S-nitrosylation of mouse galectin-2 prevents oxidative inactivation by hydrogen peroxide

• Published in: Biochemical and biophysical research communications Vol. 457; no. 4; pp. 712 - 717
• Main Authors: Tamura, Mayumi, Saito, Masanori, Yamamoto, Kaori, Takeuchi, Tomoharu, Ohtake, Kazuo, Tateno, Hiroaki, Hirabayashi, Jun, Kobayashi, Jun, Arata, Yoichiro
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 20.02.2015
• Subjects: Animals; Cysteine - analogs & derivatives; Cysteine - metabolism; dimerization; Galectin; Galectin 2 - chemistry; Galectin 2 - metabolism; Galectin-2; gastrointestinal system; hydrogen peroxide; Hydrogen Peroxide - metabolism; Lactose - metabolism; lectins; Mice; Nitric Oxide - metabolism; Oxidation; Oxidation-Reduction; Oxidative Stress; Protein Multimerization; proteomics; Recombinant Proteins - chemistry; Recombinant Proteins - metabolism; S-Nitrosothiols - metabolism; S-nitrosylation; Galectin; Galectin-2; Oxidation; S-nitrosylation
• ISSN: 0006-291X; 1090-2104; 1090-2104
• DOI: 10.1016/j.bbrc.2015.01.055

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. •Recombinant mouse galectin-2 (mGal-2) is S-nitrosylated by CysNO treatment.•Both Cys residues (Cys57 and Cys75) of mGal-2 are S-nitrosylated.•mGal-2 sugar-binding and dimerization capacity are unaffected by S-nitrosylation.•H2O2 oxidation induces the loss of mGal-2 lectin activity.•S-nitrosylation of mGal-2 blocks H2O2 oxidation-induced loss of activity.