Nitrite attenuated hypochlorous acid-mediated heme degradation in hemoglobin

被引:3
作者
Lu, Naihao [1 ,2 ]
Li, Jiayu [1 ,2 ]
Ren, Xiaoming [3 ]
Tian, Rong [1 ,2 ]
Peng, Yi-Yuan [1 ,2 ]
机构
[1] Jiangxi Normal Univ, Key Lab Green Chem, Minist Educ, Key Lab Funct Small Organ Mol, Nanchang, Peoples R China
[2] Jiangxi Normal Univ, Coll Chem & Chem Engn, Nanchang, Peoples R China
[3] Hubei Univ, Fac Mat Sci & Engn, Hubei Collaborat Innovat Ctr Adv Organ Chem Mat, Wuhan, Peoples R China
基金
中国国家自然科学基金;
关键词
Free iron; Hemoglobin; Hypochlorous acid; Nitrite; Myeloperoxidase; Inflammation; FREE IRON RELEASE; OXIDATIVE STRESS; TYROSINE NITRATION; FERRYL HEMOGLOBIN; BLOOD SUBSTITUTES; REDOX REACTIONS; IN-VITRO; MECHANISM; MYELOPEROXIDASE; DESTRUCTION;
D O I
10.1016/j.cbi.2015.05.021
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
Hypochlorous acid (HOCl) is elevated in many inflammatory diseases and causes the accumulation of free iron. Through the Fenton reaction, free iron has the ability to generate free radicals and subsequently is toxic. Recent studies have demonstrated that HOCl participates in heme destruction of hemoglobin (Hb) and free iron release. In this study, it was showed that nitrite (NO2-) could prevent HOCl-mediated Hb heme destruction and free iron release. Also, NO prevented HOC-mediated loss of Hb peroxidase activity. After the NO2-/HOCl treatment, Tyr 42 in alpha-chain was found to be nitrated in Hb, attenuating the electron transferring abilities of phenolic compounds. The protective effects of NO2- on HOCl-induced heme destruction were attributed to its reduction of ferryl Hb and/or direct scavenging of HOCl. Therefore, NO could show protective effects in some inflammatory diseases by preventing HOCl-mediated heme destruction of hemoproteins and free iron release. (C) 2015 Elsevier Ireland Ltd. All rights reserved.
引用
收藏
页码:25 / 32
页数:8
相关论文
共 40 条
[1]   Redox reactions of hemoglobin and myoglobin: Biological and toxicological implications [J].
Alayash, AI ;
Patel, RP ;
Cashon, RE .
ANTIOXIDANTS & REDOX SIGNALING, 2001, 3 (02) :313-327
[2]   Hemoglobin-based blood substitutes: oxygen carriers, pressor agents, or oxidants? [J].
Alayash, AI .
NATURE BIOTECHNOLOGY, 1999, 17 (06) :545-549
[3]   Structural analysis of fish versus mammalian hemoglobins: Effect of the heme pocket environment on autooxidation and hemin loss [J].
Aranda, Roman ;
Cai, He ;
Worley, Chad E. ;
Levin, Elena J. ;
Li, Rong ;
Olson, John S. ;
Phillips, George N., Jr. ;
Richards, Mark P. .
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS, 2009, 75 (01) :217-230
[4]   Human myeloperoxidase in innate and acquired immunity [J].
Arnhold, Juergen ;
Flemmig, Joerg .
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 2010, 500 (01) :92-106
[5]   Hemoglobin as a source of iron overload in multiple sclerosis: does multiple sclerosis share risk factors with vascular disorders? [J].
Bamm, Vladimir V. ;
Harauz, George .
CELLULAR AND MOLECULAR LIFE SCIENCES, 2014, 71 (10) :1789-1798
[6]   Protein oxidation in aging, disease, and oxidative stress [J].
Berlett, BS ;
Stadtman, ER .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1997, 272 (33) :20313-20316
[7]   Dietary nitrite supplementation protects against myocardial ischemia-reperfusion injury [J].
Bryan, Nathan S. ;
Calvert, John W. ;
Elrod, John W. ;
Gundewar, Susheel ;
Ji, Sang Yong ;
Lefer, David J. .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2007, 104 (48) :19144-19149
[8]   Mechanism of reaction of myeloperoxidase with nitrite [J].
Burner, U ;
Furtmüller, PG ;
Kettle, AJ ;
Koppenol, WH ;
Obinger, C .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2000, 275 (27) :20597-20601
[9]   H2O2/nitrite-induced post-translational modifications of human hemoglobin determined by mass spectrometry:: Redox regulation of tyrosine nitration and 3-nitrotyrosine reduction by antioxidants [J].
Chen, Hauh-Jyun Candy ;
Chang, Chia-Ming ;
Lin, Wen-Peng ;
Cheng, Dar-Long ;
Leong, Mei-I .
CHEMBIOCHEM, 2008, 9 (02) :312-323
[10]   Protein carbonyl groups as biomarkers of oxidative stress [J].
Dalle-Donne, I ;
Rossi, R ;
Giustarini, D ;
Milzani, A ;
Colombo, R .
CLINICA CHIMICA ACTA, 2003, 329 (1-2) :23-38