Glycine hydroxamate inhibits tyrosinase activity and melanin contents through downregulating cAMP/PKA signaling pathways

Yin Shiou Lin, Wen Chung Wu, Shyr Yi Lin, Wen Chi Hou

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

Among the eight amino acid hydroxamates tested, Glycine hydroxamate (GH) was the best inhibitor of mushroom tyrosinase (TYR). With l-tyrosine as substrate, the GH inhibition of the monophenolase activity of the mushroom TYR was noncompetitive. GH decreased not only TYR protein expression, but also melanin content, tyrosinase-related protein (TRP)-1, TRP-2, and microphthalmia-associated transcription factor (MITF) expression in B16F10 melanoma cells while in the presence of α-melanocyte-stimulating hormone (α-MSH). GH also significantly decreased the isobutylmethylxanthine (IBMX)-induced increase in melanin content, which was not prevented by the ERK inhibitor PD98059. These results suggest GH has the potential for use in cosmetic hypopigmentation.

Original languageEnglish
Pages (from-to)617-625
Number of pages9
JournalAmino Acids
Volume47
Issue number3
DOIs
Publication statusPublished - 2015

Fingerprint

Monophenol Monooxygenase
Melanins
Glycine
Down-Regulation
Agaricales
Microphthalmia-Associated Transcription Factor
Hypopigmentation
Melanocyte-Stimulating Hormones
Cosmetics
Tyrosine
Melanoma
Amino Acids
Substrates
Proteins

Keywords

  • Glycine hydroxamate
  • Hypopigmentation
  • Isobutylmethylxanthine
  • Melanin, microphthalmia-associated transcription factor
  • Protein kinase A
  • Tyrosinase

ASJC Scopus subject areas

  • Biochemistry
  • Clinical Biochemistry
  • Organic Chemistry

Cite this

Glycine hydroxamate inhibits tyrosinase activity and melanin contents through downregulating cAMP/PKA signaling pathways. / Lin, Yin Shiou; Wu, Wen Chung; Lin, Shyr Yi; Hou, Wen Chi.

In: Amino Acids, Vol. 47, No. 3, 2015, p. 617-625.

Research output: Contribution to journalArticle

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