New method for the quantitative determination of major protein carbonyls, α-aminoadipic and γ-glutamic semialdehydes: Investigation of the formation mechanism and chemical nature in vitro and in vivo

Chemical Research in Toxicology

Volumn 19, Issue 8, 2006, Pages 1059-1065

  Akagawa, Mitsugu ^a   Sasaki, Daisuke ^b   Ishii, Yoshihisa ^c   Kurota, Yayoi ^b   Yotsu Yamashita, Mari ^b   Uchida, Koji ^c   Suyama, Kyozo ^b,d  

^a Osaka Prefecture University   (Japan)

^b TOHOKU UNIVERSITY   (Japan)

^c NAGOYA UNIVERSITY   (Japan)

^d Japan   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

2 AMINOGLUTARALDEHYDIC ACID; ALDEHYDE DERIVATIVE; ALPHA AMINOADIPIC SEMIALDEHYDE; AMINOADIPIC ACID; ASCORBIC ACID; CARBONYL DERIVATIVE; HYDROGEN PEROXIDE; TRANSFERRIN; UNCLASSIFIED DRUG;

AMINATION; ANALYTIC METHOD; ANIMAL EXPERIMENT; ANIMAL TISSUE; ARTICLE; CATALYSIS; CHEMICAL ANALYSIS; COMPLEX FORMATION; CONTROLLED STUDY; DERIVATIZATION; DRUG DETERMINATION; FLUOROMETRY; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; HUMAN; MALE; MOUSE; NONHUMAN; OXIDATION; OXIDATIVE STRESS; PROTEIN ANALYSIS; PROTEIN MODIFICATION; QUANTITATIVE ANALYSIS;

2-AMINOADIPIC ACID; ANIMALS; ASCORBIC ACID; BLOOD PROTEINS; CATTLE; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; GLUTAMATES; HUMANS; HYDROGEN PEROXIDE; MALE; MICE; MICE, INBRED STRAINS; OXIDATION-REDUCTION; PROTEIN CARBONYLATION; RATS; TRANSFERRIN;

EID: 33748670503     PISSN: 0893228X     EISSN: None     Source Type: Journal    
DOI: 10.1021/tx060026p     Document Type: Article

References (33)

1. Davies, M. J. (2005) The oxidative environment and protein damage. Biochim. Biophys. Acta 1703, 93-109.
2. Levine, R. L. (2002) Carbonyl modified proteins in cellular regulation, aging and disease. Free Radical Biol. Med. 32, 790-796.
3. Stadtman, E. R. (1992) Protein oxidation and aging. Science 257, 1220-1224.
4. Beal, M. F. (2002) Oxidatively modified proteins in aging and disease. Free Radical Biol. Med. 32, 797-803.
5. Stadtman, E. R. (2001) Protein oxidation in aging and age-related diseases. Ann. N. Y. Acad. Sci. 928, 22-38.
6. Dalle-Donne, I., Rossi, R., Giustarini, D., Milzani, A., and Colombo, R. (2003) Protein carbonyl groups as biomarkers of oxidative stress. Clin. Chim. Acta 329, 23-38.
7. Nyström, T. (2005) Role of oxidative carbonylation in protein quality control and senescence. EMBO J. 24, 1311-1317.
8. Uchida, K., Szweda, L. I., Chae, H. Z., and Stadtman, E. R. (1993) Immunochemical detection of 4-hydroxy-2-nonenal modified proteins in oxidized hepatocytes. Proc. Natl. Acad. Sci. U.S.A. 90, 8742-8746.
9. Furuhata, A., Nakamura, M., Osawa, T., and Uchida, K. (2002) Thiolation of protein-bound carcinogenic aldehyde: An electrophilic acrolein-lysine adduct that covalently binds to thiols. J. Biol. Chem. 277, 27919-27926.
10. Uchida, K. (2003) Histidine and lysine as targets of oxidative modification. Amino Acids 25, 249-257.
11. Yamada, S., Kumazawa, S., Ishii, T., Nakayama, T., Itakura, K., Shibata, N., Kobayashi, M., Sakai, K., Osawa, T., and Uchida, K. (2001) Immunochemical detection of a lipofuscin-like fluorophore derived from malondialdehyde and lysine. J. Lipid Res. 42, 1187-1196.
12. Liggins, J., and Furth, A. J. (1997) Role of protein-bound carbonyl groups in the formation of advanced glycation endproducts. Biochim. Biophys. Acta 1361, 123-130.
13. Levine, R. L., Williams, J. A., Stadtman, E. R., and Shacter, E. (1994) Carbonyl assays for determination of oxidatively modified proteins. Methods Enzymol. 233, 346-357.
14. Choi, J., Rees, H. D., Weintraub, S. T., Levey, A. I., Chin, L. S., and Li, L. (2005) Oxidative modifications and aggregation of Cu, Zn-superoxide dismutase associated with Alzheimer and Parkinson diseases. J. Biol. Chem. 280, 11648-11655.
15. Choi, J., Malakowsky, C. A., Talent, J. M., Conrad, C. C., and Gracy, R. W. (2002) Identification of oxidized plasma proteins in Alzheimer's disease. Biochem. Biophys. Res. Commun. 293, 1566-1570.
16. Mantle, D., Falkous, G., and Walker, D. (1999) Quantification of protease activities in synovial fluid from rheumatoid and osteoarthritis cases: Comparison with antioxidant and free radical damage markers. Clin. Chim. Acta 284, 45-58.
17. Bowling, A. C., Schulz, J. B., Brown, R. H., Jr., and Beal, M. F. (1993) Superoxide dismutase activity, oxidative damage, and mitochondrial energy metabolism in familial and sporadic amyotrophic lateral sclerosis. J. Neurochem. 61, 2322-2325.
18. Grattagliano, I., Vendemiale, G., Boscia, F., Micelli-Ferrari, T., Cardia, L., and Altomare, E. (1998) Oxidative retinal products and ocular damages in diabetic patients. Free Radical Biol. Med. 25, 369-372.
19. Requena, J. R., Chao, C.-C., Levine, R. L., and Stadtman, E. R. (2001) Glutamic and aminoadipic semialdehydes are the main carbonyl products of metal-catalyzed oxidation of proteins. Proc. Natl. Acad. Sci. U.S.A. 98, 69-74.
20. Ayala, A., and Cutler, R. G. (1996) The utilization of 5-hydroxyl-2-amino valeic acid as a specific marker of oxidized arginine and proline residues in proteins. Free Radical Biol. Med. 21, 65-80.
21. Lent, R. W., Smith, B., Salcedo, L. L., Faris, B., and Franzblau, C. (1969) Studies on the reduction of elastin. II. Evidence for the presence of α-aminoadipic acid δ-semialdehyde and its aldol condensation product. Biochemistry 8, 2837-2845.
22. Daneshvar, B., Frandsen, H., Autrup, H., and Dragsted, L. O. (1997) γ-Glutamyl semialdehyde and 2-amino-adipic semialdehyde: Biomarkers of oxidative damage to proteins. Biomarkers 2, 117-123.
23. Akagawa, M., Sasaki, D., Kurota, Y., and Suyama, K. (2005) Formation of α-aminoadipic and γ-glutamic semialdehydes in proteins by the Maillard reaction. Ann. N. Y. Acad. Sci. 1043, 129-134.
24. Akagawa, M., Wako, Y., and Suyama, K. (1999) Lysyl oxidase coupled with catalase in egg shell membrane. Biochim. Biophys. Acta 1434, 151-160.
25. Yuen, C.-T., Gee, C. K., and Jones, C. (2002) High-performance liquid chromatographic profiling of fluorescent labeled N-glycans on glycoproteins. Biomed. Chromatogr. 16, 247-254.
26. Charlwood, J., Toison, D., Dwek, M., and Camilleri, P. (1999) A detailed analysis of neutral and acidic carbohydrates in human milk. Anal. Biochem. 273, 261-277.
27. Toyokuni, S., Uchida, K., Okamoto, K., Hattori-Nakakuki, Y., Hiai, H., and Stadtman, E. R. (1994) Formation of 4-hydroxy-2-nonenal-modified proteins in the renal proximal tubules of rats treated with a renal carcinogen, ferric nitrilotriacetate. Proc. Natl. Acad. Sci. U.S.A. 91, 2616-2620.
28. Okada, K., Wangpoengtrakul, C., Tanaka, T., Toyokuni, S., Uchida, K., and Osawa, T. (2001) Curcumin and especially tetrahydrocurcumin ameliorate oxidative stress-induced renal injury in mice. J. Nutr. 131, 2090-2095.
29. Lucesoli, F., Caligiuri, M., Roberti, M. F., Perazzo, J. C., and Fraga, C. G. (1999) Dose-dependent increase of oxidative damage in the testes of rats subjected to acute iron overload. Arch. Biochem. Biophys. 372, 37-43.
30. Akagawa, M., and Suyama, K. (2002) Oxidative deamination by hydrogen peroxide in the presence of metals. Free Radical Res. 36, 13-21.
31. Suh, J., Zhu, B. Z., and Frei, B. (2003) Ascorbate does not act as a pro-oxidant towards lipids and proteins in human plasma exposed to redox-active transition metal ions and hydrogen peroxide. Free Radical Biol. Med. 34, 1306-1314.
32. Saito, M., Marumo, K., Fujii, K., and Ishioka, N. (1997) Single-column high-performance liquid chromatographic-fluorescence detection of immature, mature, and senescent cross-links of collagen. Anal. Biochem. 253, 26-32.
33. Sims, T. J., and Bailey, A. J. (1992) Quantitative analysis of collagen and elastin cross-links using a single-column system. J. Chromatogr. Biomed. Appl. 582, 49-55.