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Deamination of hordenine by monoamine oxidase and its action on vasa deferentia of the rat.
Barwell, C J; Basma, A N; Lafi, M A; Leake, L D.
Afiliación
  • Barwell CJ; School of Pharmacy, Portsmouth Polytechnic, Hampshire, UK.
J Pharm Pharmacol ; 41(6): 421-3, 1989 Jun.
Article en En | MEDLINE | ID: mdl-2570842
ABSTRACT
The selectivity of the naturally occurring amine, N,N-dimethyltyramine (hordenine) for monoamine oxidase (MAO) and its action upon isolated vasa deferentia of the rat was investigated. Hordenine was deaminated by rat liver MAO with a Michaelis constant of 479 microM and maximum velocity of 128 nmol (mg protein)-1 h-1 compared with 144 microM and 482 nmol (mg protein)-1 h-1 for tyramine. Studies, with selective irreversible inhibitors of MAO, showed that hordenine was a highly selective substrate for MAO-B of liver and that it was not deaminated by the MAO-A of intestinal epithelium. In contrast to tyramine, hordenine did not produce contractions of isolated vasa deferentia. However, 25 microM hordenine potentiated contractile responses of vasa, from control animals, to submaximal doses of noradrenaline and inhibited responses to tyramine. It did not alter responses, to noradrenaline, of vasa denervated by chronic pretreatment of rats with guanethidine. Therefore, it appears that hordenine acted as an inhibitor of noradrenaline uptake, in isolated vasa deferentia. These results indicate that dietary-hordenine is unlikely to be deaminated by intestinal MAO as this is predominantly MAO-A. Consequently, it is likely to be absorbed and could affect the sympathetic nervous system, by virtue of its action as an inhibitor of noradrenaline uptake.
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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Simpatomiméticos / Alcaloides / Monoaminooxidasa / Músculo Liso Límite: Animals Idioma: En Revista: J Pharm Pharmacol Año: 1989 Tipo del documento: Article País de afiliación: Reino Unido
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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Simpatomiméticos / Alcaloides / Monoaminooxidasa / Músculo Liso Límite: Animals Idioma: En Revista: J Pharm Pharmacol Año: 1989 Tipo del documento: Article País de afiliación: Reino Unido
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