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D‐tyrosine negatively regulates melanin synthesis by competitively inhibiting tyrosinase activity
Author(s) -
Park Jisu,
Jung Hyejung,
Kim Kyuri,
Lim KyungMin,
Kim Jiyoung,
Jho Eekhoon,
Oh EokSoo
Publication year - 2018
Publication title -
pigment cell and melanoma research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.618
H-Index - 105
eISSN - 1755-148X
pISSN - 1755-1471
DOI - 10.1111/pcmr.12668
Subject(s) - melanin , tyrosinase , tyrosine , melanocyte , biochemistry , chemistry , melanosome , in vitro , tyrosine phosphorylation , tyrosine kinase , receptor tyrosine kinase , biology , melanoma , phosphorylation , cancer research , signal transduction , enzyme
Summary Although L‐tyrosine is well known for its melanogenic effect, the contribution of D‐tyrosine to melanin synthesis was previously unexplored. Here, we reveal that, unlike L‐tyrosine, D‐tyrosine dose‐dependently reduced the melanin contents of human MNT ‐1 melanoma cells and primary human melanocytes. In addition, 500 μM of D‐tyrosine completely inhibited 10 μM L‐tyrosine‐induced melanogenesis, and both in vitro assays and L‐ DOPA staining MNT ‐1 cells showed that tyrosinase activity is reduced by D‐tyrosine treatment. Thus, D‐tyrosine appears to inhibit L‐tyrosine‐mediated melanogenesis by competitively inhibiting tyrosinase activity. Furthermore, we found that D‐tyrosine inhibited melanogenesis induced by α‐ MSH treatment or UV irradiation, which are the most common environmental factors responsible for melanin synthesis. Finally, we confirmed that D‐tyrosine reduced melanin synthesis in the epidermal basal layer of a 3D human skin model. Taken together, these data suggest that D‐tyrosine negatively regulates melanin synthesis by inhibiting tyrosinase activity in melanocyte‐derived cells.