Inhibition of Type A and Type B Monoamine Oxidase by Isogentisin and its 3-O-Glucoside
- 1 May 1980
- journal article
- research article
- Published by Georg Thieme Verlag KG in Planta Medica
- Vol. 39 (05) , 19-23
- https://doi.org/10.1055/s-2008-1074899
Abstract
Isogentisin and its 3-O-glucoside were found to inhibit monoamine oxidase (MAO) in rat brain mitochondria in vitro using 5-hydroxytryptamine (5-HT) and (3-phenylethylamine (PEA) as relatively specific substrates for type A and type B MAO, respectively. Isogentisin showed much more potent MAO inhibition than its 3-O-glucoside for both substrates. The inhibition by both compounds was fully competitive for both substrates. Both compounds were found to be almost nonselective inhibitors for type A and type B MAO. popular medicine both in Europe and Asia due to their unique actions on the central nervous system [2]. In our previous preliminary communication [3], we briefly reported that isogentisin and its 3-O-glucoside inhibit monoamine oxidase (MAO) in vitro using kynuramine as substrate. Since mitochondrial MAO is believed to exist in many animal tissues in two functional forms called type A and type B [4-6], in the present paper we have studied MAO inhibition by isogentisin and its 3-O-glucoside using 5-hydroxytryptamine (5-HT) and (3-phenylethylamine (PEA) as relatively specific substrates for type A and type B MAO, respectively.Keywords
This publication has 6 references indexed in Scilit:
- Deamination of 5-methoxytryptamine, serotonin and phenylethylamine by rat MAO in vitro and in vivoLife Sciences, 1978
- Inhibition of monoamine oxidase by isogentisin and its 3-0-glucosideBiochemical Pharmacology, 1978
- Monoamine oxidase in developing chick retinaBrain Research, 1977
- Xanthone glycosidesPhytochemistry, 1977
- A simple micro-determination of type B monoamine oxidaseBiochemical Pharmacology, 1976
- MICRODETERMINATION OF MONOAMINE OXIDASE AND 5‐HYDROXYTRYPTOPHAN DECARBOXYLASE ACTIVITIES IN NERVOUS TISSUESJournal of Neurochemistry, 1965