Oxyresveratrol as the Potent Inhibitor on Dopa Oxidase Activity of Mushroom Tyrosinase

1998 ◽  
Vol 243 (3) ◽  
pp. 801-803 ◽  
Author(s):  
Nam-Ho Shin ◽  
Shi Yong Ryu ◽  
Eun Ju Choi ◽  
Seh-Hoon Kang ◽  
IL-Moo Chang ◽  
...  
Keyword(s):  
Oxidase Activity ◽  
Potent Inhibitor ◽  
Mushroom Tyrosinase ◽  
Dopa Oxidase

Potent Inhibitory Effects of N-Aryl S-Alkylthiocarbamate Derivatives on the Dopa Oxidase Activity of Mushroom Tyrosinase

2005 ◽  
Vol 53 (7) ◽  
pp. 747-749 ◽  
Author(s):  
Kun Ho Lee ◽  
Mamoru Koketsu ◽  
Sang Yoon Choi ◽  
Kang Jin Lee ◽  
Pyeongjae Lee ◽  
...  
Keyword(s):  
Oxidase Activity ◽  
Mushroom Tyrosinase ◽  
Inhibitory Effects ◽  
Dopa Oxidase

Inhibition of Melanogenesis in Murine B16/F10 Melanoma Cells by Ligusticum sinensis Oliv.

2006 ◽  
Vol 34 (03) ◽  
pp. 523-533 ◽  
Author(s):  
Ching-Yuan Wu ◽  
Jong-Hwei S. Pang ◽  
Sheng-Teng Huang
Keyword(s):  
Mrna Expression ◽  
Oxidase Activity ◽  
Underlying Mechanism ◽  
Inhibitory Effect ◽  
Melanoma Cells ◽  
Dependent Manner ◽  
Mushroom Tyrosinase ◽  
Tyrosinase Gene ◽  
Direct Inhibitory Effect ◽  
Dopa Oxidase

Ligusticum sinensis Oliv. (LSO) is an herbal drug commonly used as a topical treatment of epidermal hyperdepigmentation in Chinese medicine. However, the mechanism underlying the depigmentation by LSO is still unclear. The purpose of this study was to investigate the effects of LSO on the process of melanogenesis and its possible underlying mechanism. Suppressed DOPA oxidase activity of mushroom tyrosinase was first noted when incubated with aqueous extracts of LSO, demonstrating the direct inhibitory effect of LSO on mushroom tyrosinase. Further experiments were carried out in murine B16/F10 melanoma cells and the effects of LSO extract on melanin formation, tyrosinase activity and tyrosinase gene expression were tested. Under conditions without affecting the viability of murine B16/F10 melanoma cells, LSO extract significantly reduced the cellular melanin content in a dose-dependent manner. The DOPA oxidase activity of tyrosinase in B16/F10 cells was dose-dependently inhibited by LSO treatment, possibly mediated by the suppressed tyrosinase mRNA expression in LSO-treated B16/F10 cells. In conclusion, the inhibitory effect of LSO on melanogenesis is likely associated with decreased DOPA oxidase activity of tyrosinase that is most likely the result of the down-regulation of tyrosinase mRNA expression.

Potent Inhibitory Effects of N-Aryl S-Alkylthiocarbamate Derivatives on the Dopa Oxidase Activity of Mushroom Tyrosinase.

ChemInform ◽  
2005 ◽  
Vol 36 (52) ◽  
Author(s):  
Kun Ho Lee ◽  
Mamoru Koketsu ◽  
Sang Yoon Choi ◽  
Kang Jin Lee ◽  
Pyeongjae Lee ◽  
...  
Keyword(s):  
Oxidase Activity ◽  
Mushroom Tyrosinase ◽  
Inhibitory Effects ◽  
Dopa Oxidase

Some Commercial Azo Dyes as Inhibitors of Mushroom Tyrosinase DOPA Oxidase Activity

2007 ◽  
Vol 2 (8) ◽  
pp. 718-724 ◽  
Author(s):  
Shiv Kumar Dubey ◽  
Archana Pandey . ◽  
Ashok Kumar Bajaj . ◽  
and Krishna Misra .
Keyword(s):  
Azo Dyes ◽  
Oxidase Activity ◽  
Mushroom Tyrosinase ◽  
Dopa Oxidase

scholarly journals Oxidation of monohydric phenol substrates by tyrosinase. An oximetric study

1992 ◽  
Vol 288 (1) ◽  
pp. 63-67 ◽  
Author(s):  
S Naish-Byfield ◽  
P A Riley
Keyword(s):  
Oxygen Consumption ◽  
Maximum Rate ◽  
Low Ph ◽  
Molar Ratio ◽  
Lag Phase ◽  
Complete Oxidation ◽  
Mushroom Tyrosinase ◽  
Tyrosine Oxidation ◽  
Rate Of Reaction ◽  
Dopa Oxidase

The purity of commercially available mushroom tyrosinase was investigated by non-denaturing PAGE. Most of the protein in the preparation migrated as a single band under these conditions. This band contained both tyrosinase and dopa oxidase activity. No other activity of either classification was found in the preparation. Oxygen consumption by tyrosinase during oxidation of the monohydric phenol substrates tyrosine and 4-hydroxyanisole (4HA) was monitored by oximetry in order to determine the stoichiometry of the reactions. For complete oxidation, the molar ratio of oxygen: 4HA was 1:1. Under identical conditions, oxidation of tyrosine required 1.5 mol of oxygen/mol of tyrosine. The additional oxygen uptake during tyrosine oxidation is due to the internal cyclization of dopaquinone to form cyclodopa, which undergoes a redox reaction with dopaquinone to form dopachrome and dopa, which is then oxidized by the enzyme, leading to an additional 0.5 mol of oxygen/mol of original substrate. Oxygen consumption for complete oxidation of 200 nmol of 4HA was constant over a range of concentrations of tyrosinase of 33-330 units/ml of substrate. The maximum rate of reaction was directly proportional to the concentration of tyrosinase, whereas the length of the lag phase decreased non-linearly with increasing tyrosinase concentration. Activation of the enzyme by exposure to citrate was not seen, nor was the lag phase abolished by exposure of the enzyme to low pH. Michaelis-Menten analysis of tyrosinase in which the lag phase is abolished by pre-exposure of the enzyme to a low concentration of dithiothreitol gave Km values for tyrosine and 4HA of 153 and 20 microM respectively.

scholarly journals The Development of Dopa Oxidase Activity in the Skin and in the Hair Cycle

1961 ◽  
Vol 1961 (2) ◽  
pp. 190-194
Author(s):  
Ken HASHIMOTO ◽  
Kazuo OGAWA ◽  
Walter F. LEVER
Keyword(s):  
Oxidase Activity ◽  
Hair Cycle ◽  
Dopa Oxidase

Relationship between 4-hydroxyanisole toxicity and dopa oxidase activity for three melanoma cell lines

1997 ◽  
Vol 7 (5) ◽  
pp. 373-381 ◽  
Author(s):  
J Rodriguez-Vicente ◽  
V Vicente-Ortega ◽  
M Canteras-Jordana ◽  
F Calderon-Rubiales
Keyword(s):  
Cell Lines ◽  
Melanoma Cell ◽  
Oxidase Activity ◽  
Dopa Oxidase ◽  
Melanoma Cell Lines

Human TRP-1 Has Tyrosine Hydroxylase but no DOPA Oxidase Activity

1994 ◽  
Vol 7 (3) ◽  
pp. 131-140 ◽  
Author(s):  
HUIQUAN ZHAO ◽  
YANG ZHAO ◽  
JAMES J. NORDLUND ◽  
RAYMOND E. BOISSY
Keyword(s):  
Tyrosine Hydroxylase ◽  
Oxidase Activity ◽  
Dopa Oxidase

scholarly journals 36H: A Novel Potent Inhibitor for Antimelanogenesis

2018 ◽  
Vol 2018 ◽  
pp. 1-12 ◽  
Author(s):  
Li-Ching Lin ◽  
Chung-Yi Chen ◽  
Chia-Hung Kuo ◽  
Yun-Sheng Lin ◽  
Byeong Hee Hwang ◽  
...  
Keyword(s):  
Potent Inhibitor ◽  
Reducing Power ◽  
Competitive Inhibitor ◽  
Mushroom Tyrosinase ◽  
Antioxidant Power ◽  
Whitening Agent ◽  
Human Melanocyte ◽  
Polymerase Chain ◽  
Dpph Scavenging

N-Hydroxycinnamoylphenalkylamides (36H) exhibited both antioxidation and antityrosinase abilities. The compound was studied for its antioxidative properties, using a 1,1-diphenyl-2-picrylhydrazul- (DPPH-) scavenging test, a ferric ion-reducing antioxidant power assay (FRAP) assessment, and a metal-chelating power assay. The results showed that 36H had antioxidative capabilities in the DPPH-scavenging and ferric-reducing power examinations but the chelating power assay did not demonstrate antioxidative capability. 36H was also measured for tyrosinase inhibitory activity applying various species platforms, including in vitro mushroom, B16F10 mouse melanoma, and human melanocyte cells. In terms of in vitro mushroom tyrosinase suppression, 36H restrained the melanogenesis processes. It is assumed that 36H blocked the tyrosinase active site as a competitive inhibitor for mushroom tyrosinase, hence not decreasing the human normal melanocyte cellular viability. A quantitative real-time polymerase chain reaction (qRT-PCR) and western blot discovered that 36H downregulated melanogenesis-related RNA and proteins, including pigment production (MITF, tyrosinase, TRP-1, and TRP-2), melanosome maturation (Rab27a), and melanosome transportation (Myo5a, MLPH and Mreg). Overall, 36H displayed the biofunctions of antioxidation and melanin suppression, so there was a possibility for its application as a food additive or a skin-whitening agent.

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