Tele-methylhistamine is a specific MAO B substrate in man |
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Authors: | J. D. Elsworth Vivette Glover M. Sandler |
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Affiliation: | (1) Bermard Baron Memorial Research Laboratories and Institute of Obstetrics and Gynaecology, Queen Charlotte's Maternity Hospital, W6 0XG London, UK;(2) Present address: Neuropsychopharmacology Research Unit, Yale University School of Medicine, 333 Cedar Street, 06510 New Haven, CT, USA |
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Abstract: | Tele-methylhistamine, the first metabolite of histamine in tissues which lack diamine oxidase, is shown to be a substrate for human MAO B. Human liver homogenates were incubated with 3H-tele-methylhistamine and the products separated using thinlayer chromatography. The major product was 3-methylimidazoleacetic acid, the oxidatively deaminated metabolite of tele-methylhistamine. The reaction was inhibited by low concentrations of (-)deprenyl, the specific MAO B inhibitor. Tele-methylhistamine was also found to inhibit competitively the oxidation of phenylethylamine, but not that of 5-hydroxytryptamine, providing further evidence that it is oxidized by MAO B itself and not a related enzyme. This finding implies that (-)deprenyl and other MAO inhibitors used clinically may interfere with histamine metabolism. |
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Keywords: | Tele-methylhistamine MAO B Deprenyl |
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