysis of nitrotyrosine-containing peptides in complex proteome samples. J. Proteome Res. 2007, 6, 2257-2268.
125. Reinders, J., Sickmann, A., Modificomics: Posttranslational modifications beyond protein phosphorylation and glycosylation. Biomol. Eng. 2007, 24, 169-177.
126. Schoneich, C., Sharov, V. S., Mass spectrometry of protein modifications by reactive oxygen and nitrogen species. Free Radic. Biol. Med. 2006, 41, 1507-1520.
127. Gieseg, S. P., Simpson, J. A., Charlton, T. S., Duncan, M. W., Dean, R.T., Protein-bound 3,4-dihydroxyphenylalanine is a major reductant formed during hydroxyl radical damage to proteins. Biochemistry 1993, 32, 4780-4786.
128. Bakhtiar, R., Guan, Z., Electron capture dissociation mass spectrometry in characterization of post-translational modifications. Biochem. Biophys. Res. Commun. 2005, 334, 1-8.
129. Guan, Z., Yates, N. A., Bakhtiar R., Detection and characterization of methionine oxidation in peptides by collision-induced dissociation and electron capture dissociation. J. Am. Soc. Mass Spectrom. 2003, 14, 605-613.
130. Zhao, C., Sethuraman, M., Clavreul, N., Kaur, P., et al., Detailed map of oxidative post-translational modifications of human P21Ras using Fourier transform mass spectrometry. Anal. Chem. 2006, 78, 5134-5142.
131. Jiang, M., Jia, L., Jiang, W., Hu, X., et al., Protein disregulation in red blood cell membranes of type 2 diabetic patients. Biochem. Biophys. Res. Commun. 2003, 309, 196-200.
132. Kakhniashvili, D. G., Bulla Jr, L. A., Goodman, S. R., The human erythrocyte proteome: Analysis by ion trap mass spectrometry. Mol. Cell. Proteomics 2004, 3, 501-509.
133. Anniss, A. M., Glenister, K. M., Killian, J. J., Sparrow, R. L., Proteomic analysis of supernatants of stored real blood cell products. Transfusion 2005, 45, 1426-1433.
134. Bruschi, M., Seppi, C., Arena, S., Musante, L., et al., Proteomic analysis of erythrocyte membranes by soft immobiline gels combined with differential protein extraction. J. Proteome Res. 2005, 4, 1304-1309.
135. Kakhniashvili, D. G., Griko, N. B., Bulla Jr, L. A., Goodman, S. R., The proteomics of sickle cell disease: Profiling of erythrocyte membrane proteins by 2D-DIGE and tandem mass spectrometry. Exp. Biol. Med. 2006, 230, 787-792.
136. Tyan, Y. C., Jong, S. B., Liao, J. D., Liao, P. C., et al., Proteomic profiling of erythrocyte proteins by proteolytic digestion chip and identification using two-dimensional electro-spray ionization tandem mass spectrometry. J. Proteome Res. 2005, 4, 748-757.
137. Caterino, M., Ruoppolo, M., Orru, S., Savoia, M., et al., Characterization of red cell membrane proteins as a function of red cell density:. Annexin VII in different forms of hereditary spherocytosis. FEBS Letters 2006, 580, 6527-6532.
138. Pasini, E. M., Kirkegaard, M., Mortensen, P., Lutz, H. U., et al., In-depth analysis of the membrane and cytosolic proteome of red blood cells. Blood 2006, 108, 791-801.
139. Queloz, P. A., Thadikkaran, L., Crettaz, D., Rossier, J. S., et al., Proteomics and transfusion medicine: Future perspectives. Proteomics 2006, 6, 5606-5614.
140. D'Amici, G. M., Rinalducci, S., Zolla, L., Proteomic analysis of RBC membrane protein degradation during blood storage. J. Proteome Res. 2007, 6, 3242-3255.
141. Zhang, Y., Zhang, Y., Adachi, J., Olsen, J. V., et al., MAPU: Max-planck unified database of organellar, cellular, tissue and body fluid proteomes. Nucl. Acids Res. 2007, 35.
142. Sadrzadeh, S. M. H., Graf, E., Panter, S. S., Hemoglobin. A biologic Fenton reagent. J. Biol. Chem. 1984, 259, 14354-14356.
143. Richards, R. S., Roberts, T. K., McGregor, N. R., Dunstan, R. H., Butt, H. L., The role of erythrocytes in the inactivation of free radicals. Med. Hypotheses 1998, 50, 363-367.
144. Kiefer, C. R., Snyder, L. M., Oxidation and erythrocyte senescence. Curr. Opin. Hematol. 2000, 7, 113-116.
145. Romero, N., Radi, R., Hemoglobin and red blood cells as tools for studying peroxynitrite biochemistry. Methods Enzymol. 2005, 396, 229-245.
146. Denicola, A., Souza, J. M., Radi, R., Diffusion of peroxynitrite across erythrocyte membranes. Proc. Natl. Acad. Sci. USA 1998, 95, 3566-3571.
147. Romero, N., Denicola, A., Radi, R., Red blood cells in the metabolism of nitric oxide-derived peroxynitrite. IUBMB Life 2006, 58, 572-580.
148. Yang, K. S., Kang, S. W., Woo, H. A., Hwang, S. C., et al., Inactivation of human peroxiredoxin I during catalysis as the result of the oxidation of the catalytic site cysteine to cysteine-sulfinic acid. J. Biol. Chem. 2002, 277, 38029-38036.
149. Neumann, C. A., Krause, D. S., Carman, C. V., Das, S., et al., Essential role for the peroxiredoxin Prdx1 in erythrocyte antioxidant defence and tumour suppression. Nature 2003, 424, 561-565.
150. Lee, T. H., Kim, S. U., Yu, S. L., Kim, S. H., et al., Peroxiredoxin II is essential for sustaining life span of erythrocytes in mice. Blood 2003, 101, 5033-5038.
151. Goth, L., Eaton, J. W., Hereditary catalase deficiencies and increased risk of diabetes. Lancet 2000, 356, 1820-1821.
152. Gaetani, G. F., Ferraris, A. M., Rolfo, M., Mangerini, R., et al., Predominant role of catalase in the disposal of hydrogen peroxide within human erythrocytes. Blood 1996, 87, 1595-1599.
153. Peskin, A. V., Low, F. M., Paton, L. N., Maghzal, G. J., et al., The high reactivity of peroxiredoxin 2 with H2O2 is not reflected in its reaction with other oxidants and thiol reagents. J. Biol. Chem. 2007, 282, 11885-11892.
154. Wood, Z. A., Poole, L. B., Karplus, P. A., Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling. Science 2003, 300, 650-653.
155. Kang, S. W., Rhee, S. G., Chang, T. S., Jeong, W., Choi, M. H., 2-Cys peroxiredoxin function in intracellular signal transduction: Therapeutic implications. Trends Mol. Med. 2005, 11, 571-578.
156. Low, F. M., Hampton, M. B., Peskin, A. V., Winterbourn, C. C., Peroxiredoxin 2 functions as a noncatalytic scavenger of low-level hydrogen peroxide in the erythrocyte. Blood 2007, 109, 2611-2617.
157. Rettig, M. P., Low Philip S, P. S., Gimm, J. A., Mohandas, N., et al., Evaluation of biochemical changes during in vivo erythrocyte senescence in the dog. Blood 1999, 93, 376-384.
158. Davies, K. J., Goldberg, A. L., Oxygen radicals stimulate intracellular proteolysis and lipid peroxidation by independent mechanisms in erythrocytes. J. Biol. Chem. 1987, 262, 8220-8226.
159. Arese, P., Turrini, F., Schwarzer, E., Band 3/complement-mediated recognition and removal of normally senescent and pathological human erythrocytes. Cell. Physiol. Biochem. 2005, 16, 133-146.
160. Bratosin, D., Estaquier, J., Petit, F, Arnoult, D., et al., Programmed cell death in mature erythrocytes: A model for investigating death effector pathways operating in the absence of mitochondria. Cell Death Differ. 2001, 8, 1143-1156.
161. Berg, C. P., Engels, I. H., Rothbart, A., Lauber, K., et al., Human mature red blood cells express caspase-3 and caspase-8, but are devoid of mitochondrial regulators of apoptosis. Cell Death Differ. 2001, 8, 1197-1206.
162. Matarrese, P., Straface, E., Pietraforte, D., Gambardella, L., et al., Peroxynitrite induces senescence and apoptosis of red blood cells through the activation of aspartyl and cysteinyl proteases. FASEB J. 2005, 19, 416-418.
163. Pietraforte, D., Matarrese, P., Straface, E., Gambardella, L., et al., Two different pathways are involved in peroxynitrite-induced senescence and apoptosis of human erythrocytes. Free Radic. Biol. Med. 2007, 42, 202-214.
164. Krötz, F., Sohn, H. Y., Pohl, U., Reactive oxygen species: Players in the platelet game. Arterioscler. Thromb. Vasc. Biol. 2004, 24, 1988-1996.
165. Ghezzi, P., Casagrande, S., Massignan, T., Basso, M., et al., Redox regulation of cyclophilin A by glutathionylation. Proteomics 2006, 6, 817-825.
166. Tome, M. E., Johnson, D. B. F., Rimsza, L. M., Roberts, R. A., et al.., A redox signature score identifies diffuse large B-cell lymphoma patients with a poor prognosis. Blood 2005, 106, 3594-3601.
167. Makino, Y., Yoshikawa, N., Okamoto, K., Hirota, K., et al., Direct association with thioredoxin allows redox regulation of glucocorticoid receptor function. Journal of Biological Chemistry 1999, 274, 3182-3188.
168. Ito, K., Hirao, A., Arai, F., Takubo, K., et al., Reactive oxygen species act through p38 MAPK to limit the lifespan of hematopoietic stem cells. Nature Medicine 2006, 12, 446-451.
169. Bozic, B., Cucnik, S., Kveder, T., Rozman, B., Changes in avidity and specificity of IgG during electro-oxidation. Relevance of binding of antibodies to ?2-GPI. Autoimmun. Rev. 2006, 6, 28-32.
170. Kroon, D. J., Baldwin-Ferro, A., Lalan, P., Identification of sites of degradation in a therapeutic monoclonal antibody by peptide mapping. Pharm. Res. 1992, 9, 1386-1393.
171. Liu, H., Gaza-Bulseco, G., Xiang, T., Chumsae, C., Structural effect of deglycosylation and methionine oxidation on a recombinant monoclonal antibody. Mol. Immunol. 2008, 45, 701-708.
172. Liu, H., Gaza-Bulseco, G., Sun, J., Characterization of the stability of a fully human monoclonal IgG after prolonged incubation at elevated temperature. J. Chromatogr. B: Anal. Technol. Biomed. Life Sci. 2006, 837, 35-43.
173. McIntyre, J. A., Chapman, J., Shavit, E. E., Hamilton, R. L., DeKosky, S. T., Redox-reactive autoantibodies in Alzheimer's patients' cerebrospinal fluids: Preliminary studies. Autoimmunity 2007, 40, 390-396.
174. McIntyre, J. A., Hamilton, R. L., DeKosky, S. T., Redox-reactive autoantibodies in cerebrospinal fluids. Ann. N.Y. Acad. Sci. 2007, 1109, 296-302.
175. McIntyre, J. A., Wagenknecht, D. R., Faulk, W. P., Auto-antibodies unmasked by redox reactions. J. Autoimmun. 2005, 24, 311-317.
176. McIntyre, J. A., Wagenknecht, D. R., Faulk, W. P., Redox-reactive autoantibodies: Detection and physiological relevance. Autoimmun. Rev. 2006, 5, 76-83.
177. De Maat, M. P. M., Verschuur, M., Fibrinogen heterogeneity: Inherited and noninherited. Curr. Opin. Hematol. 2005, 12, 377-383.
178. Lowe, G. D. O., Rumley, A., Mackie, I. J., Plasma fibrinogen. Ann. Clin. Biochem. 2004, 41, 430-440.
179. Mosesson, M. W., Fibrinogen and fibrin structure and functions. J. Thromb. Haemost. 2005, 3, 1894-1904.
180. Cote, H. C. F., Lord, S. T., Pratt, K. P., Gamma-chain dysfibrinogenemias: Molecular structure-function relationships of naturally occurring mutations in the Gamma chain of human fibrinogen. Blood 1998, 92, 2195-2212.
181. Shacter, E., Williams, J. A., Lim, M., Levine, R. L., Differential susceptibility of plasma proteins to oxidative modification: Examination by western blot immunoassay. Free Radic. Biol. Med. 1994, 17, 429-437.
182. Lee, Y. J., Shacter, E., Role of carbohydrates in oxidative modification of fibrinogen and other plasma proteins. Arch. Biochem. Biophys. 1995, 321, 175-181.
183. Inada, Y., Hessel, B., Blomback, B., Photooxidation of fibrinogen in the presence of methylene blue and its effect on polymerization. Biochim. Biophys. Acta 1978, 532, 161-170.
184. Shimizu, A., Saito, Y., Matsushima, A., Inada, Y., Identification of an essential histidine residue for fibrin polymerization. Essential role of histidine 16 of the Bbeta-chain. J. Biol. Chem. 1983, 258, 7915-7917.
185. Suontaka, A. M., Blomback, M., Chapman, J., Changes in functional activities of plasma fibrinogen after treatment with methylene blue and red light. Transfusion 2003, 43, 568-575.
186. Shacter, E., Williams, J. A., Levine, R. L., Oxidative modification of fibrinogen inhibits thrombin-catalyzed clot formation. Free Radic. Biol. Med. 1995, 18, 815-821.
187. Akhter, S., Vignini, A., Wen, Z., English, A., et al., Evidence for S-nitrosothiol-dependent changes in fibrinogen that do not involve transnitrosation or thiolation. Proc. Natl. Acad. Sci. USA 2002, 99, 9172-9177.
188. Roitman, E. V., Azizova, O. A., Morozov, Y. A., Aseichev, A. V., Oxidatively modified fibrinogen modulates blood rheological parameters. Bull. Exp. Biol. Med. 2004, 138, 467-469.
189. Seghatchian, J., de Sousa, G., Pathogen-reduction systems for blood components: The current position and future trends. Transfus. Apher. Sci. 2006, 35, 189-196.
190. Grossweiner, L. I., Photochemistry of proteins: A review. Curr. Eye Res. 1984, 3, 137-144.
191. Davies, M. J., Singlet oxygen-mediated damage to proteins and its consequences. Biochem. Biophys. Res. Commun. 2003, 305, 761-770.
192. Chan, H. L., Gaffney, P. R., Waterfield, M. D., Anderle, H., et al., Proteomic analysis of UVC irradiation-induced damage of plasma proteins: Serum amyloid P component as a major target of photolysis. FEBS Letters 2006, 580, 3229-3236.
193. Garwood, M., Cardigan, R. A., Drummond, O., Hornsey, V. S., et al., The effect of methylene blue photoinactivation and methylene blue removal on the quality of fresh-frozen plasma. Transfusion 2003, 43, 1238-1247.
194. Crettaz, D., Sensebe, L., Vu, D. H., Schneider, P., et al., Proteomics of methylene blue photo-treated plasma before and after removal of the dye by an absorbent filter. Proteomics 2004, 4, 881-891.
195. Depasse, F., Sensebe, L., Seghatchian, J., Andreu, G., Samama, M. M., The influence of methylene blue light treatment and methylene blue removal filter on fibrinogen activity states and fibrin polymerisation indices. Transfus. Apher. Sci. 2005, 33, 63-69.
196. Creasy, D. M., Cottrell, J. S., Unimod: Protein modifications for mass spectrometry. Proteomics 2004, 4, 1534-1536.
197. Hoogland, C., Mostaguir, K., Sanchez, J. C., Hochstrasser, D. F., Appel, R. D., SWISS-2DPAGE, ten years later. Proteomics 2004, 4, 2352-2356.