Preparation and characterization of a polyclonal antibody against brominated protein

Journal of Clinical Biochemistry and Nutrition

Volumn 44, Issue 1, 2009, Pages 95-103

  Kambayashi, Yasuhiro ^a   Ogino, Keiki ^b   Takemoto, Kei ^b   Imagama, Takashi ^c   Takigawa, Tomoko ^b   Kimura, Shingo ^a   Hibino, Yuri ^a   Hitomi, Yoshiaki ^a   Nakamura, Hiroyuki ^a  

^a KANAZAWA UNIVERSITY   (Japan)

^b OKAYAMA UNIVERSITY   (Japan)

^c YAMAGUCHI UNIVERSITY SCHOOL OF MEDICINE   (Japan)

Author keywords

(Di)bromotyrosine; Allergic disease; Eosinophil activation marker; Oxidative stress; Polyclonal antibody

Indexed keywords

3 NITROTYROSINE; BOVINE SERUM ALBUMIN; BROMINE; CHLORINE; DIBROMOTYROSINE; DIIODOTYROSINE; EOSINOPHIL PEROXIDASE; EPITOPE; IODOTYROSINE; KEYHOLE LIMPET HEMOCYANIN; PHOSPHOTYROSINE; POLYCLONAL ANTIBODY; TYROSINE; TYROSINE DERIVATIVE; UNCLASSIFIED DRUG;

ALLERGY; ANTIBODY SPECIFICITY; ARTICLE; ASTHMA; ATOPIC DERMATITIS; BROMINATION; CELL ACTIVATION; CHLORINATION; CONTROLLED STUDY; ENZYME LINKED IMMUNOSORBENT ASSAY; EOSINOPHIL; HALOGENATION; IMMUNOHISTOCHEMISTRY; NITRATION; NONHUMAN; PATHOGENESIS; RABBIT; RAT;

BOVINAE; ORYCTOLAGUS CUNICULUS; RATTUS;

EID: 60849115833     PISSN: 09120009     EISSN: None     Source Type: Journal    
DOI: 10.3164/jcbn.08-196     Document Type: Article

References (38)

1. Wang, J. and Slungaard, A.: Role of eosinophil peroxidase in host defense and disease pathology. Arch. Biochem. Biophys., 445, 256-260, 2006.
2. MacPherson, J.C., Comhair, S.A.A., Erzurum, S.C., Klein, D.F., Lipscomb, M.F., Kavuru, M.S., Samoszuk, M.K., and Hazen, S.L.: Eosinophils are a major source of nitric oxide-derived oxidants in severe asthma: characterization of pathways available to eosinophils for generating reactive nitrogen species. J. Immunol., 166, 5763-5772, 2001.
3. Kubo, M., Kambayashi, Y., Takemoto, K., Okuda, J., Muto, M., and Ogino, K.: Reactive nitrogen species formation in eosinophils and imbalance in nitric oxide metabolism are involved in atopic dermatitis-like skin lesions in NC/Nga mice. Free Radic. Res., 39, 719-727, 2005.
4. Shibamori, M., Ogino, K., Kambayashi, Y., and Ishiyama, H.: Intranasal mite allergen induces allergic asthma-like responses in NC/Nga mice. Life Sci., 78, 987-994, 2006.
5. Takano, H., Yanagisawa, R., and Inoue, K.: Components of diesel exhaust particles diversely enhance a variety of respiratory diseases related to infection or allergy: extracted organic chemicals and the residual particles after extraction differently affect respiratory diseases. J. Clin. Biochem. Nutr., 40, 101-107, 2007.
6. Hazen, S.L. and Heinecke, J.W.: 3-Chlorotyrosine, a specific marker of myeloperoxidase-catalyzed oxidation, is markedly elevated in low density lipoprotein isolated from human atherosclerotic intima. J. Clin. Invest., 99, 2075-2081, 1997.
7. Buss, I.H., Senthilmohan, R., Darlow, B.A., Mogridge, N., Kettle, A.J., and Winterbourn, C.C.: 3-Chlorotyrosine as a marker of protein damage by myeloperoxidase in tracheal aspirates from preterm infants: association with adverse respiratory outcome. Pediatr. Res., 53, 455-462, 2003.
8. Gujral, J.S., Hinson, J.A., Farhood, A., and Jaeschke, H.: NADPH oxidase-derived oxidant stress is critical for neutrophil cytotoxicity during endotoxemia. Am. J. Phys. Gastrointest. Liver Physiol., 287, G243-G252, 2004.
9. Wu, W., Chen, Y., d'Avignon, A., and Hazen, S.L.: 3-Bromotyrosine and 3,5-dibromotyrosine are major products of protein oxidation by eosinophil peroxidase: potential markers for eosinophil-dependent tissue injury in vivo. Biochemistry, 38, 3538-3548, 1999.
10. Harrison, J.E. and Schultz, J.: Studies on the chlorinating activity of myeloperoxidase. J. Biol. Chem., 251, 1371-1374, 1976.
11. Weiss, S.J., Klein, R., Slivka, A., and Wei, M.: Chlorination of taurine by human neutrophils. Evidence for hypochlorous acid generation. J. Clin. Invest., 70, 598-607, 1982.
12. Foote, C.S., Goyne, T.E., and Lehrer, R.I.: Assessment of chlorination by human neutrophils. Nature, 301, 715-716, 1983.
13. Mayeno, A.N., Curran, A.J., Roberts, R.L., and Foote, C.S.: Eosinophils preferentially use bromide to generate halogenating agents. J. Biol. Chem., 264, 5660-5668, 1989.
14. van Dalen, C.J. and Kettle, A.J.: Substrates and products of eosinophil peroxidase. Biochem. J., 358, 233-239, 2001.
15. Weiss, S.J., Test, S.T., Eckmann, C.M., Ross, D., and Regiani, S.: Brominating oxidants generated by human eosinophils. Science, 234, 200-203, 1986.
16. Thomas, E.L., Bozeman, P.M., Jefferson, M.M., and King, C.C.: Oxidation of bromide by the human leukocyte enzymes myeloperoxidase and eosinophil peroxidase. Formation of bromamines. J. Biol. Chem., 270, 2906-2913, 1995.
17. Furtmüller, P.G., Zederbauer, M., Jantschko, W., Helm, J., Bogner, M., Jakopitsch, C., and Obinger, C.: Active site structure and catalytic mechanisms of human peroxidases. Arch. Biochem. Biophys., 445, 199-213, 2006.
18. Senthilmohan, R. and Kettle, A.J.: Bromination and chlorination reactions of myeloperoxidase at physiological concentrations of bromine and chloride. Arch. Biochem. Biophys., 445, 225-234, 2006.
19. Spalteholz, H., Panasenko, O.M., and Arnhold, J.: Formation of reactive halide species by myeloperoxidase and eosinophil peroxidase. Arch. Biochem. Biophys., 445, 225-234, 2006.
20. Brennan, M.L., Wu, W., Fu, X., Shen, Z., Song, W., Frost, H., Vadseth, C., Narine, L., Lenkiewicz, E., Borchers, M.T., Lusis, A.J., Lee, J.J., Lee, N.A., Abu-Soud, H.M., Ischiropoulos, H., and Hazen, S.L.: 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 peroxidase-generated reactive nitrogen species. J. Biol. Chem., 277, 17415-17427, 2002.
21. Aldridge, R.E., Chan, T., van Dalen, C.J., Senthilmohan, R., Winn, M., Venge, P., Town, G.I., and Kettle, A.J.: Eosinophil peroxidase produces hypobromous acid in the airways of stable asthmatics. Free Radic. Biol. Med., 33, 847-856, 2002.
22. Mita, H., Higashi, N., Taniguchi, M., Higashi, A., Kawagishi, Y., and Akiyama, K.: Urinary 3-bromotyrosine and 3-chlorotyrosine concentrations in asthmatic patients: lack of increase in 3-bromotysine concentration in urine and plasma proteins in aspirin-induced asthma after intravenous aspirin challenge. Clin. Exp. Allergy, 34, 931-938, 2004.
23. Morris, J.C.: The acid ionization constant of HOC1 from 5 to 35°C. J. Phys. Chem., 70, 3798-3805, 1966.
24. Wajon, J.E. and Morris, J.C.: Rates of formation of N-bromo amines in aqueous solution. Inorg. Chem., 21, 4258-4263, 1982.
25. 67Ga-labeled antibodies for immuno-scintigraphy and evaluation of tumor targeting of drug-antibody conjugates in mice. Cancer Res., 48, 1189-1194, 1988.
26. Hinson, J.A., Michael, S.L., Ault, S.G., and Pumford, N.R.: Western blot analysis for nitrotyrosine protein adducts in livers of saline-treated and acetaminophen-treated mice. Toxicol. Sci., 53, 467-473, 2000.
27. Seiler, G., Westerman, R.A., and Wilson, J.A.: The role of specific eosinophil granules in eosinophil-induced experimental encephalitis. Neurology, 19, 478-488, 1969.
28. Holzbecher, J. and Ryan, D.E..: The rapid determination of total bromine and iodine in biological fluids by neutron activation. Clin. Biochem., 13, 277-278, 1980.
29. Tsikas, D.: Methods of quantitative analysis of the nitric oxide metabolites nitrite and nitrate in human biological fluids. Free Radic. Res., 39, 797-815, 2005.
30. Zheng, L., Settle, M., Brubaker, G., Schmitt, D., Hazen, S.L., Smith, J.D., and Kinter, M.: Localization of nitration and chlorination sites on apoprotein A-I catalyzed by myeloperoxidase in human atheroma and associated oxidative impairment in ABCA1-dependent cholesterol efflux from macrophages. J. Biol. Chem., 280, 38-47, 2005.
31. Shao, B., Bergt, C., Fu, X., Green, P., Voss, J.C., Oda, M.N., Oram, J.F., and Heinecke, J.W.: 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, 2005.
32. Shao, B., Oda, M.N., Bergt, C., Fu, X., Green, P.S., Brot, N., Oram, J.F., and Heinecke, J.W.: Myeloperoxidase impairs ABCA1-dependent cholesterol efflux through methionine oxidation and site-specific tyrosine chlorination of apolipoprotein A-I. J. Biol. Chem., 281, 9001-9004, 2006.
33. Salavej, P., Spalteholz, H., and Arnhold, J.: Modification of amino acid residues in human serum albumin by myeloperoxidase. Free Radic. Biol. Med., 40, 516-525, 2006.
34. Malle, E., Hazell, L., Stocker, R., Sattler, W., Esterbauer, H., and Waeg, G.: Immunologic detection and measurement of hypochlorite-modified LDL with specific monoclonal antibodies. Arterioscler. Thromb. Vasc. Biol., 15, 982-989, 1995.
35. Kato, Y., Kawai, Y., Morinaga, H., Kondo, H., Dozaki, N., Kitamoto, N., and Osawa, T.: Immunogenicity of a brominated protein and successive establishment of a monoclonal antibody to dihalogenated tyrosine. Free Radic. Biol, Med., 38, 24-31, 2005.
36. Hasegawa, T., Malle, E., Farhood, A., and Jaeschke, H.: Generation of hypochlorite-modified proteins by neutrophils during ischemia-reperfusion injury in rat liver: attenuation by ischemic preconditioning. Am. J. Physiol. Gastrointest. Liver Physiol., 289, G760-G767, 2005.
37. Chapman, A.L.P., Senthilmohan, R., Winterbourn, C.C., and Kettle, A.J.: Comparison of mono- and dichlorinated tyrosines with carbonyls for detection of hypochlorous acid modified proteins. Arch. Biochem. Biophys., 377, 95-100, 2000.
38. Wu, W., Samoszuk, M.K., Comhair, S.A.A., Thomassen, M.J., Farver, C.F., Dweik, R.A., Kavuru, M.S., Erzurum, S.C., and Hazen, S.L.: Eosinophils generate brominating oxidants in allergen-induced asthma. J. Clin. Invest., 105, 1455-1463, 2000.