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J Biol Chem, Vol. 273, Issue 16, 9966-9970, April 17, 1998
From INSERM U-385, Faculté de médecine, Avenue de
Valombrose, 06107 Nice Cedex 2, France, and In B16 melanoma cells, mitogen-activated protein
(MAP) kinases are activated during cAMP-induced melanogenesis (Englaro,
W., Rezzonico, R., Durand-Clément, M., Lallemand, D., Ortonne,
J. P., and Ballotti, R. (1995) J. Biol. Chem.
270, 24315-24320). To establish the role of the MAP kinases in
melanogenesis, we studied the effects of a specific MAP kinase kinase
(MEK) inhibitor PD 98059 on different melanogenic parameters. We showed
that PD 98059 inhibits the activation of MAP kinase extracellular
signal-regulated kinase 1 by cAMP, but does not impair the effects of
cAMP either on the morphological differentiation, characterized by an
increase in dendrite outgrowth, or on the up-regulation of tyrosinase
that is the key enzyme in melanogenesis. On the contrary, PD 98059 promotes by itself cell dendricity and increases the tyrosinase amount
and activity. Moreover, down-regulation of the MAP kinase pathway by PD
98059, or with dominant negative mutants of p21ras and MEK,
triggers a stimulation of the tyrosinase promoter activity and enhances
the effect of cAMP on this parameter. Conversely, activation of the MAP
kinase pathway, using constitutive active mutants of p21ras and
MEK, leads to an inhibition of basal and cAMP-induced tyrosinase gene
transcription. These results demonstrate that the MAP kinase pathway
activation is not required for cAMP-induced melanogenesis. Furthermore,
the inhibition of this pathway induces B16 melanoma cell
differentiation, while a sustained activation impairs the melanogenic
effect of cAMP-elevating agents.
Inhibition of the Mitogen-activated Protein Kinase Pathway
Triggers B16 Melanoma Cell Differentiation
,, Centre de
Biochimie, CNRS-UMR 134, Faculté des Sciences, 06018 Nice, France
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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