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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Thioredoxin reductase induction coincides with melanin biosynthesis in brown and black guinea pigs and in murine melanoma cells.

X-rays were used to induce melanin biosynthesis in brown and black guinea pigs in vivo. During the course of pigmentation, the expression of thioredoxin reductase was increased, whereas for the other antioxidant enzymes, superoxide dismutase (cytosol Cu/Zn-enzyme), catalase, and glutathione reductase, levels and activities decreased. Isobutylmethylxanthine induced eumelanin biosynthesis in murine melanoma cells (Cloudman S-91). In these cells, thioredoxin reductase levels coincided with melanogenesis. Our results suggest that both tyrosinase and thioredoxin reductase respond to oxidative stress in the epidermis as well as in melanoma cells and react with superoxide anion radicals to stimulate melanogenesis and to prevent peroxidative damage, respectively.[1]

References

  1. Thioredoxin reductase induction coincides with melanin biosynthesis in brown and black guinea pigs and in murine melanoma cells. Schallreuter, K.U., Lemke, K.R., Hill, H.Z., Wood, J.M. J. Invest. Dermatol. (1994) [Pubmed]
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