S-nitrosylation of mouse galectin-2 prevents oxidative inactivation by hydrogen peroxide
S-nitrosylation of mouse galectin-2 prevents oxidative inactivation by hydrogen peroxide
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小鼠半乳糖凝集素 2 的 S-亚硝基化可防止过氧化氢氧化失活
DOI：
10.1016/j.bbrc.2015.01.055
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发表时间：
2015
期刊：
影响因子：
--
通讯作者：
Arata Y
中科院分区：
文献类型：
--
作者：
Tamura M;Saito M;Yamamoto K;Takeuchi T;Ohtake K;Tateno H;Hirabayashi J;Kobayashi J;Arata Y
半乳糖凝集素是一类对β-半乳糖苷具有特异性的动物凝集素。半乳糖凝集素-2（Gal-2）主要在胃肠道中表达。蛋白质组学分析确定Gal-2作为一种蛋白质，当小鼠胃粘膜裂解物与S-亚硝基谷胱甘肽（一种生理学相关的S-亚硝基化试剂）反应时，Gal-2被S-亚硝基化。在本研究中，使用亚硝基半胱氨酸（CysNO）对重组小鼠（m）Gal-2进行S-亚硝基化，这对蛋白质的糖结合特异性和二聚化能力没有影响。另一方面，H2 O2氧化mGal-2导致糖结合能力的丧失，而S-亚硝基化防止H2 O2诱导的失活，推测是通过保护蛋白质中的Cys残基。这些结果表明，S-亚硝基化的一氧化氮保护Gal-2氧化应激在胃肠道。
Galectins are a group of animal lectins characterized by their specificity for β-galactosides. Galectin-2 (Gal-2) is predominantly expressed in the gastrointestinal tract. A proteomic analysis identified Gal-2 as a protein that was S-nitrosylated when mouse gastric mucosal lysates were reacted with S-nitrosoglutathione, a physiologically relevant S-nitrosylating agent. In the present study, recombinant mouse (m)Gal-2 was S-nitrosylated using nitrosocysteine (CysNO), which had no effect on the sugar-binding specificity and dimerization capacity of the protein. On the other hand, mGal-2 oxidation by H2O2resulted in the loss of sugar-binding ability, while S-nitrosylation prevented H2O2-inducted inactivation, presumably by protecting the Cys residue(s) in the protein. These results suggest that S-nitrosylation by nitric oxides protect Gal-2 from oxidative stress in the gastrointestinal tract.