Identification of 3-Nitrotyosine-Modified Brain Proteins by Redox Proteomics

Methods in Enzymology

Volumn 440, Issue , 2008, Pages 295-308

  Butterfield, D Allan ^a,b   Sultana, Rukhsana ^a,b  

^a UNIVERSITY OF KENTUCKY   (United States)

^b UNIVERSITY OF KENTUCKY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

3 NITROTYROSINE; BRAIN PROTEIN; 3-NITROTYROSINE; DRUG DERIVATIVE; NERVE PROTEIN; TYROSINE;

GEL ELECTROPHORESIS; IMAGE ANALYSIS; ISOELECTRIC FOCUSING; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEOMICS; REHYDRATION; REVIEW; TWO DIMENSIONAL GEL ELECTROPHORESIS; WESTERN BLOTTING; ANIMAL; BRAIN; CHEMISTRY; CLASSIFICATION; HUMAN; METABOLISM; METHODOLOGY; OXIDATION REDUCTION REACTION;

ANIMALIA;

ANIMALS; BRAIN; HUMANS; NERVE TISSUE PROTEINS; OXIDATION-REDUCTION; PROTEOMICS; TYROSINE;

EID: 44849106187     PISSN: 00766879     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0076-6879(07)00819-1     Document Type: Review

References (43)

1. Amoresano A., Chiappetta G., Pucci P., D'Ischia M., and Marino G. Bidimensional tandem mass spectrometry for selective identification of nitration sites in proteins. Anal. Chem. 79 (2007) 2109-2117
2. Anantharaman M., Tangpong J., Keller J.N., Murphy M.P., Markesbery W.R., Kiningham K.K., and St. Clair D.K. Beta-amyloid mediated nitration of manganese superoxide dismutase: Implication for oxidative stress in a APPNLH/NLH X PS-1P264L/P264L double knock-in mouse model of Alzheimer's disease. Am. J. Pathol. 168 (2006) 1608-1618
3. Aulak K.S., Koeck T., Crabb J.W., and Stuehr D.J. Dynamics of protein nitration in cells and mitochondria. Am. J. Physiol. Heart Circ. Physiol. 286 (2004) H30-H38
4. Aulak K.S., Koeck T., Crabb J.W., and Stuehr D.J. Proteomic method for identification of tyrosine-nitrated proteins. Methods Mol. Biol. 279 (2004) 151-165
5. Beckman J.S. Protein tyrosine nitration and peroxynitrite. FASEB J. 16 (2002) 1144
6. Beckman J.S., Ischiropoulos H., Zhu L., van der Woerd M., Smith C., Chen J., Harrison J., Martin J.C., and Tsai M. Kinetics of superoxide dismutase- and iron-catalyzed nitration of phenolics by peroxynitrite. Arch. Biochem. Biophys. 298 (1992) 438-445
7. Buchczyk D.P., Grune T., Sies H., and Klotz L.O. Modifications of glyceraldehyde-3-phosphate dehydrogenase induced by increasing concentrations of peroxynitrite: Early recognition by 20S proteasome. Biol. Chem. 384 (2003) 237-241
8. Butterfield D.A. Proteomics: A new approach to investigate oxidative stress in Alzheimer's disease brain. Brain Res. 1000 (2004) 1-7
9. Butterfield D.A., Boyd-Kimball D., and Castegna A. Proteomics in Alzheimer's disease: Insights into mechanisms of neurodegeneration. J. Neurochem. 86 (2003) 1313-1327
10. Butterfield D.A., Perluigi M., and Sultana R. Oxidative stress in Alzheimer's disease brain: New insights from redox proteomics. Eur. J. Pharmacol. 545 (2006) 39-50
11. Butterfield D.A., Poon H.F., St. Clair D., Keller J.N., Pierce W.M., Klein J.B., and Markesbery W.R. Redox proteomics identification of oxidatively modified hippocampal proteins in mild cognitive impairment: Insights into the development of Alzheimer's disease. Neurobiol. Dis. 22 (2006) 223-232
12. Butterfield D.A., Reed T., Newman S.F., and Sultana R. Roles of amyloid beta-peptide-associated oxidative stress and brain protein modifications in the pathogenesis of Alzheimer's disease and mild cognitive impairment. Free Radic. Biol. Med. 43 (2007) 658-677
13. Butterfield D.A., Reed T.T., Perluigi M., De Marco C., Coccia R., Keller J.N., Markesbery W.R., and Sultana R. Elevated levels of 3-nitrotyrosine in brain from subjects with amnestic mild cognitive impairment: Implications for the role of nitration in the progression of Alzheimer's disease. Brain Res. 1148 (2007) 243-248
14. Butterfield D.A., and Stadtman E.R. Protein oxidation processes in aging brain. Adv. Cell Aging Gerontol. 2 (1997) 161-191
15. Castegna A., Thongboonkerd V., Klein J.B., Lynn B., Markesbery W.R., and Butterfield D.A. Proteomic identification of nitrated proteins in Alzheimer's disease brain. J. Neurochem. 85 (2003) 1394-1401
16. Dalle-Donne I., Scaloni A., and Butterfield D.A. "Redox Proteomics: From Protein Modifications to Cellular Dysfunction and Diseases." (2006), Wiley, Hoboken, NJ
17. Dalle-Donne I., Scaloni A., Giustarini D., Cavarra E., Tell G., Lungarella G., Colombo R., Rossi R., and Milzani A. Proteins as biomarkers of oxidative/nitrosative stress in diseases: The contribution of redox proteomics. Mass Spectrom. Rev. 24 (2005) 55-99
18. Di Stasi A.M., Mallozzi C., Macchia G., Petrucci T.C., and Minetti M. Peroxynitrite induces tryosine nitration and modulates tyrosine phosphorylation of synaptic proteins. J. Neurochem. 73 (1999) 727-735
19. Good P.F., Hsu A., Werner P., Perl D.P., and Olanow C.W. Protein nitration in Parkinson's disease. J. Neuropathol. Exp. Neurol. 57 (1998) 338-342
20. Gow A.J., Duran D., Malcolm S., and Ischiropoulos H. Effects of peroxynitrite-induced protein modifications on tyrosine phosphorylation and degradation. FEBS Lett. 385 (1996) 63-66
21. Grune T., Reinheckel T., and Davies K.J. Degradation of oxidized proteins in mammalian cells. FASEB J. 11 (1997) 526-534
22. Halliwell B., Zhao K., and Whiteman M. Nitric oxide and peroxynitrite. The ugly, the uglier and the not so good: A personal view of recent controversies. Free Radic. Res. 31 (1999) 651-669
23. Hensley K., Maidt M.L., Yu Z., Sang H., Markesbery W.R., and Floyd R.A. Electrochemical analysis of protein nitrotyrosine and dityrosine in the Alzheimer brain indicates region-specific accumulation. J. Neurosci. 18 (1998) 8126-8132
24. Horiguchi T., Uryu K., Giasson B.I., Ischiropoulos H., LightFoot R., Bellmann C., Richter-Landsberg C., Lee V.M., and Trojanowski J.Q. Nitration of tau protein is linked to neurodegeneration in tauopathies. Am. J. Pathol. 163 (2003) 1021-1031
25. Hyun D.H., Lee M., Halliwell B., and Jenner P. Proteasomal inhibition causes the formation of protein aggregates containing a wide range of proteins, including nitrated proteins. J. Neurochem. 86 (2003) 363-373
26. Ischiropoulos H., and Beckman J.S. Oxidative stress and nitration in neurodegeneration: Cause, effect, or association?. J. Clin. Invest. 111 (2003) 163-169
27. Ischiropoulos H., Zhu L., Chen J., Tsai M., Martin J.C., Smith C.D., and Beckman J.S. Peroxynitrite-mediated tyrosine nitration catalyzed by superoxide dismutase. Arch. Biochem. Biophys. 298 (1992) 431-437
28. Jiang H., and Balazy M. Detection of 3-nitrotyrosine in human platelets exposed to peroxynitrite by a new gas chromatography/mass spectrometry assay. Nitric Oxide 2 (1998) 350-359
29. Kong S.K., Yim M.B., Stadtman E.R., and Chock P.B. Peroxynitrite disables the tyrosine phosphorylation regulatory mechanism: Lymphocyte-specific tyrosine kinase fails to phosphorylate nitrated cdc2(6-20)NH2 peptide. Proc. Natl. Acad. Sci. USA 93 (1996) 3377-3382
30. Koppenol W.H., Moreno J.J., Pryor W.A., Ischiropoulos H., and Beckman J.S. Peroxynitrite, a cloaked oxidant formed by nitric oxide and superoxide. Chem. Res. Toxicol. 5 (1992) 834-842
31. Kuhn D.M., Sakowski S.A., Sadidi M., and Geddes T.J. Nitrotyrosine as a marker for peroxynitrite-induced neurotoxicity: The beginning or the end of the end of dopamine neurons?. J. Neurochem. 89 (2004) 529-536
32. Mallozzi C., Di Stasi A.M., and Minetti M. Peroxynitrite modulates tyrosine-dependent signal transduction pathway of human erythrocyte band 3. FASEB J. 11 (1997) 1281-1290
33. Marechal A., Mattioli T.A., Stuehr D.J., and Santolini J. Activation of peroxynitrite by inducible nitric-oxide synthase: A direct source of nitrative stress. J. Biol. Chem. 282 (2007) 14101-14112
34. Pennathur S., Jackson-Lewis V., Przedborski S., and Heinecke J.W. Mass spectrometric quantification of 3-nitrotyrosine, ortho-tyrosine, and o,o'-dityrosine in brain tissue of 1-methyl-4-phenyl-1,2,3, 6-tetrahydropyridine-treated mice, a model of oxidative stress in Parkinson's disease. J. Biol. Chem. 274 (1999) 34621-34628
35. Poladia D.P., and Bauer J.A. Early cell-specific changes in nitric oxide synthases, reactive nitrogen species formation, and ubiquitinylation during diabetes-related bladder remodeling. Diabetes Metab. Res. Rev. 19 (2003) 313-319
36. Smith M.A., Richey Harris P.L., Sayre L.M., Beckman J.S., and Perry G. Widespread peroxynitrite-mediated damage in Alzheimer's disease. J. Neurosci. 17 (1997) 2653-2657
37. Sodum R.S., Akerkar S.A., and Fiala E.S. Determination of 3-nitrotyrosine by high-pressure liquid chromatography with a dual-mode electrochemical detector. Anal. Biochem. 280 (2000) 278-285
38. Souza J.M., Choi I., Chen Q., Weisse M., Daikhin E., Yudkoff M., Obin M., Ara J., Horwitz J., and Ischiropoulos H. Proteolytic degradation of tyrosine nitrated proteins. Arch. Biochem. Biophys. 380 (2000) 360-366
39. Squadrito G.L., and Pryor W.A. Mapping the reaction of peroxynitrite with CO2: Energetics, reactive species, and biological implications. Chem. Res. Toxicol. 15 (2002) 885-895
40. Sultana R., Poon H.F., Cai J., Pierce W.M., Merchant M., Klein J.B., Markesbery W.R., and Butterfield D.A. Identification of nitrated proteins in Alzheimer's disease brain using a redox proteomics approach. Neurobiol. Dis. 22 (2006) 76-87
41. Sultana R., Reed T.T., Perluigi M., Coccia R., Pierce W.M., and Butterfield D.A. Proteomic identification of nitrated brain proteins in amnestic mild cognitive impairment: A regional study. J. Cell. Mol. Med. 11 (2007) 839-851
42. van der Vliet A., Eiserich J.P., O'Neill C.A., Halliwell B., and Cross C.E. Tyrosine modification by reactive nitrogen species: A closer look. Arch. Biochem. Biophys. 319 (1995) 341-349
43. Yi D., Ingelse B.A., Duncan M.W., and Smythe G.A. Quantification of 3-nitrotyrosine in biological tissues and fluids: Generating valid results by eliminating artifactual formation. J. Am. Soc. Mass Spectrom. 11 (2000) 578-586