Inhibition of melanogenesis by BMY-28565, a novel compound depressing tyrosinase activity in B16 melanoma cells

Terao Mineko, Tomita Koji, Oki Toshikazu, Linda Tabe, Maurizio Gianni, Enrico Garattini

Research output: Contribution to journalArticlepeer-review

Abstract

The mechanism of a novel melanin synthesis inhibitor, BMY-28565, was studied using mouse B16 melanoma cells. This compound was active in depressing the intracellular accumulation of melanin with an IC50 of 5 μM. At dose levels causing no cytotoxicity, the melanolytic effect of this compound was correlated strongly with depression of the enzymatic activity of tyrosinase (monophenol oxygenase, EC 1.14.18.1), the key enzyme in the melanin synthesis pathway. Transcription of the tyrosinase gene was not inhibited by BMY-28565, as determined by RNA blotting analysis. BMY-28565 and three other active derivatives of this compound caused increased glycosylation of proteins in B16 melanoma cells, as assessed by radioactive mannose incorporation. It is, thus, suggested that the mechanism of inhibition of tyrosinase might be related to modifications of the sugar moiety of this enzyme or of a protein(s) that is essential for the expression of its enzymatic activity.

Original languageEnglish
Pages (from-to)183-189
Number of pages7
JournalBiochemical Pharmacology
Volume43
Issue number2
DOIs
Publication statusPublished - Jan 22 1992

ASJC Scopus subject areas

  • Pharmacology

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