Plumbagin Suppresses α-MSH-Induced Melanogenesis in B16F10 Mouse Melanoma Cells by Inhibiting Tyrosinase Activity
Recent studies have shown that plumbagin has anti-inflammatory, anti-allergic, antibacterial, and anti-cancer activities; however, it has not yet been shown whether plumbagin suppresses alpha-melanocyte stimulating hormone (α-MSH)-induced melanin synthesis to prevent hyperpigmentation. In this study...
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doaj-550154dc212f4d2f8e685bff61fe37702020-11-25T00:49:05ZengMDPI AGInternational Journal of Molecular Sciences1422-00672017-02-0118232010.3390/ijms18020320ijms18020320Plumbagin Suppresses α-MSH-Induced Melanogenesis in B16F10 Mouse Melanoma Cells by Inhibiting Tyrosinase ActivityTaek-In Oh0Jeong-Mi Yun1Eun-Ji Park2Young-Seon Kim3Yoon-Mi Lee4Ji-Hong Lim5Department of Biomedical Chemistry, College of Biomedical and Health Science, Konkuk University, Chungju 380-701, KoreaDepartment of Biomedical Chemistry, College of Biomedical and Health Science, Konkuk University, Chungju 380-701, KoreaDepartment of Biomedical Chemistry, College of Biomedical and Health Science, Konkuk University, Chungju 380-701, KoreaDepartment of Biomedical Chemistry, College of Biomedical and Health Science, Konkuk University, Chungju 380-701, KoreaInterdisciplinary Research Center for Health, Konkuk University, Chungju 380-701, KoreaDepartment of Biomedical Chemistry, College of Biomedical and Health Science, Konkuk University, Chungju 380-701, KoreaRecent studies have shown that plumbagin has anti-inflammatory, anti-allergic, antibacterial, and anti-cancer activities; however, it has not yet been shown whether plumbagin suppresses alpha-melanocyte stimulating hormone (α-MSH)-induced melanin synthesis to prevent hyperpigmentation. In this study, we demonstrated that plumbagin significantly suppresses α-MSH-stimulated melanin synthesis in B16F10 mouse melanoma cells. To understand the inhibitory mechanism of plumbagin on melanin synthesis, we performed cellular or cell-free tyrosinase activity assays and analyzed melanogenesis-related gene expression. We demonstrated that plumbagin directly suppresses tyrosinase activity independent of the transcriptional machinery associated with melanogenesis, which includes micropthalmia-associated transcription factor (MITF), tyrosinase (TYR), and tyrosinase-related protein 1 (TYRP1). We also investigated whether plumbagin was toxic to normal human keratinocytes (HaCaT) and lens epithelial cells (B3) that may be injured by using skin-care cosmetics. Surprisingly, lower plumbagin concentrations (0.5–1 μM) effectively inhibited melanin synthesis and tyrosinase activity but do not cause toxicity in keratinocytes, lens epithelial cells, and B16F10 mouse melanoma cells, suggesting that plumbagin is safe for dermal application. Taken together, these results suggest that the inhibitory effect of plumbagin to pigmentation may make it an acceptable and safe component for use in skin-care cosmetic formulations used for skin whitening.http://www.mdpi.com/1422-0067/18/2/320plumbaginmelanogenesispigmentationtyrosinase |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Taek-In Oh Jeong-Mi Yun Eun-Ji Park Young-Seon Kim Yoon-Mi Lee Ji-Hong Lim |
spellingShingle |
Taek-In Oh Jeong-Mi Yun Eun-Ji Park Young-Seon Kim Yoon-Mi Lee Ji-Hong Lim Plumbagin Suppresses α-MSH-Induced Melanogenesis in B16F10 Mouse Melanoma Cells by Inhibiting Tyrosinase Activity International Journal of Molecular Sciences plumbagin melanogenesis pigmentation tyrosinase |
author_facet |
Taek-In Oh Jeong-Mi Yun Eun-Ji Park Young-Seon Kim Yoon-Mi Lee Ji-Hong Lim |
author_sort |
Taek-In Oh |
title |
Plumbagin Suppresses α-MSH-Induced Melanogenesis in B16F10 Mouse Melanoma Cells by Inhibiting Tyrosinase Activity |
title_short |
Plumbagin Suppresses α-MSH-Induced Melanogenesis in B16F10 Mouse Melanoma Cells by Inhibiting Tyrosinase Activity |
title_full |
Plumbagin Suppresses α-MSH-Induced Melanogenesis in B16F10 Mouse Melanoma Cells by Inhibiting Tyrosinase Activity |
title_fullStr |
Plumbagin Suppresses α-MSH-Induced Melanogenesis in B16F10 Mouse Melanoma Cells by Inhibiting Tyrosinase Activity |
title_full_unstemmed |
Plumbagin Suppresses α-MSH-Induced Melanogenesis in B16F10 Mouse Melanoma Cells by Inhibiting Tyrosinase Activity |
title_sort |
plumbagin suppresses α-msh-induced melanogenesis in b16f10 mouse melanoma cells by inhibiting tyrosinase activity |
publisher |
MDPI AG |
series |
International Journal of Molecular Sciences |
issn |
1422-0067 |
publishDate |
2017-02-01 |
description |
Recent studies have shown that plumbagin has anti-inflammatory, anti-allergic, antibacterial, and anti-cancer activities; however, it has not yet been shown whether plumbagin suppresses alpha-melanocyte stimulating hormone (α-MSH)-induced melanin synthesis to prevent hyperpigmentation. In this study, we demonstrated that plumbagin significantly suppresses α-MSH-stimulated melanin synthesis in B16F10 mouse melanoma cells. To understand the inhibitory mechanism of plumbagin on melanin synthesis, we performed cellular or cell-free tyrosinase activity assays and analyzed melanogenesis-related gene expression. We demonstrated that plumbagin directly suppresses tyrosinase activity independent of the transcriptional machinery associated with melanogenesis, which includes micropthalmia-associated transcription factor (MITF), tyrosinase (TYR), and tyrosinase-related protein 1 (TYRP1). We also investigated whether plumbagin was toxic to normal human keratinocytes (HaCaT) and lens epithelial cells (B3) that may be injured by using skin-care cosmetics. Surprisingly, lower plumbagin concentrations (0.5–1 μM) effectively inhibited melanin synthesis and tyrosinase activity but do not cause toxicity in keratinocytes, lens epithelial cells, and B16F10 mouse melanoma cells, suggesting that plumbagin is safe for dermal application. Taken together, these results suggest that the inhibitory effect of plumbagin to pigmentation may make it an acceptable and safe component for use in skin-care cosmetic formulations used for skin whitening. |
topic |
plumbagin melanogenesis pigmentation tyrosinase |
url |
http://www.mdpi.com/1422-0067/18/2/320 |
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