Evaluation of the inhibition of mushroom tyrosinase and cellular tyrosinase activities of oxyresveratrol: comparison with mulberroside A

Kim, Jeong Keun; Park, Keun Tae; Lee, Hyun Sun; Kim, Mijin; Lim, Young Hee

doi:10.3109/14756366.2011.598866

Cited by 34 publications

(23 citation statements)

References 29 publications

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“…Kim's results showed competitive inhibition, whereas our results showed mixed-type inhibition. In addition, our results showed that MA had apparent inhibition of the diphenolase, which differed from their reports [24] . These inconsistent results were most likely caused by differences in the purity of the sample, the source of the mushroom tyrosinase, the reaction systems and operator errors.…”

Section: Discussioncontrasting

confidence: 99%

“…The results concerning the effect of OR on the inhibition of the mushroom tyrosinase were similar to our results. The strong tyrosinase inhibitory activity of OR was previously confirmed in other studies, which found that the IC 50 value of OR was 0.46∼1.10 µmol/L, depending on the assay conditions [8] , [24] Concerning the OR-inhibited monophenolase activity, the IC 50 value of OR extracted from the mulberry twigs was 0.943 µmol/L (0.23 µg/L), which was reported by Lee et al [8] . Compared with our results, there was an 8-fold difference in the IC 50 value.…”

Section: Discussionsupporting

confidence: 67%

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An Efficient Preparation of Mulberroside A from the Branch Bark of Mulberry and Its Effect on the Inhibition of Tyrosinase Activity

et al. 2014

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A bioactive ingredient in an ethanol extract from the branch bark of cultivated mulberry Husang-32 (Morus multicaulis Perr.) was isolated using a macroporous resin column. The primary component, which was purified by semi-preparative high-performance liquid chromatography diode array detection (HPLC-DAD), was identified as mulberroside A (MA) by liquid chromatograph-mass spectrometer (LC-MS), 1H and 13C nuclear magnetic resonance (NMR) spectra. In total, 4.12 g MA was efficiently extracted from one kilogram of mulberry bark. The enzymatic analysis showed that MA inhibited the generation of dopachrome by affecting the activities of monophenolase and diphenolase of tyrosinase in vitro. This analysis indicated that MA and oxyresveratrol (OR), which is the the aglycone of mulberroside A, exhibited strong inhibition of the monophenolase activity with IC50 values of 1.29 µmol/L and 0.12 µmol/L, respectively. However, the former showed weaker inhibitory activity than the latter for diphenolase. For the monophenolase activity, the inhibitory activity of MA and OR was reversible and showed mixed type 1 inhibition. Additionally, the inhibition constant KI (the inhibition constant of the effectors on tyrosinase) values were 0.385 µmol/L and 0.926 µmol/L, respectively, and the KIS (the inhibition constants of the enzyme-substrate complex) values were 0.177 µmol/L and 0.662 µmol/L, respectively. However, MA showed competitive inhibition of diphenolase activity, and KI was 4.36 µmol/L. In contrast, OR showed noncompetitive inhibition and KI = KIS = 2.95 µmol/L. Taken together, these results provide important information concerning the inhibitory mechanism of MA on melanin synthesis, which is widely used in whitening cosmetics.

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Section: Discussioncontrasting

confidence: 99%

Section: Discussionsupporting

confidence: 67%

An Efficient Preparation of Mulberroside A from the Branch Bark of Mulberry and Its Effect on the Inhibition of Tyrosinase Activity

et al. 2014

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“…7) It was reported that mulberroside A (MulA), one major constituent in the medicinal herb Mori Cortex, which is widely used to treat gout, arthritis and rheumatism in traditional Chinese medicine, was converted to OXY, and the latter was transported into the circulating blood and tissues at high rates in rats 8) and exhibited higher biological activity than MulA in both in vivo and in vitro studies. 9) Although there are many studies focusing on assessment of the pharmacological activity of OXY, its metabolism has not been adequately characterized. The presence of four hydroxyl groups on the stilbene core structure (Fig.…”

Section: Introductionmentioning

confidence: 99%

Regioselective Glucuronidation of Oxyresveratrol, a Natural Hydroxystilbene, by Human Liver and Intestinal Microsomes and Recombinant UGTs

Mei

Ruan

et al. 2014

Drug Metabolism and Pharmacokinetics

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Oxyresveratrol (OXY) is a natural hydroxystilbene that shows similar bioactivity but better water solubility than resveratrol. This study aims to characterize its glucuronidation kinetics in human liver (HLMs) and intestinal (HIMs) microsomes and identify the main UDP-glucuronosyltransferase (UGT) isoforms involved. Three and four mono-glucuronides of OXY were generated in HIMs and HLMs, respectively, with oxyresveratrol-2-O-β-D-glucuronosyl (G4) as the major metabolite in both organs. The kinetics of G4 formation fit a sigmoidal model in HLMs and biphasic kinetics in HIMs. Multiple UGT isoforms catalyzed G4 formation with the highest activity observed with UGT1A9 followed by UGT1A1. G4 formation by both isoforms followed substrate inhibition kinetics. Propofol (UGT1A9 inhibitor) effectively blocked G4 generation in HLMs (IC50 63.7 ± 11.6 µM), whereas the UGT1A1 inhibitor bilirubin only produced partial inhibition in HLMs and HIMs. These findings shed light on the metabolic mechanism of OXY and arouse awareness of drug interactions.

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“…It is a very interesting compound because of its many uses in the agricultural, medicinal, and cosmetic industries . It has been described that oxyresveratrol and its analogous resveratrol have an inhibitory effect on the enzyme tyrosinase , a copper monooxigenase widely distributed in bacteria, fungi, plants, and animals, which is responsible for melanization in animals and browning in plants . In fact oxyresveratrol has basically been described as a potent inhibitor of the dopa‐oxidase activity of this enzyme .…”

Section: Introductionmentioning

confidence: 99%

Kinetic characterization of oxyresveratrol as a tyrosinase substrate

et al. 2015

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Oxyresveratrol is a stilbenoid described as a powerful inhibitor of tyrosinase and proposed as skin-whitening and anti-browning agent. However, the enzyme is capable of acting on it, considering it as a substrate, as it has been proved in the case of its analogous resveratrol. Tyrosinase hydroxylates the oxyresveratrol to an odiphenol and oxidizes the latter to an o-quinone, which finally isomerizes to p-quinone. For these reactions to take place the presence of the E ox (oxy-tyrosinase) form is necessary. The kinetic analysis of the proposed mechanism has allowed the kinetic characterization of this molecule as a substrate of tyrosinase, affording a catalytic constant of 5.

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Evaluation of the inhibition of mushroom tyrosinase and cellular tyrosinase activities of oxyresveratrol: comparison with mulberroside A

Cited by 34 publications

References 29 publications

An Efficient Preparation of Mulberroside A from the Branch Bark of Mulberry and Its Effect on the Inhibition of Tyrosinase Activity

An Efficient Preparation of Mulberroside A from the Branch Bark of Mulberry and Its Effect on the Inhibition of Tyrosinase Activity

Regioselective Glucuronidation of Oxyresveratrol, a Natural Hydroxystilbene, by Human Liver and Intestinal Microsomes and Recombinant UGTs

Kinetic characterization of oxyresveratrol as a tyrosinase substrate

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