• Title/Summary/Keyword: Monoamine oxidase

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Inhibitory Activity on Monoamine Oxidase of Chrysanthemum indicum L. (감국의 Monoamine Oxidase 저해활성)

  • Chang, Eun-Ju;Choi, Dong-Kug;Park, Tae-Kyu;Hwang, Keum-Hee
    • Korean Journal of Pharmacognosy
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    • v.38 no.1
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    • pp.27-30
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    • 2007
  • We examined the inhibitory activities against monoamine oxidase (MAO) of Chrysanthemum indicum L. in vitro and in vivo methods. Methanolic extract of C. indicum showed significant inhibitory activities on MAO-A that were prepared from rat brain in vitro. The inhibitory activities were measured by serotonin as a substrate. The $IC_{50}$ value of methanolic extract of C. indicum was 0.24 mg/ml for the inhibition of MAO-A. The ethylacetate fraction of methanolic extract of C. indicum exhibited the best activity toward MAO-A with $IC_{50}$ value of 0.05 mg/ml in vitro. It was observed that those activities in vivo tests have different tendency each other. Ethanolic extract of C. indicum was have no effect on rat MAO by the oral administration (p<0.05). However, MAO inhibitory activities of ethanolic extract of C. indicum by the oral administration have similar tendency to those of iproniazid. Consequently, we suggest that C. indicum may have the effects on the inhibitory activities against MAO both in vitro and in vivo. These results indicates that the C. indicum extract has properties indicative of potential neuroprotective ability.

Monoamine Oxidase Inhibitory Components from the Roots of Sophora flavescens

  • Hwang Ji-Sang;Lee Seon A;Hong Seong Su;Lee Kyong Soon;Lee Myung Koo;Hwang Bang Yeon;Ro Jai Seup
    • Archives of Pharmacal Research
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    • v.28 no.2
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    • pp.190-194
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    • 2005
  • In our search for monoamine oxidase (MAO) inhibitors from natural resources, we found that the methanol extract of the roots of Sophora flavescens showed an inhibitory effect on mouse brain monoamine oxidase (MAO). Bioactivity-guided isolation of the extract yielded two known flavonoids, formononetin (1) and kushenol F (2), as active compounds along with three inactive compounds, oxymatrine (3), trifolirhizin (4), and ${\beta}$-sitosterol (5). Formononetin (1) and kushenol F (2) showed significant inhibitory effects on MAO in a dose-dependent manner with $IC_{50}$ values of 13.2 and $69.9\;{\mu}M$, respectively. Formononetin (1) showed a slightly more potent inhibitory effect against MAO-B ($IC_{50}:\;11.0\;{\mu}M$) than MAO-A ($IC_{50}:\;21.2\;{\mu}M$). Kushenol F (2) also preferentially inhibited the MAO-B activity than MAO-A activity with the $IC_{50}$ values of 63.1 and $103.7\;{\mu}M$, respectively.

Effects of Higenamine and Its Derivatives on the Activity of Rat Brain Mitochondrial Monoamine Oxidase (Higenamine과 그 유도체들이 흰쥐 미토콘드리아 Monoamine Oxidase 활성에 미치는 영향)

  • Suh, Yoo-Hun;Park, Hae-Young;Lim, Jung-Kyoo;Park, Chan-Woong
    • The Korean Journal of Pharmacology
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    • v.20 no.2
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    • pp.73-80
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    • 1984
  • The effect of higenamine and its derivatives on the activity of rat bran mitochondrial monoamine oxidase(MAO) was studied. Methoxyhigenamine of drugs tested had no effect on isometric contraction of heart and reversibly inhibited MAO towards 5-hydroxytryptamine(5-HT) and phenylethylamine(PEA) in a pure competitive fashion and in a hyperbolic mixed fashion, respectively, but was found to be relatively MAO-A selective inhibitor, with IC50 value for 5-HT lower ten fold than for PEA. The results suggest that methoxyhigenamine is a reversible, relatively MAO-A specific inhibitor in virto.

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Fluorescent Probes for Analysis and Imaging of Monoamine Oxidase Activity

  • Kim, Dokyoung;Jun, Yong Woong;Ahn, Kyo Han
    • Bulletin of the Korean Chemical Society
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    • v.35 no.5
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    • pp.1269-1274
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    • 2014
  • Monoamine oxidases catalyze the oxidative deamination of dietary amines and amine neurotransmitters, and assist in maintaining the homeostasis of the amine neurotransmitters in the brain. Dysfunctions of these enzymes can cause neurological and behavioral disorders including Parkinson's and Alzheimer's diseases. To understand their physiological roles, efficient assay methods for monoamine oxidases are essential. Reviewed in this Perspective are the recent progress in the development of fluorescent probes for monoamine oxidases and their applications to enzyme assays in cells and tissues. It is evident that still there is strong need for a fluorescent probe with desirable substrate selectivity and photophysical properties to challenge the much unsolved issues associated with the enzymes and the diseases.

Monoamine Oxidase-A Inhibitors from Medicinal Plants

  • Ryu, Shi-Yong;Han, Yong-Nam;Han, Byung-Hoon
    • Archives of Pharmacal Research
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    • v.11 no.3
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    • pp.230-239
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    • 1988
  • Thirty kinds of medicinal plants were screened to examine inhibitory activities on rat brain monoamine oxidase A, using serotonin as a substrate. As active principles, various kinds of stilbenes were isolated from Veratri Rhizoma, Reynoutriae Radix and Rhei undulati Rhizoma, and several kinds of flavonoids from Sophorae Flos, Chrisanthemi Flos and Glycine max. Among the compounds isolated, resveratrol(I) strongly inhibited MAO-A competitively, and its $IC_{50}$ and Ki values were 2 ${\mu}M$ and 2.5 ${\mu}M$, respectively. Inhibitory potencies towards MAO-A of some stilbenes and flavonoids were also compared.

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Monoamine Oxidase Inhibitor from Uncaria rhynchophylla

  • Hong, Seong-Su;Han, Xiang Hua;Park, So-Young;Choi, Woo-Hoi;Lee, Myung-Koo;Hur, Jae-Doo;Hwang, Bang-Yeon;Ro, Jai-Seup
    • Natural Product Sciences
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    • v.11 no.3
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    • pp.145-149
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    • 2005
  • A methanol soluble extract from the dried hooks and stems of Uncaria rhynchophylla showed a strong inhibitory activity against monoamine oxidase in mouse brain. Using a bioassay-guided purification of this extract, a known ${\beta}-carboline$ type alkaloid, harman (1), was obtained as an active constituent. In addition, five known indole alkaloids, isocorynoxeine (2), isorhynchophylline (3), corynoxeine (4), cadambine (5), and $3{\alpha}-dihydrocadambine$ (6), were isolated and found to be weakly active or inactive.

Inhibitory Effects of Coptisine on Monoamine Oxidase Activity

  • Lee, Myung-Koo;Lee, Kyong-Soon;Kim, Hack-Seang;Hong, Seung-Soo;Ro, Jai-Seup
    • Natural Product Sciences
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    • v.6 no.2
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    • pp.70-72
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    • 2000
  • The effects of coptisine on monoamine oxidase (EC 1.4.3.4; MAO) activity in mouse brain were investigated. Coptisine showed an inhibitory effect on MAO activity with a concentration-dependent manner. Coptisine exhibited 51.0% inhibition of MAO activity at $9\;{\mu}M$. The $IC_{50}$ value of coptisine was $8.7\;{\mu}M$. Coptisine inhibited MAO activity competitively with kynuramine as a substrate. The $K_i$ value of coptisine was $4.1\;{\mu}M$. These results indicate that coptisine functions to regulate the catecholamine content at biologically active sites.

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Monoamine Oxidase Inhibitors from Cinnamomi Cortex

  • Huong, Dang Thi Lan;Jo, Young-Su;Lee, Myung-Koo;Bae, Ki-Hwan;Kim, Young-Ho
    • Natural Product Sciences
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    • v.6 no.1
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    • pp.16-19
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    • 2000
  • Four compounds were isolated from the dichloromethane fraction of Cinnamomi Cortex through bioassay-guided isolation. Their structures were identified as coumarin (1), 3,3-dimethoxy-1-propenyl benzene (2), cinnamic acid (3) and o-methoxy cinnamaldehyde (4) on the basis of spectroscopic data. All four compounds showed inhibitory activities in vitro against monoamine oxidase (MAO) prepared by mouse brain. The $IC_{50}$ values were $41.4\;{\mu}M\;(1),\;110.6\;{\mu}M\;(2),\;252.5\;{\mu}M\;(3)\;and\;83.1\;{\mu}M$ (4), respectively.

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The Inhibitory Activity on Monoamine Oxidase of the Fruit of Morus alba (상심자의 모노아민산화효소 저해활성)

  • Hwang, keum-Hee;Song, Im
    • Korean Journal of Pharmacognosy
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    • v.34 no.2 s.133
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    • pp.185-189
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    • 2003
  • We examined the inhibitory activities against monoamine oxidase (MAO) of Morus alba in vitro and in vivo methods. Methanolic extract of M. alba showed significantly inhibitory activities on MAO-A and MAO-B that were prepared from rat brain and liver in vitro. The inhibitory activities were measured by serotonin and benzylamine as substrates, respectively. MAO-A and MAO-B activities were potently inhibited by ethylacetate extracts of M. alba in vitro tests. Those activities in vivo tests have different tendency each other. MAO-A activity was increased by the oral administration of methanolic extract of M. Alba, while, MAO-B activity was decreased. Consequently, we can suggest that M. alba may have the effects on the inhibitory activities against MAO both in vitro and in vivo.

Monoamine Oxidase Inhibitors Attenuate Cytotoxicity of 1-Methyl-4-phenylpyridinium by Suppressing Mitochondrial Permeability Transition

  • Lee, Chung-Soo
    • The Korean Journal of Physiology and Pharmacology
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    • v.10 no.4
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    • pp.207-212
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    • 2006
  • Mitochondrial permeability transition has been shown to be involved in neuronal cell death. Mitochondrial monoamine oxidase (MAO)-B is considered to play a part in the progress of nigrostriatal cell death. The present study examined the effect of MAO inhibitors against the toxicity of 1-methyl-4-phenylpyridinium $(MPP^+)$ in relation to the mitochondrial permeability transition. Chlorgyline (a selective inhibitor of MAO-A), deprenyl (a selective inhibitor of MAO-B) and tranylcypromine (nonselective inhibitor of MAO) all prevented cell viability loss, cytochrome c release, caspase-3 activation, formation of reactive oxygen species and depletion of GSH in differentiated PC12 cells treated with $500\;{\mu}M$$MPP^+$. The MAO inhibitors at $10\;{\mu}M$ revealed a maximal inhibitory effect and beyond this concentration the inhibitory effect declined. On the basis of concentration, the inhibitory potency was tranylcypromine, deprenyl and chlorgyline order. The results suggest that chlorgyline, deprenyl and tranylcypromine attenuate the toxicity of $MPP^+$ against PC12 cells by suppressing the mitochondrial permeability transition that seems to be mediated by oxidative stress.