Detection and Quantification of Protein Disulfides in Biological Tissues: A Fluorescence-Based Proteomic Approach

Methods in Enzymology

Volumn 473, Issue , 2010, Pages 161-177

  Pérez, Viviana I ^a,c   Pierce, Anson ^a,c,d   de Waal, Eric M ^b   Ward, Walter F ^a,c   Bokov, Alex ^a,c   Chaudhuri, Asish ^c,d   Richardson, Arlan ^a,c,d  

^a University of Texas Health Science Center at San Antonio   (United States)

^b UNIVERSITY OF TEXAS AT SAN ANTONIO   (United States)

^c UNIVERSITY OF TEXAS HEALTH SCIENCE CENTER AT SAN ANTONIO   (United States)

^d SOUTH TEXAS VETERANS HEALTH CARE SYSTEM   (United States)

Author keywords

Aging; Cysteine oxidation; Protein disulfide; Protein oxidation

Indexed keywords

DISULFIDE; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; PROTEIN;

AGING; ANIMAL; ANIMAL ANATOMY; ARTICLE; C57BL MOUSE; CHEMISTRY; COMPARATIVE STUDY; EVALUATION; FLUORESCENCE; LUMINESCENCE; MALE; METABOLISM; METHODOLOGY; MOUSE; OXIDATIVE STRESS; PHYSIOLOGY; PROTEOMICS;

AGING; ANIMAL STRUCTURES; ANIMALS; DISULFIDES; FLUORESCENCE; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE (PHOSPHORYLATING); LUMINESCENT MEASUREMENTS; MALE; MICE; MICE, INBRED C57BL; OXIDATIVE STRESS; PROTEINS; PROTEOMICS;

EID: 77956207153     PISSN: 00766879     EISSN: 15577988     Source Type: Book Series    
DOI: 10.1016/S0076-6879(10)73008-1     Document Type: Chapter

References (31)

1. Berlett, B.S., Stadtman, E.R., Protein oxidation in aging, disease, and oxidative stress. J. Biol. Chem. 272 (1997), 20313–20316.
2. Bokov, A., Chaudhuri, A., Richardson, A., The role of oxidative damage and stress in aging. Mech. Ageing Dev. 125 (2004), 811–826.
3. Butterfield, D.A., Kanski, J., Brain protein oxidation in age-related neurodegenerative disorders that are associated with aggregated proteins. Mech. Ageing Dev. 122 (2001), 945–962.
4. Cabreiro, F., Picot, C.R., Friguet, B., Petropoulos, I., Methionine sulfoxide reductases: Relevance to aging and protection against oxidative stress. Ann. NY Acad. Sci. 1067 (2006), 37–44.
5. Chao, C.C., Ma, Y.S., Stadtman, E.R., Modification of protein surface hydrophobicity and methionine oxidation by oxidative systems. Proc. Natl. Acad. Sci. USA 94 (1997), 2969–2974.
6. Chaudhuri, A.R., Khan, I.A., Luduena, R.F., Detection of disulfide bonds in bovine brain tubulin and their role in protein folding and microtubule assembly in vitro: A novel disulfide detection approach. Biochemistry 40 (2001), 8834–8841.
7. Chaudhuri, A.R., de Waal, E.M., Pierce, A., Van Remmen, H., Ward, W.F., Richardson, A., Detection of protein carbonyls in aging liver tissue: A fluorescence-based proteomic approach. Mech. Ageing Dev. 127 (2006), 849–861.
8. Cumming, R.C., Andon, N.L., Haynes, P.A., Park, M., Fischer, W.H., Schubert, D., Protein disulfide bond formation in the cytoplasm during oxidative stress. J. Biol. Chem. 279 (2004), 21749–21758.
9. Eaton, P., Protein thiol oxidation in health and disease: Techniques for measuring disulfides and related modifications in complex protein mixtures. Free Radic. Biol. Med. 40 (2006), 1889–1899.
10. Han, E.S., Muller, F.L., Perez, V.I., Qi, W., Liang, H., Xi, L., Fu, C., Doyle, E., Hickey, M., Cornell, J., Epstein, C.J., Roberts, L.J., Van Remmen, H., Richardson, A., The in vivo gene expression signature of oxidative stress. Physiol. Genomics 34 (2008), 112–126.
11. Huggins, T.G., Wells-Knecht, M.C., Detorie, N.A., Baynes, J.W., Thorpe, S.R., Formation of o-tyrosine and dityrosine in proteins during radiolytic and metal-catalyzed oxidation. J. Biol. Chem. 268 (1993), 12341–12347.
12. Jones, G.M., Vale, J.A., Mechanisms of toxicity, clinical features, and management of diquat poisoning: A review. J. Toxicol. Clin. Toxicol. 38 (2000), 123–128.
13. Kanski, J., Schoneich, C., Protein nitration in biological aging: Proteomic and tandem mass spectrometric characterization of nitrated sites. Methods Enzymol. 396 (2005), 160–171.
14. Kim, S.O., Merchant, K., Nudelman, R., Beyer, W.F. Jr., Keng, T., DeAngelo, J., Hausladen, A., Stamler, J.S., OxyR: A molecular code for redox-related signaling. Cell 109 (2002), 383–396.
15. Olivares-Corichi, I.M., Ceballos, G., Medina-Santillan, R., Medina-Navarro, R., Guzman-Grenfell, A.M., Hicks, J.J., Oxidation by reactive oxygen species (ROS) alters the structure of human insulin and decreases the insulin-dependent D-glucose-C14 utilization by human adipose tissue. Front. Biosci. 10 (2005), 3127–3131.
16. Oliver, C.N., Ahn, B.W., Moerman, E.J., Goldstein, S., Stadtman, E.R., Age-related changes in oxidized proteins. J. Biol. Chem. 262 (1987), 5488–5491.
17. Pierce, A., deWaal, E., Van Remmen, H., Richardson, A., Chaudhuri, A., A novel approach for screening the proteome for changes in protein conformation. Biochemistry 45 (2006), 3077–3085.
18. Pierce, A.P., de Waal, E., McManus, L.M., Shireman, P.K., Chaudhuri, A.R., Oxidation and structural perturbation of redox-sensitive enzymes in injured skeletal muscle. Free Radic. Biol. Med. 43 (2007), 1584–1593.
19. Pierce, A., Mirzaei, H., Muller, F., De Waal, E., Taylor, A.B., Leonard, S., Van Remmen, H., Regnier, F., Richardson, A., Chaudhuri, A., GAPDH is conformationally and functionally altered in association with oxidative stress in mouse models of amyotrophic lateral sclerosis. J. Mol. Biol. 382 (2008), 1195–1210.
20. Raju, S.V., Barouch, L.A., Hare, J.M., Nitric oxide and oxidative stress in cardiovascular aging. Sci. Aging Knowledge Environ., 21, 2005, re4.
21. Schmalhausen, E.V., Pleten, A.P., Muronetz, V.I., Ascorbate-induced oxidation of glyceraldehyde 3-phosphate dehydrogenase. Biochem. Biophys. Res. Commun. 308 (2003), 492–496.
22. Schoneich, C., Protein modification in aging: An update. Exp. Gerontol. 41 (2006), 807–812.
23. Smith, L.L., Paraquat toxicity. Philos. Trans. R. Soc. Lond. B Biol. Sci. 311 (1985), 647–657.
24. Sohal, R.S., Agarwal, S., Dubey, A., Orr, W.C., Protein oxidative damage is associated with life expectancy of houseflies. Proc. Natl. Acad. Sci. USA 90 (1993), 7255–7259.
25. Sohal, R.S., Sohal, B.H., Orr, W.C., Mitochondrial superoxide and hydrogen peroxide generation, protein oxidative damage, and longevity in different species of flies. Free Radic. Biol. Med. 19 (1995), 499–504.
26. Stadtman, E.R., Van Remmen, H., Richardson, A., Wehr, N.B., Levine, R.L., Methionine oxidation and aging. Biochim. Biophys. Acta 1703 (2005), 135–140.
27. Thomas, J.A., Mallis, R.J., Aging and oxidation of reactive protein sulfhydryls. Exp. Gerontol. 36 (2001), 1519–1526.
28. Uchida, K., Toyokuni, S., Nishikawa, K., Kawakishi, S., Oda, H., Hiai, H., Stadtman, E.R., Michael addition-type 4-hydroxy-2-nonenal adducts in modified low-density lipoproteins: Markers for atherosclerosis. Biochemistry 33 (1994), 12487–12494.
29. Yoo, B.S., Regnier, F.E., Protoemic analysis of carbonylated proteins in two-dimensional gel electrophoresis using avidin-fluorescein affinity staining. Electrophoresis 25 (2004), 1334–1341.
30. Zeng, R., Xu, Q., Shao, X.X., Wang, K.Y., Xia, Q.C., Determination of the disulfide bond pattern of a novel C-type lectin from snake venom by mass spectrometry. Rapid Commun. Mass Spectrom. 15 (2001), 2213–22120.
31. Zhou, J.Q., Gafni, A., Exposure of rat muscle phosphoglycerate kinase to a nonenzymatic MFO system generates the old form of the enzyme. J. Gerontol. 46 (1991), B217–B221.