• Bulletin of the Korean Chemical Society
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• v.32 no.3
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• pp.977-980
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• 2011

A new analytical method for measurement of 3,4-dihydroxyphenylalanine (DOPA) in human urine was developed. DOPA from an aqueous solution was converted into an ethoxycarbonyl (EOC) derivative. A tertbutyldimethylsilyl (TBDMS) reaction under anhydrous conditions was then attempted for analysis by gas chromatography-mass spectrometry in selected ion monitoring mode. A new mass spectral data on DOPA as a tri-EOC/mono-TBDMS derivative was built. This method showed good linearity (r ${\geq}$ 0.999), precision (% relative standard deviation = 3.1-9.2), and accuracy (% relative error = -7.2-8.8), with a detection limit of 0.05 ng/mL. This selective and accurate method of DOPA analysis will be useful for biochemical monitoring of various neurological disorders including Parkinson's disease in biological fluids.

• Archives of Pharmacal Research
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• v.29 no.8
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• pp.645-650
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• 2006

Tributyltin chloride (TBTC) at concentrations of $0.5-1.0\;{\mu}M$ inhibits dopamine biosynthesis in PC12 cells. In this study, the effects of TBTC on L-3,4-dihydroxyphenylalanine (L-DOPA)-induced cytotoxicity in PC12 cells were investigated. TBTC at concentrations up to $1.0\;{\mu}M$ neither affected cell viability, nor induced apoptosis after 24 or 48 h in PC12 cells. However, TBTC at concentrations higher than $2.0\;{\mu}M$ caused cytotoxicity through an apoptotic process. In addition, exposure of PC12 cells to non-cytotoxic (0.5 and $1.0\;{\mu}M$) or cytotoxic $(2.0\;{\mu}M)$ concentrations of TBTC in combination with L-DOPA (20, 50 and $100\;{\mu}M$) resulted in a significant increase in cell loss and the percentage of apoptotic cells after 24 or 48 h compared with TBTC or L-DOPA alone. The enhancing effects of TBTC on L-DOPA-induced cytotoxicity were concentration- and treatment time-dependent. These data demonstrate that TBTC enhances L-DOPA-induced cytotoxicity in PC 12 cells.

• Journal of Korean Dental Science
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• v.11 no.2
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• pp.43-56
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• 2018

Purpose: The purpose of this study was to assess the adhesiveness and cytotoxicity of 3, 4-dihydroxyphenylalanine (DOPA), and to evaluate the role of collagen membrane with DOPA in the guided bone regeneration. Materials and Methods: Peel resistance and cell cytotoxicity test were performed. Four defect types in nine rabbit calvaria were randomly allocated: i) control, ii) membrane, iii) deproteinized porcine bone mineral (DPBM) covered by membrane with DOPA, and iv) DPBM covered by membrane with cyanoacrylate. Animals were sacrificed at 2 (n=4) and 8 weeks (n=5) for microcomputed tomography and histomorphometric analysis. DOPA showed low peel resistance but high cell viability. Result: Cyanoacrylate and DOPA groups showed significantly higher mineralized tissue volume (MTV) compared to control and membrane groups at 2 weeks (P<0.05). At 8 weeks, DOPA group showed the highest MTV. Significantly higher new bone area was found in DOPA group at 8 weeks (P<0.05). Bone formation increased from 2 to 8 weeks in DOPA group (P<0.05). Conclusion: DOPA showed high cell viability and in vivo study revealed predictable performance in bone regeneration.

• Bulletin of the Korean Chemical Society
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• v.25 no.5
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• pp.625-628
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• 2004

Ceruloplasmin (CP), the blue oxidase present in all vertebrates, is the major copper-containing protein of plasma. It has been proposed that oxidation of L-3,4-dihydroxyphenylalanine (DOPA) may contribute to the pathogenesis of neurodegenerative disorders. The effect of the oxidized products of DOPA on the modification of human CP was investigated. When CP was incubated with the oxidized L-DOPA, the protein was induced to be aggregated and ferroxidase activity was decreased in a time-dependent manner. Radical scavengers and catalase significantly inhibited the oxidized DOPA-mediated CP aggregation. Copper chelatrors, Diethylenetriaminepenta acetic acid (DTPA) and Diethyldithiocarbamic acid (DDC), also inhibited the oxidative modification of CP. The results suggested that DOPA oxidation led to the formation of free radical and induced the CP aggregation.

• Journal of Environmental Health Sciences
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• v.22 no.1
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• pp.1-4
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• 1996

I have conducted two testings to find out which water is better for drinking water. First, I made 20 mM L-DOPA solutions by solving L-DOPA (3,4-Dihydroxyphenylalanine) in tap water, Waters' mineral water and reverse osmotic water. Then I measured activities after adding Tyrosinase (purifide enzyme, step 3), which was extracted from Salanum melongena(mad apple), in each L-DOPA solution. Second, I solved 0.1, 0.5 and 0.9% salt in each 20 mM L-DOPA distilled water to measure activity of each salt solution. The results of the testings are as follows: 1. 10 minutes after adding Salanum melongena(mad apple) tyrosinase in each L-DOPA solution, activity of Waters' mineral water was 0.867 tap water 0.777 and reverse osmotic water 0.742. 2. Activity of Waters' mineral water was higher than that of tap water by 10.4% and higher then reverse osmotic by 14.4%. 3. Activity of Waters' mineral water was much higher than that of 0.9% salt water by 41.8%. 4. The optimum pH of Salanum melongena (mad apple) tyrosinase is 9.0. Most enzymes working in the human metabolism are alkaline and body fluids' pH also alkaline. In conclusion, an alkaline water is believed better than an acidic water for drinking.

• Bulletin of the Korean Chemical Society
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• v.26 no.8
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• pp.1251-1254
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• 2005

It has been proposed that oxidation of L-3,4-dihydroxyphenylalanine (DOPA) may contribute to the pathogenesis of neurodegenerative disease. In this study, L-DOPA-Fe(III)-mediated DNA cleavage and the protection by carnosine and homocarnosine against this reaction were investigated. When plasmid DNA was incubated with L-DOPA in the presence of Fe(III), DNA strand was cleaved. Radical scavengers and catalase significantly inhibited the DNA breakage. These results suggest that $H_2O_2$ may be generated from the oxidation of DOPA and then $Fe^{3+}$ likely participates in a Fenton’s type reaction to produce hydroxyl radicals, which may cause DNA cleavage. Carnosine and homocarnosine have been proposed to act as anti-oxidants in vivo. The protective effects of carnosine and homocarnosine against L-DOPA-Fe(III)-mediated DNA cleavage have been studied. Carnosine and homocarnosine significantly inhibited DNA cleavage. These compounds also inhibited the production of hydroxyl radicals in L-DOPA/$Fe^{3+}$ system. The results suggest that carnosine and homocarnosine act as hydroxyl radical scavenger to protect DNA cleavage. It is proposed that carnosine and homocarnosine might be explored as potential therapeutic agents for pathologies that involve damage of DNA by oxidation of DOPA.

• Nutrition Research and Practice
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• v.7 no.4
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• pp.249-255
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• 2013

In this study, the protective effects of EGCG on L-3,4-dihydroxyphenylalanine (L-DOPA)-induced oxidative cell death in catecholaminergic PC12 cells, the in vitro model of Parkinson's disease, were investigated. Treatment with L-DOPA at concentrations higher than $150{\mu}M$ caused cytotoxicity in PC12 cells, as determined using the 3-(4,5-dimetylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) assay and flow cytometry detection. The apoptotic ratio was similar in cells treated with $100{\mu}M$ EGCG plus $150{\mu}M$ L-DOPA (5.02%) and the control (0.96%) (P > 0.05), and was lower than that of cells treated with L-DOPA only (32.24%, P < 0.05). The generation level of ROS (% of control) in cells treated with EGCG plus L-DOPA was lower than that in cells treated with L-DOPA only (123.90% vs 272.32%, P < 0.05). The optical density in production of TBARS in cells treated with L-DOPA only was higher than that in the control ($0.27{\pm}0.05$ vs $0.08{\pm}0.04$, P < 0.05), and in cells treated with EGCG only ($0.14{\pm}0.02$, P < 0.05), and EGCG plus L-DOPA ($0.13{\pm}0.02$, P < 0.05). The intracellular level of GSH in cells treated with EGCG plus L-DOPA was higher than that in cells treated with L-DOPA only ($233.25{\pm}16.44$ vs $119.23{\pm}10.25$, P < 0.05). These results suggest that EGCG protects against L-DOPA-induced oxidative apoptosis in PC12 cells, and might be a potent neuroprotective agent.

• Biomolecules & Therapeutics
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• v.13 no.1
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• pp.32-34
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• 2005

Effect of isoliquiritigenin isolated from the heartwood of Dalbergia odorifera T. Chen (Leguminosae) on mushroom tyrosinase activity was investigated in vitro using L-tyrosine and L-3, 4-dihydroxyphenylalanine (L-DOPA) as the substrates. When L-tyrosine was used as a substrate, both isoliquiritigenin and kojic acid, a positive control, inhibited tyrosinase activity in a concentration-dependent manner. IC$_{50}$ values of isoliquiritigenin and kojic acid were 61.4 and 52.2 ${\muM}$, respectively. However, isoliquiritigenin showed week inhibitory effect on the oxidation of L-DOPA by tyrosinase with inhibition ratio of 9.1 ${\pm}$ 7.1% at 100 ${\muM}$. It is also suggested that 3-unsubstituted and 4-hydroxyl phenyl group in isoliquiritigenin plays an important role on the inhibition of tyrosinase activity when L-tyrosine was used as a substrate. Analysis of Lineweaver-Burk plot showed that isoliquiritigenin acts as a competitive inhibitor in case of L-tyrosine as a substrate.

• Korean Journal of Plant Resources
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• v.14 no.1
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• pp.32-37
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• 2001

Mammalian tyrosinase plays an important role in the process of melanin polymer biosynthesis by catalyzing the hydroxylation of tyrosine to 3,4-dihydroxyphenylalanine(DOPA) and the oxidation of DOPA to dopaquinone. These processes are major determinant of human skin color and involved in localized hyperpigmentation. Therefore, the enzyme inhibitors have been of great concern as skin-whitening cosmetics. Methanol extracts of 174 oriental herbs were screened for the mushroom tyrosinase inhibitory activity.

• Korean Chemical Engineering Research
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• v.54 no.6
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• pp.817-821
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• 2016

Levodopa or L-3,4-dihydroxyphenylalanine (L-DOPA) is the direct precursor of the neurotransmitter dopamine. L-DOPA is a well-known neuroprotective agent for the treatment of Parkinson's disease symptoms. L-DOPA was synthesized using the enzyme, tyrosinase, as a biocatalyst for the conversion of L-tyrosine to L-DOPA and an electrochemical method for reducing L-DOPAquinone, the product resulting from enzymatic synthesis, to L-DOPA. In this study, three electrode systems were used: A glassy carbon electrode (GCE) as working electrode, a platinum, and a Ag/AgCl electrode as auxiliary and reference electrodes, respectively. GCE has been modified using electropolymerization of pyrrole to facilitate the electron transfer process and immobilize tyrosinase. Optimum conditions for the electropolymerization modified electrode were a temperature of $30^{\circ}C$ and a pH of 7 producing L-DOPA concentration 0.315 mM. After 40 days, the relative activity of an enzyme for electropolymerization remained 38.6%, respectively.