Quantitative evaluation of the role of cysteine and methionine residues in the antioxidant activity of human serum albumin using recombinant mutants

IUBMB Life

Volumn 64, Issue 5, 2012, Pages 450-454

  Iwao, Yasunori ^a,b   Ishima, Yu ^a   Yamada, Junji ^a   Noguchi, Taishi ^a   Kragh Hansen, Ulrich ^c   Mera, Katsumi ^a   Honda, Daisuke ^a   Suenaga, Ayaka ^a   Maruyama, Toru ^a   Otagiri, Masaki ^a,d  

^a KUMAMOTO UNIVERSITY   (Japan)

^b UNIVERSITY OF SHIZUOKA   (Japan)

^c AARHUS UNIVERSITY   (Denmark)

^d SOJO UNIVERSITY   (Japan)

Author keywords

Antioxidant activity; Cysteine; Human serum albumin; Methionine; Nitric oxide; Reactive oxygen species

Indexed keywords

CYSTEINE; HUMAN SERUM ALBUMIN; HYDROXYL RADICAL; HYPOCHLOROUS ACID; METHIONINE; MUTANT PROTEIN; REACTIVE NITROGEN SPECIES; REACTIVE OXYGEN METABOLITE; RECOMBINANT PROTEIN;

ANTIOXIDANT ACTIVITY; ARTICLE; CHEMOLUMINESCENCE; CONTROLLED STUDY; ELECTRON SPIN RESONANCE; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; HUMAN; QUANTITATIVE ANALYSIS;

AMINO ACID SUBSTITUTION; CYSTEINE; ELECTRON SPIN RESONANCE SPECTROSCOPY; FREE RADICAL SCAVENGERS; FREE RADICALS; HUMANS; METHIONINE; MUTAGENESIS, SITE-DIRECTED; NITRIC OXIDE; REACTIVE OXYGEN SPECIES; RECOMBINANT PROTEINS; SERUM ALBUMIN;

EID: 84859795566     PISSN: 15216543     EISSN: 15216551     Source Type: Journal    
DOI: 10.1002/iub.567     Document Type: Article

References (18)

1. Cross, C. E., Halliwell, B., Borish, E. T., Pryor, W. A., Ames, et al. (1987) Oxygen radicals and human disease. Ann. Intern. Med. 107, 526-545.
2. Halliwell, B. and Whiteman, M. (2004) Measuring reactive species and oxidative damage in vivo and in cell culture: how should you do it and what do the results mean? Br. J. Pharmacol. 142, 231-255. (Pubitemid 38746160)
3. Halliwell, B. (1996) Antioxidants in human health and disease. Annu. Rev. Nutr. 16, 33-50.
4. Phillips, A., Shaper, A. G., and Whincup, P. H. (1989) Association between serum albumin and mortality from cardiovascular disease, cancer, and other causes. Lancet 2, 1434-1436. (Pubitemid 20012066)
5. Bourdon, E. and Blache, D. (2001) The importance of proteins in defense against oxidation. Antioxid. Redox. Signal. 3, 293-311. (Pubitemid 32473344)
6. Oettl, K. and Stauber, R. E. (2007) Physiological and pathological changes in the redox state of human serum albumin critically influence its binding properties. Br. J. Pharmacol. 151, 580-590. (Pubitemid 47016287)
7. Narazaki, R., Maruyama, T., and Otagiri, M. (1997) Probing the cysteine 34 residue in human serum albumin using fluorescence techniques. Biochim. Biophys. Acta. 1338, 275-281. (Pubitemid 27157009)
8. Berlett, B. S. and Stadtman, E. R. (1997) Protein oxidation in aging, disease, and oxidative stress. J. Biol. Chem. 272, 20313-20316. (Pubitemid 27355575)
9. Levine, R. L., Mosoni, L., Berlett, B. S., and Stadtman, E. R. (1996) Methionine residues as endogenous antioxidants in proteins. Proc. Natl. Acad. Sci. USA 93, 15036-15040. (Pubitemid 27009547)
10. Moskovitz, J., Flescher, E., Berlett, B. S., Azare, J., Poston, J. M., et al. (1998) Overexpression of peptide-methionine sulfoxide reductase in Saccharomyces cerevisiae and human T cells provides them with high resistance to oxidative stress. Proc. Natl. Acad. Sci. USA 95, 14071-14075. (Pubitemid 28549322)
11. Bourdon, E., Loreau, N., Lagrost, L., and Blache, D. (2005) Differential effects of cysteine and methionine residues in the antioxidant activity of human serum albumin. Free Radic. Res. 39, 15-20. (Pubitemid 40309466)
12. Finch, J. W., Crouch, R. K., Knapp, D. R., and Schey, K. L. (1993) Mass spectrometric identification of modifications to human serum albumin treated with hydrogen peroxide. Arch. Biochem. Biophys. 305, 595-599. (Pubitemid 23282951)
13. Salavej, P., Spalteholz, H., and Arnhold, J. (2006) Modification of amino acid residues in human serum albumin by myeloperoxidase. Free Radic. Biol. Med. 40, 516-525. (Pubitemid 43139687)
14. Iwao, Y., Anraku, M., Yamasaki, K., Kragh-Hansen, U., Kawai, K., et al. (2006) Oxidation of Arg-410 promotes the elimination of human serum albumin. Biochim. Biophys. Acta. 1764, 743-749.
15. Jourd'heuil, F. L., Lowery, A. M., Melton, E. M., Mnaimneh, S., Bryan, N. S., et al. (2010) Redox-sensitivity and site-specificity of S- and N-denitrosation in proteins. PLoS One 5, e14400.
16. Ascenzi, P., Cao, Y., di Masi, A., Gullotta, F., De Sanctis, G., et al. (2010) Reductive nitrosylation of ferric human serum heme-albumin. FEBS J. 277, 2474-2485.
17. 2-mediated oxidation of ferrous nitrosylated human serum heme-albumin is limited by nitrogen monoxide dissociation. Biochem. Biophys. Res. Commun. 406, 112-116.
18. Di Giuseppe, D., Ulivelli, M., Bartalini, S., Battistini, S., Cerase, A., et al. (2010) Regulation of redox forms of plasma thiols by albumin in multiple sclerosis after fasting and methionine loading test. Amino Acids 38, 1461-1471.