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Title: Functioning methionine sulfoxide reductases A and B are present in human epidermal melanocytes in the cytosol and in the nucleus

Journal Article · · Biochemical and Biophysical Research Communications
 [1];  [2];  [2];  [2];  [2];  [2];  [3]
  1. Clinical and Experimental Dermatology/Department of Biomedical Sciences, University of Bradford (United Kingdom) and Institute for Pigmentary Disorders in Association with EM, Arndt University, Greifswald, Germany and University of Bradford (United Kingdom)
  2. Clinical and Experimental Dermatology/Department of Biomedical Sciences, University of Bradford (United Kingdom)
  3. Institute for Pigmentary Disorders in Association with EM, Arndt University, Greifswald (Germany) and University of Bradford (United Kingdom)

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 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.

OSTI ID:
20798869
Journal Information:
Biochemical and Biophysical Research Communications, Vol. 342, Issue 1; Other Information: DOI: 10.1016/j.bbrc.2006.01.124; PII: S0006-291X(06)00201-4; Copyright (c) 2006 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA); ISSN 0006-291X
Country of Publication:
United States
Language:
English