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Dipeptides Inhibit Melanin Synthesis in Mel-Ab Cells through Down-Regulation of Tyrosinase

  • Lee, Hyun-E (Department of Biochemistry, Chung-Ang University College of Medicine) ;
  • Kim, Eun-Hyun (Department of Biochemistry, Chung-Ang University College of Medicine) ;
  • Choi, Hye-Ryung (Department of Dermatology, Seoul National University College of Medicine) ;
  • Sohn, Uy-Dong (Department of Pharmacology, College of Pharmacy, Chung-Ang University) ;
  • Yun, Hye-Young (Department of Biochemistry, Chung-Ang University College of Medicine) ;
  • Baek, Kwang-Jin (Department of Biochemistry, Chung-Ang University College of Medicine) ;
  • Kwon, Nyoun-Soo (Department of Biochemistry, Chung-Ang University College of Medicine) ;
  • Park, Kyoung-Chan (Department of Dermatology, Seoul National University College of Medicine) ;
  • Kim, Dong-Seok (Department of Biochemistry, Chung-Ang University College of Medicine)
  • Received : 2012.05.31
  • Accepted : 2012.07.19
  • Published : 2012.08.30

Abstract

This study investigated the effects of proline-serine (PS) and valine-serine (VS) dipeptides on melanogenesis in Mel-Ab cells. Proline-serine and VS significantly inhibited melanin synthesis in a concentration-dependent manner, though neither dipeptide directly inhibited tyrosinase activity in a cell-free system. Both PS and VS down-regulated the expression of microphthalmia-associated transcription factor (MITF) and tyrosinase. In a follow-up study also described here, the effects of these dipeptides on melanogenesis-related signal transduction were quantified. Specifically, PS and VS induced ERK phosphorylation, though they had no effect on phosphorylation of the cAMP response element binding protein (CREB). These data suggest that PS and VS inhibit melanogenesis through ERK phosphorylation and subsequent down-regulation of MITF and tyrosinase. Properties of these dipeptides are compatible with application as skin-whitening agents.

Keywords

References

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