Protein carbonyl and the methionine sulfoxide reductase system.

Abstract

The formation and accumulation of protein-carbonyl by reactive oxygen species may serve as a marker of oxidative stress, aging, and age-related diseases. Enzymatic reversal of the protein-carbonyl modification has not yet been detected. However, an enzymatic reversal of protein-methionine sulfoxide modification exists and is mediated by the methionine sulfoxide reductase (Msr) system. Methionine sulfoxide modifications to proteins may precede the formation of protein-carbonyl adducts because of consequent structural changes that increase the vulnerability of amino acid residues to carbonylation. Supportive evidence for this possibility arises from the elevated protein-carbonyl accumulations observed in organisms, such as yeast and mice, lacking the methionine sulfoxide reductase A (MsrA) enzyme. In addition, advanced age or enhanced oxidative-stress conditions foster the accumulations of protein-carbonyls. This review discusses the possible involvement of methionine sulfoxide formation in the occurrence of protein-carbonyl adducts and their relevance to the aging process and neurodegenerative diseases.

• Authors: Jackob Moskovitz, Derek B Oien
• Journal: Antioxidants & redox signaling (Antioxid Redox Signal) Vol. 12 Issue 3 Pg. 405-15 (Mar 2010) ISSN: 1557-7716 [Electronic] United States
• PMID: 19686038 (Publication Type: Journal Article, Review)

Chemical References

• Methionine
• Oxidoreductases
• Methionine Sulfoxide Reductases
• methionine sulfoxide reductase
• methionine sulfoxide

Topics

• Aging (genetics, metabolism)
• Animals
• Humans
• Methionine (analogs & derivatives, metabolism)
• Methionine Sulfoxide Reductases
• Mice
• Models, Biological
• Neurodegenerative Diseases (genetics, metabolism)
• Oxidoreductases (genetics, metabolism)
• Protein Carbonylation (genetics, physiology)