Anemonin is a natural bioactive compound that can regulate tyrosinase-related proteins and mRNA in human melanocytes

Yen Hua Huang, Tzong Huei Lee, Kuei Jung Chan, Feng Lin Hsu, Yu Chih Wu, Mei Hsien Lee

Research output: Contribution to journalArticlepeer-review

33 Citations (Scopus)


Background: Melanin is the pigment responsible for skin color. Melanin synthesis occurs with the participation of the tyrosinase (TYR) family of proteins including TYR, tyrosinase-related protein 1 (TRP1), and tyrosinase-related protein 2 (TRP2/DCT). Objective: The effect of a newly isolated natural compound that inhibits hyperpigmentation on the regulation of the TYR family of proteins was examined. Methods: The natural compound, anemonin, was isolated from Clematis crassifolia Benth and was used to inhibit cellular TYR activity; it was found to have a low cytotoxicity (cell viability > 80%) in human melanocytes. Results: In human melanocytes, anemonin showed both time- and dose-dependent inhibition (IC50 43.5 μM) of TYR. Western blot analysis and immunocytochemical staining revealed that expression of TYR, TRP1, and TRP2 was decreased in anemonin-treated melanocytes. Additionally, reverse transcription and quantitative real-time polymerase chain reaction analyses revealed that expression of mRNAs for MITF, TYR, TYRP1, and TYRP2 was also suppressed by anemonin. Conclusion: The natural compound, anemonin, an active compound of C. crassifolia, inhibits pigmentation synthesis in human melanocytes. Anemonin inhibits melanin synthesis by inhibiting the transcription of the genes encoding MITF, TYR, TRP1, and TRP2. This natural compound may be a candidate for cosmetic use.

Original languageEnglish
Pages (from-to)115-123
Number of pages9
JournalJournal of Dermatological Science
Issue number2
Publication statusPublished - Feb 2008


  • Anemonin
  • Melanocytes
  • Quantitative real-time polymerase chain
  • Tyrosinase
  • Tyrosinase-related proteins

ASJC Scopus subject areas

  • Dermatology


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