The lactoferricin B-derived peptide, LfB17-34, induces melanogenesis in B16F10 cells

• Published in: International journal of molecular medicine 2017-03, Vol.39 (3), p.595-602
• Main Authors: Huang, Hsiu-Chin, Lin, Hsuan, Huang, Min-Chuan
• Format: Article
• Language: English
• Subjects: Care and treatment; Cellular proteins; Development and progression; Enzymes; Gene expression; Genetic aspects; Health aspects; Kinases; Lactoferrins; Mammals; Melanoma; Peptides; Phosphorylation; Pigmentation disorders; Proteins; Studies; Vitiligo
• ISSN: 1107-3756; 1791-244X
• DOI: 10.3892/ijmm.2017.2884

Lactoferricin B (LfcinB), a peptide of bovine lactoferrin (LfB), exhibits multiple biological functions, including antimicrobial, antiviral, antioxidant and immuno-modulatory activities. However, the role of LfcinB-related peptides in melanogenesis remains unclear. In this study, a set of five LfcinB-related peptides was examined. We found that LfB17-34, an 18-mer LfcinB-derived peptide, increased melanogenesis in B16F10 melanoma cells without significantly affecting cell viability. LfB17-34 increased in vitro tyrosinase activity and melanin content in a dose-dependent manner. The results of RT-qPCR and western blot analyses showed that LfB17-34 increased the mRNA and protein expression of tyrosinase and tyrosinase-related protein 1 (Trp1). Moreover, LfB17-34 inhibited the phosphorylation of MAPK/Erk, but not p38 and Akt, and constitutively active MEK was able to reverse the LfB17-34-enhanced pigmentation, melanin content, and tyrosinase activity, suggesting a role of Erk signaling in the process of LfB17-34-mediated pigmentation. Taken together, these results suggest that LfB17-34 induces melanogenesis in B16F10 cells primarily through increased tyrosinase expression and activity and that LfB17-34 could be further developed for the treatment of hypopigmentation disorders.