• Archives of Pharmacal Research
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• v.11 no.3
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• pp.213-217
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• 1988

The effects of ethanol and acetaldehyde on monoamine oxidase activity in mouse liver mitochondrial fraction were studied. In vivo, a single dose of ethanol increased the hepatic monoamine oxidase activity compared to control group, and chronic ethanol consumption also increased the enzyme activity using tyramine, benzylamine or serotonin as substrate. Acetaldehyde, the metabolite of ethanol, significantly increased monoamine oxidase activity more than ethanol did. In contrast to the in vivo results, it was found that the monoamine oxidase activity was inhibited in vitro by ethanol or acetaldehyde in the dose-dependent manner.

• The Korean Journal of Pharmacology
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• v.8 no.2
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• pp.41-47
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• 1972

Fluorides were supposed to exert a stimulatory action on the catecholamine release. In this study, the authors attempted to investigate the action of sodium fluoride on the catecholamine release from the isolated perfused cow adrenal gland and rat heart. And also the inhibitory effect of sodium fluoride on the monoamine oxidase activity in rat heart and liver mitochondria was investigated. The monoamine oxidase activity was measured by the conversion of benzylamine to benzaldehyde. The results obtained were follows; 1. Sodium fluoride stimulated the release of catecholamine from the isolated perfused cow adrenal gland and rat heart. 2. Sodium fluoride inhibited the rat heart and liver mitochondrial monoamine oxidase activity.

• Archives of Pharmacal Research
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• v.13 no.2
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• pp.132-135
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• 1990

Polyhydroxystilbenes including resveratrol were reported to competitively inhibit monoamine oxidase-A-without structural relation with substrates and cynthetic inhibitors for the enzyme. We attempt to explore a plausible mechanism for their inhibitory activity on MAO-A. All the polyhydroxystilbenes tested showed the antioxidant activity on liver homogenate. Furthermore, the antioxidant activity turned out to closely correlate with the MAO-A inhibitory activity.

• The Korean Journal of Food And Nutrition
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• v.17 no.4
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• pp.347-355
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• 2004

This study was undertaken in order to evaluate effects of methanol extracts of Stachys sieboldii MIQ and its related enzyme activities in brain tissues of rats. Sprague-Dawley(SD) male rats were fed within a control group, which is a basic diet group. The experimental diet group was given 100 and 200 mg/kg to supervise 100 and 200 mg/kg body weight per day for 20 days. Lipid peroxide levels and acetylcholine esterase activity in brain tissues were slightly decreased at a dose dependent manner, in vitro. Lipid peroxide levels were also decreased at a dose dependent manner; methanolic extracts of Stachys sieboldii MIQ demonstrated significant inhibitory effects, in vivo. Monoamine oxidase and xanthine oxidase activities were significantly inhibited in the brain tissues of experimental group compared to control group and the ratio of type conversion of xanthine oxidase were decreased.

• Korean Journal of Pharmacognosy
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• v.29 no.4
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• pp.271-276
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• 1998

The inhibitory effects of MeOH extracts of 100 medicinal herbs on monoamine oxidase (MAO) activity were investigated. MAO was purified from mouse brain and its activity was determined by fluorospectrophotomer using kynuramine as a substrate. Nine kinds of MeOH extracts of herbs including Artemisia iwayomogi showed a mild inhibitory effect with ${100}-{200}\;{\mu}/ml$ in their $IC_{50}$ values on MAO activity. Seventeen MeOH extracts including Juglans mandshurica exhibited a weak inhibition of MAO activity with ${200}-{300}\;{\mu}/ml$ in their $IC_{50}$ values.

• Korean Journal of Pharmacognosy
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• v.37 no.3
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• pp.157-161
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• 2006

We examined the inhibitory activities against monoamine oxidase (MAO) of Prunella vulgaris in vitro and in vivo methods. Methanolic extract of P. vulgaris showed significantly Inhibitorγ 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 P. vulgaris in vitro tests. It was observed that those activities in vivo tests have different tendency each other. MAO-A activity was increased by the oral administration of methanolic extract of P. vulgaris while MAO-B activity was decreased. Consequently, we suggest that P. vulgaris may have the effects on the inhibitory activities against MAO both in vitro and in vivo.

• The Journal of the Korean life insurance medical association
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• v.1 no.1
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• pp.84-87
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• 1984

1. Effect of bretylium on the pressor response of the whole and spinal rabbits to tyramine was observed in conditions of monoamine oxidase inhibition brought about by catron administration. 2. Bretylium increased the prossor response to tyramine in the whole and spinal rabbits. 3. Bretylium failed to increase the tyramine effect if bretylium was given after administration of catron, a monoamine oxidase inhibitor. Actually the tyramine effect was decreased by bretylium in this situation. 4. The increase of the tyramine effect by bretylium will be due to its monoamine oxidase inhibitory property, and the decrease of the tyramine effect will be due to its adrenergic neurone b1coking property.

• Korean Journal of Pharmacognosy
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• v.37 no.4 s.147
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• pp.320-323
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• 2006

The effects of evodiamine on monoamine oxidase (MAO) activity were investigated. MAO was purified from mouse brain and the $K_m\;and\;V_{max}$ values of MAO were $78.5{\pm}5.28{\mu}M$ and $0.68{\pm}0.07$ nmol/min/mg protein, respectively (n=4). Evodiamine at $30-120{\mu}M$ showed an inhibitory effect on MAO activity using a substrate kynuramine with an $IC_{50}$ value of $104.2{\mu}M$ (n=4). Evodiamine also exhibited a non-competitive inhibition on MAO. The $K_i$ value for evodiamine was $72.5{\pm}10.8{\mu}M$ (n=4). These results suggest that evodiamine partially contributes to the regulation of monoamine content.

• Applied Biological Chemistry
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• v.42 no.2
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• pp.166-169
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• 1999

The repeated silica gel colum chromatographies of n-BuOH fraction obtained from MeOH extracts of Eucommia ulmoides leaves led to isolation of a flavonoid-glycoside inhibiting monoamine oxidase B activity. Its chemical structure was determined to be $3-O-[{\beta}-D-glucopyranosyl\;(1{\rightarrow}2)\;{\beta}-D-xylopyranosyl]$ quercetin through interpretation of spectral data and adaptation of acid hydrolysis. The $IC_{50}$ value of this compound in rat brain mitochondrial MAO-B inhibitory activity was evaluated to be $8.05\;{\mu}mol/l$.

• Bulletin of the Korean Chemical Society
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• v.32 no.7
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• pp.2428-2432
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• 2011

A series of new 4-aryl-6,8-dimethylpyrimido[4,5-c]pyridazine-5,7(6H,8H)-diones have been synthesized via three component reaction of 1,3-dimethylbarbituric acid with arylglyoxals in the presence of hydrazinium dihydrochloride in ethanol. All of these derivatives may act as potential monoamine oxidase inhibitors.