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

被引:49
作者
Iwao, Yasunori [1 ,2 ]
Ishima, Yu [1 ,3 ]
Yamada, Junji [1 ]
Noguchi, Taishi [1 ]
Kragh-Hansen, Ulrich [4 ]
Mera, Katsumi [1 ]
Honda, Daisuke [1 ]
Suenaga, Ayaka [1 ]
Maruyama, Toru [1 ,3 ]
Otagiri, Masaki [1 ,5 ]
机构
[1] Kumamoto Univ, Dept Biopharmaceut, Grad Sch Pharmaceut Sci, Kumamoto 8620973, Japan
[2] Univ Shizuoka, Sch Pharmaceut Sci, Dept Pharmaceut Engn, Shizuoka 4228526, Japan
[3] Kumamoto Univ, Ctr Clin Pharmaceut Sci, Kumamoto, Japan
[4] Univ Aarhus, Dept Med Biochem, DK-8000 Aarhus C, Denmark
[5] Sojo Univ, Fac Pharmaceut Sci, Kumamoto, Japan
关键词
human serum albumin; antioxidant activity; reactive oxygen species; nitric oxide; cysteine; methionine; OXIDATIVE STRESS; DISEASE; PROTEINS;
D O I
10.1002/iub.567
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The importance of cysteine (Cys) and methionine (Met) residues for the antioxidant activity of human serum albumin (HSA) was investigated using recombinant HSA mutants, in which Cys34 and/or the six Met residues had been mutated to Ala. The scavenging activities of the mutants against five reactive oxygen and nitrogen species were evaluated by a chemiluminescence assay, electron paramagnetic resonance spectroscopy, or a HPLC-flow reactor assay. Our results showed that the contributions of Cys34 and the Met residues to the antioxidant activity of HSA were 61% and 29% against O2 -, 68% and 61% against H2O2, 38% and 6% against HO, 36% and 13% against HOCl, and 51% and 1% against NO, respectively. Thus, the findings propose in a direct way that Cys34 plays a more important role than the Met residues in the antioxidant activity of HSA. (c) 2012 IUBMB Life, 2012
引用
收藏
页码:450 / 454
页数:5
相关论文
共 18 条
[11]   Oxidation of Arg-410 promotes the elimination of human serum albumin [J].
Iwao, Yasunori ;
Anraku, Makoto ;
Yamasaki, Keishi ;
Kragh-Hansen, Ulrich ;
Kawai, Keiichi ;
Maruyama, Toru ;
Otagiri, Masaki .
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS, 2006, 1764 (04) :743-749
[12]   Redox-Sensitivity and Site-Specificity of S- and N-Denitrosation in Proteins [J].
Jourd'heuil, Frances L. ;
Lowery, Anthony M. ;
Melton, Elaina M. ;
Mnaimneh, Sanie ;
Bryan, Nathan S. ;
Fernandez, Bernadette O. ;
Park, Joo-Ho ;
Ha, Chung-Eun ;
Bhagavan, Nadhipuram V. ;
Feelisch, Martin ;
Jourd'heuil, David .
PLOS ONE, 2010, 5 (12)
[13]   Methionine residues as endogenous antioxidants in proteins [J].
Levine, RL ;
Mosoni, L ;
Berlett, BS ;
Stadtman, ER .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1996, 93 (26) :15036-15040
[14]   Overexpression of peptide-methionine sulfoxide reductase in Saccharomyces cerevisiae and human T cells provides them with high resistance to oxidative stress [J].
Moskovitz, J ;
Flescher, E ;
Berlett, BS ;
Azare, J ;
Poston, JM ;
Stadtman, ER .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1998, 95 (24) :14071-14075
[15]   Probing the cysteine 34 residue in human serum albumin using fluorescence techniques [J].
Narazaki, R ;
Maruyama, T ;
Otagiri, M .
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY, 1997, 1338 (02) :275-281
[16]   Physiological and pathological changes in the redox state of human serum albumin critically influence its binding properties [J].
Oettl, K. ;
Stauber, R. E. .
BRITISH JOURNAL OF PHARMACOLOGY, 2007, 151 (05) :580-590
[17]  
PHILLIPS A, 1989, LANCET, V2, P1434
[18]   Modification of amino acid residues in human serum albumin by myeloperoxidase [J].
Salavej, P ;
Spalteholz, H ;
Arnhold, J .
FREE RADICAL BIOLOGY AND MEDICINE, 2006, 40 (03) :516-525