TXM13 human melanoma cells: a novel source for the inhibition kinetics of human tyrosinase and for screening whitening agents

Abstract

Research involving whitening agents requires several steps of experimentation, and the initial step is to test whitening agents with human melanocytes and those with human tyrosinase. Unfortunately, it takes a long time to gather human melanocytes, and these cells have some limitations when it comes to performing experiments, such as their passage difficulties and their cost. In this study, we suggest that the TXM13 human melanoma cells could be a useful cell candidate for studying human tyrosinase inhibition and depigmentation. We applied a tyrosinase inhibitor, such as dithioglycerine (DTGC), to validate the cell line's usefulness, and we tested the effect of DTGC on TXM13 melanogenesis. The results showed that human tyrosinase from TXM13 was appropriate, according to the inhibition kinetics, and that the conspicuous depigmentation of TXM13 occurred after DTGC treatment without downregulating the tyrosinase expression level. When taken together, our findings provide useful information regarding the use of the TXM13 melanoma cells for the development of whitening agents.

Anti-melanogenic and anti-oxidant activities of ethanol extract of Kummerowia striata: Kummerowia striata regulate anti-melanogenic activity through down-regulation of TRP-1, TRP-2 and MITF expression

“…Tyrosinase, TRP-1, and TRP-2 play important roles in melanin biosynthesis [ 27 ]. Thus, the mechanism underlying the effect of skin whitening agents involves inhibition of melanin production by decreasing tyrosinase activity [ 28 ]. The expression of tyrosinase, TRP-1, and TRP-2 genes is known to be regulated by MITF [ 29 ].…”

Kinetic, structural and molecular docking studies on the inhibition of tyrosinase induced by arabinose

“…We monitored such changes using spectrofluorometry. The inhibitory mechanism of arabinose resembled that of a copper chelator, but differs in that arabinose did not directly bind to copper atoms at the active site [34][35][36][37].…”

Inhibitory Effect of Phthalic Acid on Tyrosinase: The Mixed-Type Inhibition and Docking Simulations

“…Experimentally, our kinetic studies consistently confirmed all results and the model described in Scheme 1. The inhibitory mechanism of PA was partly similar to those of copper chelators but still has different aspect that PA did not directly bind to coppers at the active site [33, 34]. V max value changes were predicted by docking simulation that PA might not compete with L-DOPA for docking because the binding sites are not located in the active site pocket.…”