Functioning methionine sulfoxide reductases A and B are present in human epidermal melanocytes in the cytosol and in the nucleus.
Article Details
- CitationCopy to clipboard
Schallreuter KU, Rubsam K, Chavan B, Zothner C, Gillbro JM, Spencer JD, Wood JM
Functioning methionine sulfoxide reductases A and B are present in human epidermal melanocytes in the cytosol and in the nucleus.
Biochem Biophys Res Commun. 2006 Mar 31;342(1):145-52. Epub 2006 Feb 3.
- PubMed ID
- 16480945 [ View in PubMed]
- Abstract
Oxidation of methionine residues by reactive oxygen (ROS) in protein structures leads to the formation of methionine sulfoxide which can consequently lead to a plethora of impaired functionality. The generation of methionine sulfoxide yields ultimately a diastereomeric mixture of the S and R sulfoxides. So far two distinct enzyme families have been identified. MSRA reduces methionine S-sulfoxide, while MSRB reduces the R-diastereomer. It has been shown that these enzymes are involved in regulation of protein function and in elimination of ROS via reversible methionine formation besides protein repair. Importantly, both enzymes require coupling to the NADPH/thioredoxin reductase/thioredoxin electron donor system. In this report, we show for the first time the expression and function of both sulfoxide reductases together with thioredoxin reductase in the cytosol as well as in the nucleus of epidermal melanocytes which are especially sensitive to ROS. Since this cell resides in the basal layer of the epidermis and its numbers and functions are reduced upon ageing and for instance also in depigmentation processes, we believe that this discovery adds an intricate repair mechanism to melanocyte homeostasis and survival.
DrugBank Data that Cites this Article
- Drug Enzymes
Drug Enzyme Kind Organism Pharmacological Action Actions Methionine Methionine-R-sulfoxide reductase B2, mitochondrial Protein Humans UnknownSubstrateDetails Methionine Mitochondrial peptide methionine sulfoxide reductase Protein Humans UnknownSubstrateDetails