Inhibition of human surfactant protein a function by oxidation intermediates of nitrite

被引:32
作者
Davis, IC
Zhu, S
Sampson, JB
Crow, JP
Matalon, S
机构
[1] Univ Alabama, Dept Anesthesiol, Birmingham, AL 35205 USA
[2] Univ Alabama, Dept Pharmacol & Toxicol, Birmingham, AL 35205 USA
[3] Univ Alabama, Dept Physiol & Biophys, Birmingham, AL 35205 USA
关键词
nitric oxide; surfactant protein A; myeloperoxidase; nitration; oxidation; free radicals;
D O I
10.1016/S0891-5849(02)01170-X
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
Nitration of protein tyrosine residues by peroxynitrite (ONOO-) has been implicated in a variety of inflammatory diseases such as acute respiratory distress syndrome (ARDS). Pulmonary surfactant protein A (SP-A) has multiple functions including host defense. We report here that a mixture of hypochlorous acid (HOCl) and nitrite (NO2-) induces nitration, oxidation, and chlorination of tyrosine residues in human SP-A and inhibits SP-A's ability to aggregate lipids and bind mannose. Nitration and oxidation of SP-A was not altered by the presence of lipids, suggesting that proteins are preferred targets in lipid-rich mixtures such as pulmonary surfactant. Moreover, both horseradish peroxidase and myeloperoxidase (MPO) can utilize NO2- and hydrogen peroxide (H2O2) as substrates to catalyze tyrosine nitration in SP-A and inhibit its lipid aggregation function. SP-A nitration and oxidation by MPO is markedly enhanced in the presence of physiological concentrations of Cl- and the lipid aggregation function of SP-A is completely abolished. Collectively, our results suggest that MPO released by activated neutrophils during inflammation utilizes physiological or pathological levels of NO2- to nitrate proteins, and may provide an additional mechanism in addition to ONOO- formation, for tissue injury in ARDS and other inflammatory diseases associated with upregulated (NO)-N-. and oxidant production. (C) 2002 Elsevier Science Inc.
引用
收藏
页码:1703 / 1713
页数:11
相关论文
共 45 条
[1]  
AMADO R, 1984, METHOD ENZYMOL, V107, P377
[2]   FLUOROMETRIC ASSAY OF PROTEINS IN NANOGRAM RANGE [J].
BOHLEN, P ;
STEIN, S ;
DAIRMAN, W ;
UDENFRIEND, S .
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 1973, 155 (01) :213-220
[3]   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].
Brennan, ML ;
Wu, WJ ;
Fu, XM ;
Shen, ZZ ;
Song, W ;
Frost, H ;
Vadseth, C ;
Narine, L ;
Lenkiewicz, E ;
Borchers, MT ;
Lusis, AJ ;
Lee, JJ ;
Lee, NA ;
Abu-Soud, HM ;
Ischiropoulos, H ;
Hazen, SL .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2002, 277 (20) :17415-17427
[4]   Chlorination of bacterial and neutrophil proteins during phagocytosis and killing of Staphylococcus aureus [J].
Chapman, ALP ;
Hampton, MB ;
Senthilmohan, R ;
Winterbourn, CC ;
Kettle, AJ .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2002, 277 (12) :9757-9762
[5]   Collectins and pulmonary host defense [J].
Crouch, EC .
AMERICAN JOURNAL OF RESPIRATORY CELL AND MOLECULAR BIOLOGY, 1998, 19 (02) :177-201
[6]  
Crowder RA, 1999, ENVIRON ST, V3, P151
[7]  
Dean RT, 1997, BIOCHEM J, V324, P1
[8]  
den Hartog GJM, 2002, BIOL CHEM, V383, P709
[9]  
DRICKAMER K, 1988, J BIOL CHEM, V263, P9557
[10]   Formation of nitric oxide derived inflammatory oxidants by myeloperoxidase in neutrophils [J].
Eiserich, JP ;
Hristova, M ;
Cross, CE ;
Jones, AD ;
Freeman, BA ;
Halliwell, B ;
van der Vliet, A .
NATURE, 1998, 391 (6665) :393-397