Ablation of the Mammalian Methionine Sulfoxide Reductase A Affects the Expression Level of Cysteine Deoxygenase.
From: University of Kansas, School of Pharmacy, Department of Pharmacology and Toxicology, Lawrence, KS 66045, USA.
Biochemical and biophysical research communications
- Publish Date: Jan 2007
- ISSN: 0006-291X
- Volume: 352
- Issue: 2
- Pages: 556-9
- Medium: Print
- Language: English
- Citation (JAMA): Oien Derek B, Moskovitz Jackob, et al. Ablation of the Mammalian Methionine Sulfoxide Reductase A Affects the Expression Level of Cysteine Deoxygenase.. Biochem. Biophys. Res. Commun. Jan 2007;352:556-9
Abstract
Methionine sulfoxide reductases (Msrs) are able to reduce methionine sulfoxide to methionine both in proteins and free amino acids. By their action it is possible to regulate the function of specific proteins and the cellular antioxidant defense against oxidative damage. Similarly, cysteine deoxygenase (CDO) may be involved in the regulation of protein function and antioxidant defense mechanisms by its ability to oxidized cysteine residues. The two enzymes’ involvement in sulfur amino-acids metabolism seems to be connected. Lack of methionine sulfoxide reductase A (MsrA) in liver of MsrA-/- led to a significant drop in the cellular level of thiol groups and lowered the CDO level of expression. Moreover, following selenium deficient diet (applied to decrease the expression levels of selenoproteins like MsrB), the latter effect was maintained while the basal levels of thiol decreased in both mouse strains. We suggest that both enzymes are working in coordination to balance cellular antioxidant defense.
Mesh Headings (Keywords): Animals, Cysteine Dioxygenase, Gene Expression Regulation, Liver, Mice, Mice, Inbred C57BL, Mice, Knockout, Oxidoreductases
Check for Full Text / PubMed Unique Identifier (PMID): 17126812
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