The redox - biochemistry of human hair pigmentation.
Schallreuter, Karin U. Salem, Mohamed M.A. Hasse, Sybille Rokos, Hartmut
Schallreuter, Karin U.
Salem, Mohamed M.A.
Hasse, Sybille
Rokos, Hartmut
Publication Date
2011-02
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2010-10
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Abstract
The biochemistry of hair pigmentation is a complex field involving a plethora of protein and peptide mechanisms. The in loco factory for melanin formation is the hair follicle melanocyte, but it is common knowledge that melanogenesis results from a fine tuned concerted interaction between the cells of the entire dermal papilla in the anagen hair follicle. The key enzyme is tyrosinase to initiate the active pigmentation machinery. Hence, an intricate understanding from transcription of mRNA to enzyme activity, including enzyme kinetics, substrate supply, optimal pH, cAMP signaling, is a must. Moreover, the role of reactive oxygen species on enzyme regulation and functionality needs to be taken into account. So far our knowledge on the entire hair cycle relies on the murine model of the C57BL/6 mouse. Whether this data can be translated into humans still needs to be shown. This article aims to focus on the effect of H2O2-redox homeostasis on hair follicle pigmentation via tyrosinase, its substrate supply and signal transduction as well as the role of methionine sulfoxide repair via methionine sulfoxide reductases A and B (MSRA and B).
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Schallreuter KU, Salem MAEL, Hasse S and Rokos H. (2011) The redox - biochemistry of human hair pigmentation. Pigment Cell & Melanoma Research, 24(1): 51-62.
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