Detection of kynurenine modifications in proteins using a monoclonal antibody

被引:17
作者
Staniszewska, Magdalena
Nagaraj, Ram H. [1 ]
机构
[1] Dept Ophthalmol, Cleveland, OH 44106 USA
[2] Case Western Reserve Univ, Cleveland, OH 44106 USA
基金
美国国家卫生研究院;
关键词
monoclonal antibody; indoleamine 2,3-dioxygenase; kynurenine; N-formylkynurenine; protein modifications; tryptophan oxidation;
D O I
10.1016/j.jim.2007.05.002
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
N-formylkynurenine and kynurenine are oxidation products of tryptophan formed from the reaction catalyzed by indoleamine 2,3-dioxygenase. These kynurenines react with proteins to produce chemical modifications in the lens. We developed a novel monoclonal antibody that detects a kynurenine modification in proteins. The antibody recognized proteins (human lens proteins, RNase A and BSA) that were modified by either kynurenine or N-formylkynurenine. The antibody also reacted strongly with N-formylkynurenine-modified N-alpha-acetyl histidine and weakly with N-formylkynurenine-modified N-alpha-acetyl lysine, N-alpha-acetyl cysteine and N-alpha-acetyl arginine. The antibody recognized kynurenine and N-fonnylkynurenine but not other tryptophan oxidation products. We isolated and purified a major antigen from the reaction mixture of N-alpha-acetyl histidine and N-fonnylkynurenine and identified the product as N-acetyl-1-[3-(2-aminophenyl)-1-carboxy-3-oxopropyl]-histidine. We then used our purified antibody to detect kynurenine modifications in kynurenine-treated human lens epithelial cells and human lens. We found epithelial immunoreactivity in a lens from an aged donor but not in one from a very young donor. This would suggest that the antibody detects age-related changes in lens proteins altered by kynurenines. We believe that our antibody could be used to establish the importance of kynurenine modifications in diseases where tryptophan oxidation is enhanced. (C) 2007 Published by Elsevier B.V.
引用
收藏
页码:63 / 73
页数:11
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