Skip to main content

Lund University Publications

LUND UNIVERSITY LIBRARIES

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

Smit, N. ; Tilgmann, C. LU orcid ; Karhunen, T. ; Slingerland, R. ; Ulmanen, I. ; Westerhof, W. and Pavel, S. (1994) In Pigment Cell Research 7(6). p.403-408
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... (More)

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.

(Less)
Please use this url to cite or link to this publication:
author
; ; ; ; ; and
publishing date
type
Contribution to journal
publication status
published
in
Pigment Cell Research
volume
7
issue
6
pages
6 pages
publisher
Wiley-Blackwell
external identifiers
  • scopus:0028724964
  • pmid:7539130
ISSN
0893-5785
language
English
LU publication?
no
id
a79be7c8-057f-426c-a7e2-1b9a675898cc
date added to LUP
2016-04-11 13:21:46
date last changed
2025-10-14 12:28:32
@article{a79be7c8-057f-426c-a7e2-1b9a675898cc,
  abstract     = {{<p>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.</p>}},
  author       = {{Smit, N. and Tilgmann, C. and Karhunen, T. and Slingerland, R. and Ulmanen, I. and Westerhof, W. and Pavel, S.}},
  issn         = {{0893-5785}},
  language     = {{eng}},
  number       = {{6}},
  pages        = {{403--408}},
  publisher    = {{Wiley-Blackwell}},
  series       = {{Pigment Cell Research}},
  title        = {{O-methylation of L-dopa in melanin metabolism and the presence of catechol-O-methyltransferase in melanocytes.}},
  volume       = {{7}},
  year         = {{1994}},
}