Kynurenine binds to the peptide binding region of the chaperone αB-crystallin
Kynurenine binds to the peptide binding region of the chaperone αB-crystallin
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DOI：
10.1006/bbrc.2001.5288
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发表时间：
2001-08-03
影响因子：
3.1
通讯作者：
Truscott, RJW
中科院分区：
文献类型：
--
作者：
Aquilina, JA;Truscott, RJW
紫外线过滤剂，如犬尿氨酸，存在于人类透镜中。它们在中性pH下自发不稳定，脱氨基形成反应性α，β不饱和酮。这个过程变得更加突出后，透镜障碍发展到中年。在这里，我们表明，脱氨基犬尿氨酸反应主要与组氨酸残基的α B-晶状体蛋白：一个主要的透镜蛋白，缺乏半胱氨酸。发现α B-晶体蛋白中的九个组氨酸中的五个与犬尿氨酸缀合。此外，共价修饰的主要位点在组氨酸83处，其在α B-晶状体蛋白的推定肽结合区中发现;该位点对于其作为伴侣蛋白的作用至关重要。我们建议，修改α B-晶状体蛋白的紫外线过滤器可能会损害这种蛋白质的伴侣作用。(C)北京：科学出版社.
UV filters, such as kynurenine, are present in the human lens. They are spontaneously unstable at neutral pH and deaminate to form reactive alpha, beta unsaturated ketones. This process becomes more prominent after the lens barrier develops in middle age. Here we show that deaminated kynurenine reacts primarily with histidine residues in alphaB-crystallin: a major lens protein that lacks cysteine. Five of the nine histidines in alphaB-crystallin were found to be conjugated with kynurenine. Furthermore, a major site of covalent modification was at histidine 83, which is found in the putative peptide binding region of alphaB-crystallin; a site crucial for its role as a chaperone. We propose that modification of alphaB-crystallin by UV filters may compromise the chaperone action of this protein. (C) 2001 Academic Press.