Back to Search
Start Over
Identification of the cysteine residue responsible for oxidative inactivation of mouse galectin-2.
- Source :
-
Journal of biochemistry [J Biochem] 2016 Oct; Vol. 160 (4), pp. 233-241. Date of Electronic Publication: 2016 Apr 27. - Publication Year :
- 2016
-
Abstract
- Galectins are a group of animal lectins characterized by their specificity for β-galactosides. Mouse galectin-2 (mGal-2) is predominantly expressed in the gastrointestinal tract and has been identified as one of the main gastric mucosal proteins that are uniquely sensitive to S-nitrosylation. We have previously reported that oxidation of mGal-2 by hydrogen peroxide (H <subscript>2</subscript> O <subscript>2</subscript> ) resulted in the loss of sugar-binding ability, whereas pre-treatment of mGal-2 with S-nitrosocysteine prevented H <subscript>2</subscript> O <subscript>2</subscript> -induced inactivation. In this study, we used point-mutated recombinant mGal-2 proteins to study which of the two highly conserved Cys residues in mGal-2 must be S-nitrosylated for protection against oxidative inactivation. Mutation of Cys <superscript>57</superscript> to a Met residue (C57M) did not result in lectin inactivation following H <subscript>2</subscript> O <subscript>2</subscript> treatment, whereas Cys <superscript>75</superscript> mutation to Ser (C75S) led to significantly reduced lectin activity, as is the case for wild-type mGal-2. However, pre-treatment of the C75S mutant with S-nitrosocysteine protected the protein from H <subscript>2</subscript> O <subscript>2</subscript> -induced inactivation. Therefore, Cys <superscript>57</superscript> is suggested to be responsible for oxidative inactivation of the mGal-2 protein, and protection of the sulfhydryl group of the Cys <superscript>57</superscript> in mGal-2 by S-nitrosylation is likely important for maintaining mGal-2 protein function in an oxidative environment such as the gastrointestinal tract.<br /> (© The Authors 2016. Published by Oxford University Press on behalf of the Japanese Biochemical Society. All rights reserved.)
Details
- Language :
- English
- ISSN :
- 1756-2651
- Volume :
- 160
- Issue :
- 4
- Database :
- MEDLINE
- Journal :
- Journal of biochemistry
- Publication Type :
- Academic Journal
- Accession number :
- 27122052
- Full Text :
- https://doi.org/10.1093/jb/mvw029