<abstract xmlns="http://www.w3.org/1999/xhtml"><p>Agmatine has been functionally characterized as an important hormone and co-neurotransmitter in mammals. Given its ability in binding Imidazoline sites, a regolatory site of monoaminoxydase, it has been suggested to be involved in many neurological aspects. However, its inhibitory effect on this enzyme still remains an unanswered question. This present study is aimed to asses whether different experimental conditions could affect the agmatine action on monoaminoxydase activity. We demonstrate that the monoaminoxydase inhibition by agmatine is obtained under alkaline conditions and a long time of incubation. No inhibitiory action was found for shorter times of reaction at elevated pH, or at neutral condition and long time of incubation. No inhibition was also detected by substituting the monoamineoxydase substrate tyramine with kynuramine, however, while in these conditions a remarkable inhibition was shown by two aminoxydase inhibitors tranylcypromine and idazoxan. Herein, we discuss a mechanism model and the functional consequences of agmatine action on monoaminoxydase.</p></abstract>

Agmatine has been functionally characterized as an important hormone and co-neurotransmitter in mammals. Given its ability in binding Imidazoline sites, a regolatory site of monoaminoxydase, it has been suggested to be involved in many neurological aspects. However, its inhibitory effect on this enzyme still remains an unanswered question. This present study is aimed to asses whether different experimental conditions could affect the agmatine action on monoaminoxydase activity. We demonstrate that the monoaminoxydase inhibition by agmatine is obtained under alkaline conditions and a long time of incubation. No inhibitiory action was found for shorter times of reaction at elevated pH, or at neutral condition and long time of incubation. No inhibition was also detected by substituting the monoamineoxydase substrate tyramine with kynuramine, however, while in these conditions a remarkable inhibition was shown by two aminoxydase inhibitors tranylcypromine and idazoxan. Herein, we discuss a mechanism model and the functional consequences of agmatine action on monoaminoxydase.

Inhibitory effects of agmatine on monoamine oxidase (MAO) activity: Reconciling the discrepancies

Department of Chemistry, Biology and Biotechnologies

The EuroBiotech Journal

This work is licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 3.0 License.

Agmatine has been functionally characterized as an important hormone and co-neurotransmitter in mammals. Given its ability in binding Imidazoline sites, a...

Inhibitory effects of agmatine on monoamine oxidase (MAO) activity: Reconciling the discrepancies

Article Category: Research Article

Publié en ligne: 25 avr. 2018

Pages: 121 - 127

DOI: https://doi.org/10.2478/ebtj-2018-0016

Mots clés
Agmatine, MAO inhibition, imidizoline receptors, co-neurotransmitters and neurological disorders

© 2018 Loretta Mancinelli, Francesco Ragonese, Samuela Cataldi, Maria Rachele Ceccarini, Rossana G. Iannitti, Cataldo Arcuri, Bernard Fioretti, published by Sciendo

This work is licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 3.0 License.

Inhibitory effects of agmatine on monoamine oxidase (MAO) activity: Reconciling the discrepancies

Article Category: Research Article

Publié en ligne: 25 avr. 2018

Pages: 121 - 127

DOI: https://doi.org/10.2478/ebtj-2018-0016

Mots clésAgmatine, MAO inhibition, imidizoline receptors, co-neurotransmitters and neurological disorders

© 2018 Loretta Mancinelli, Francesco Ragonese, Samuela Cataldi, Maria Rachele Ceccarini, Rossana G. Iannitti, Cataldo Arcuri, Bernard Fioretti, published by Sciendo

This work is licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 3.0 License.

Mots clés
Agmatine, MAO inhibition, imidizoline receptors, co-neurotransmitters and neurological disorders