BioDiscovery : Conference Abstract
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Corresponding author: Milena Mishonova (mmishonova@abv.bg)
Received: 21 Jul 2017 | Published: 01 Aug 2017
© 2017 Milena Mishonova, Hristo Gagov
This is an open access article distributed under the terms of the Creative Commons Attribution License (CC BY 4.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Citation: Mishonova M, Gagov H (2017) Testosterone as Diamine Oxidase Activity Regulator. BioDiscovery 20: e17372. https://doi.org/10.3897/biodiscovery.20.e17372
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Diamine oxidase (DAO) is a key enzyme of the metabolism of polyamines. Its activity was assayed in homogenate of male immature rat liver and kidney. The androgens are important regulators of polyamines’ metabolism. It was known that testosterone (T) activates DAO in murine kidney, an effect that might depend on the intracellular level of polyamines. The aim of this research was to study the participation of androgen receptor and ornithine decarboxylase (ODC) in DAO testosterone regulation. The rats were treated i.p. 4 hours before measurements with T, T + Hydroxyflutamide (HF), an androgen receptor antagonist or T + difluoromethylornithine (DFMO), an inhibitor of ODC. It was observed that i) T significantly increased DAO activity of rat liver and kidney; ii) the presence of HF abolished the effect of T ; iii) the presence of DFMO slowly reduced the effect of T on DAO activity. It is concluded that T activates DAO mainly by a mechanism, which includes androgen receptor binding and ODC stimulation.
poliamines, diamine oxidase, sex steroids
Milena Mishonova
World BioDiscovery Congress 2017
This work was supported by Scientific Research Fund, Sofia University project №: 80-10-17/12.04.2017 and
project №: BG05M2OP001-2.009-0019-С01/02.06.2017, supported by Operational Programme "Science and Education for Smart Growth".
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