PMID: 7539130Dec 1, 1994Paper

O-methylation of L-dopa in melanin metabolism and the presence of catechol-O-methyltransferase in melanocytes

Pigment Cell Research
N P SmitS Pavel

Abstract

O-Methylation of L-dopa was investigated as a possible regulatory mechanism in melanin metabolism. The methylation product of L-dopa, 3-O-methoxytyrosine was detected in extracts of cultured human melanocytes. The enzyme catechol-O-methyltransferase is responsible for this O-methylation and that of the dihydroxyindolic intermediates of melanogenesis. The enzyme is present in melanocytes in its soluble and membrane-bound isoforms. Immuno-electron microscopy suggests the presence of the membrane-bound enzyme in the endoplasmic reticulum. This localization may indicate a role of catechol-O-methyltransferase in protecting the melanocyte against reactive dihydroxyphenolic intermediates of melanogenesis leaking from the melanogenic compartments. On the other hand, the O-methylation of L-dopa may serve as a regulatory point in melanogenesis during early stage of tyrosinase processing in the endoplasmic reticulum.

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Citations

Aug 13, 2011·Pigment Cell & Melanoma Research·Andrzej SlominskiJohn Pawelek
Feb 10, 2007·The Journal of Investigative Dermatology·Matthew S McNeillRobert A Cornell
Aug 30, 2008·International Journal of Cancer. Journal International Du Cancer·Luís Sánchez-del-Campo, José Neptuno Rodríguez-López
May 3, 2012·Photodermatology, Photoimmunology & Photomedicine·Sofia MaginaDaniel Moura
Sep 24, 2004·Physiological Reviews·Andrzej SlominskiJacobo Wortsman
Nov 18, 2005·Journal of Environmental Science and Health. Part C, Environmental Carcinogenesis & Ecotoxicology Reviews·William H Tolleson
Sep 20, 1996·Journal of Chromatography. B, Biomedical Applications·C Tilgmann, I Ulmanen

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