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- W2114117815 abstract "Problem statement: The role of 5-HT has been investigated in many behavioral activities.Thus, studies using raphe lesion showed that 5-HT is involved in sleep, general activity levels,habituation, aggression, pain sensitivity and morphine analgesia, avoidance behavior, self-stimulationand water consumption. Approach: The metabolic interaction between serotonin (5-hydroxytrptamine) and indole-3-aldehyde and xanthine via aldehyde oxidase (EC 1.2.3.1) and xanthineoxidase (EC 1.1.3.22), respectively, were studied in liver tissue homogenate of Dunkin-Hartley guineapigs by following the decrease in substrate concentration using spectrophotometer. Homogenates ofliver were incubated with indole-3-aldehyde in the presence and absence of serotonin or(chlorpromazine and allopurinol a potent and selective inhibitors for aldehyde oxidase and xanthineoxidase, respectively). Oxidation of indole-3-aldehyde to indole-3-acetic acid was reduced up to 63.2%in the presence of serotonin (100 µM), while oxidation of xanthine to uric acid was reduced up to 51.6% under the same conditions. Results: In comparison, incubation of the substrates with their specific inhibitors (100 µM of chlorpromazine and 100 µM allopurinol) give almost complete inhibition. These results demonstrate that in the guinea pig liver a metabolic interaction between serotonin and indole-3-aldehyde or xanthine via molybdenum hydroxylases system may take place in liver, which is the main tissue for xenobiotics detoxification. Conclusion: The overall conclusion from this research is that serotonin could be a protector for neurons and other tissue from the insult of oxidation of aldehydes and xanthines by molybdenum hydroxylases." @default.
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- W2114117815 date "2010-03-01" @default.
- W2114117815 modified "2023-09-27" @default.
- W2114117815 title "<i>In Vitro</i> Interaction of 5-Hydroxytrptamine with Cytosolic Molybdenum Hydroxylases as a Potential Inhibitor for Initial Rates Activities" @default.
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- W2114117815 doi "https://doi.org/10.3844/ajbbsp.2010.181.186" @default.
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