1. S-nitrosylation of mouse galectin-2 prevents oxidative inactivation by hydrogen peroxide.
- Author
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Tamura M, Saito M, Yamamoto K, Takeuchi T, Ohtake K, Tateno H, Hirabayashi J, Kobayashi J, and Arata Y
- Subjects
- Animals, Cysteine metabolism, Galectin 2 chemistry, Lactose metabolism, Mice, Nitric Oxide metabolism, Oxidation-Reduction, Oxidative Stress, Protein Multimerization, Recombinant Proteins chemistry, Recombinant Proteins metabolism, Cysteine analogs & derivatives, Galectin 2 metabolism, Hydrogen Peroxide metabolism, S-Nitrosothiols metabolism
- Abstract
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 H2O2 resulted 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., (Copyright © 2015 Elsevier Inc. All rights reserved.)
- Published
- 2015
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