Biochemical Characterization of Ferulic Acid and Caffeic Acid Which Effectively Inhibit Melanin Synthesis via Different Mechanisms in B16 Melanoma Cells
| Autor: | Motoki Imai, Hiroko Maruyama, Fumitaka Kawakami, Fazel Shamsa, Thet-Thet Lwin |
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| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
Coumaric Acids Tyrosinase Melanoma Experimental Pharmaceutical Science Ferulic acid Melanin Mice 03 medical and health sciences chemistry.chemical_compound Caffeic Acids 0302 clinical medicine Biosynthesis Cell Line Tumor Benzoquinones Caffeic acid Animals Phosphorylation Casein Kinase II Catechol oxidase Melanins Pharmacology chemistry.chemical_classification biology Monophenol Monooxygenase food and beverages General Medicine Enzyme assay Dihydroxyphenylalanine 030104 developmental biology Enzyme chemistry Biochemistry 030220 oncology & carcinogenesis biology.protein |
| Zdroj: | Biological and Pharmaceutical Bulletin. 41:806-810 |
| ISSN: | 1347-5215 0918-6158 |
| DOI: | 10.1248/bpb.b17-00892 |
| Popis: | In this study, we examined the inhibitory effects of ferulic acid and caffeic acid on melanin production using a murine B16 melanoma cell line. The mechanisms by which the two acids inhibit melanin production were investigated by evaluating their effects on the activity of tyrosinase, which is involved is the first step of melanin biosynthesis. Ferulic acid showed no toxicity against the melanoma cells at any dose, whereas caffeic acid exerted cellular toxicity at concentrations higher than 0.35 mM. Both ferulic and caffeic acids effectively inhibited melanin production in the B16 melanoma cells. Ferulic acid reduced tyrosinase activity by directly binding to the enzyme, whereas no binding was observed between caffeic acid and tyrosinase. Both ferulic acid and caffeic acid inhibited casein kinase 2 (CK2)-induced phosphorylation of tyrosinase in a dose-dependent manner in vitro. Ferulic acid was found to be a more effective inhibitor of melanin production than caffeic acid; this difference in the inhibitory efficacy between the two substances could be attributable to the difference in their tyrosine-binding activity. Our analysis revealed that both substances also inhibited the CK2-mediated phosphorylation of tyrosinase. |
| Databáze: | OpenAIRE |
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