作者: Hideaki Fujita , Maya Hongo , Mayu Mochizuki , Kouji Yokoyama , Yoshitaka Tanaka
DOI: 10.1111/J.1600-0625.2010.01241.X
关键词: Octadecatrienoic acid 、 Tyrosinase 、 Brefeldin A 、 Golgi apparatus 、 Lysosome 、 Melanin 、 Cellular pigmentation 、 Biology 、 Biochemistry 、 Melissa officinalis
摘要: 16-hydroxy-9-oxo-10E,12E,14E-octadecatrienoic acid, also known as Corchorifatty acid B (CFAB), is isolated from the ethanol extracts of aerial parts Melissa officinalis Linne (Labiatae) and exhibits inhibitory effects on cellular pigmentation in both human melanocytes mouse melanoma B16 cells. CFAB specifically decreases melanin by most likely inducing rapid degradation tyrosinase Interestingly, unlike other reagents that promote proteasomes or lysosomes, neither proteasomal nor lysosomal inhibitors can halt CFAB-induced degradation. Only brefeldin A, which inhibits protein transport endoplasmic reticulum to Golgi complex, effectively impede decrease. These results suggest decrease occurs post-Golgi compartments but not compartments. Taken together, a unique reagent primarily accelerates mechanism differs those considered for hypopigmentation currently reported.