Journal
AMINO ACIDS
Volume 43, Issue 2, Pages 505-517Publisher
SPRINGER WIEN
DOI: 10.1007/s00726-011-1175-9
Keywords
Protein methionine oxidation; Methionine sulfoxide; Calcium/calmodulin-dependent protein kinase II; BK potassium channel; Protein fibrillation; Neurodegenerative diseases; Singlet oxygen
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Funding
- MOST China 973 Program [2011CB809101]
- NSFC [30728020, 30870580, 30970675]
- NSFBJ [5102020]
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The sulfur-containing amino acid residue methionine (Met) in a peptide/protein is readily oxidized to methionine sulfoxide [Met(O)] by reactive oxygen species both in vitro and in vivo. Methionine residue oxidation by oxidants is found in an accumulating number of important proteins. Met sulfoxidation activates calcium/calmodulin-dependent protein kinase II and the large conductance calcium-activated potassium channels, delays inactivation of the Shaker potassium channel ShC/B and L-type voltage-dependent calcium channels. Sulfoxidation at critical Met residues inhibits fibrillation of atherosclerosis-related apolipoproteins and multiple neurodegenerative disease-related proteins, such as amyloid beta, alpha-synuclein, prion, and others. Methionine residue oxidation is also correlated with marked changes in cellular activities. Controlled key methionine residue oxidation may be used as an oxi-genetics tool to dissect specific protein function in situ.
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