| Title | The role of aldehyde oxidase on 2-phenylethylamine oxidation by freshly prepared and cryopreserved guinea pig liver slices | |
| Author | Georgios I. Panoutsopoulos
Department of Experimental Pharmacology, Medical School, Athens University, Athens, Greece |
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| Citation | Panoutsopoulos, G.I.: The role of aldehyde oxidase on 2-phenylethylamine oxidation by freshly prepared and cryopreserved guinea pig liver slices, Epitheorese Klin. Farmakol. Farmakokinet. 20(2): 268-269 (2006) | |
| Publication Date | Accepted for publication: 19-20 May 2006 | |
| Full Text Language | English | |
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| Keywords | Aldehyde oxidase, 2-phenylethylamine, oxidation, guinea pig liver slices. | |
| Other Terms | review article | |
| Summary | 2-Phenylethylamine is an endogenous amine, which acts as a neuromodulator of dopaminergic responses. Exogenous 2-Phenylethylamine is found in certain foodstuffs such as cheese, chocolate and wine and has been known to trigger migraine attacks in susceptible individuals. The present investigation examines the metabolism of 2-phenylethylamine to phenylacetic acid, via phenylacetaldehyde, with freshly prepared guinea pig liver slices in the absence/or presence of specific inhibitors for each oxidizing enzyme. The inhibitors used were isovanillin for aldehyde oxidase, allopurinol for xanthine oxidase and disulfiram for aldehyde dehydrogenase. In freshly prepared and cryopreserved liver slices, phenylacetic acid was the main metabolite of 2-phenylethylamine. In freshly prepared liver slices, phenylacetic acid was completely inhibited by disulfiram (inhibitor of aldehyde dehydrogenase), whereas isovanillin (inhibitor of aldehyde oxidase) inhibited acid formation to a lesser extent and allopurinol (inhibitor of xanthine oxidase) had no effect. In cryopreserved liver slices, isovanillin inhibited phenylacetic acid by 85%, whereas disulfiram inhibited acid formation to a lesser extent and allopurinol had no effect. The results in this study have shown that, in freshly prepared and cryopreserved liver slices, 2-phenylethylamine is converted to phenylacetic acid, via phenylacetaldehyde, by both aldehyde dehydrogenase and aldehyde oxidase with no contribution from xanthine oxidase. Therefore, aldehyde dehydrogenase is not the only enzyme responsible in the metabolism of the intermediate phenylacetaldehyde, but also aldehyde oxidase has a prominent role in this metabolism. | |
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Online ISSN 1011-6575
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