Chapter title |
Endogenous oxidized indoles share inhibitory potency against [3H]isatin binding in rat brain.
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Chapter number | 4 |
Book title |
Neuropsychiatric Disorders An Integrative Approach
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Published in |
Journal of neural transmission Supplementum, January 2007
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DOI | 10.1007/978-3-211-73574-9_4 |
Pubmed ID | |
Book ISBNs |
978-3-21-173573-2, 978-3-21-173574-9
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Authors |
M. Crumeyrolle-Arias, A. Medvedev, A. Cardona, M.-C. Tournaire, V. Glover, Crumeyrolle-Arias, M., Medvedev, A., Cardona, A., Tournaire, M.-C., Glover, V. |
Abstract |
Isatin is an endogenous oxidized indole that influences a range of processes in vivo and in vitro. It has a distinct and discontinuous distribution in the brain and [3H]isatin binding sites are widely distributed in rat brain sections. The highest labelling is found in hypothalamic nuclei and in the cortex, hippocampus, and cerebellum (Crumeyrolle-Arias et al., 2003). However, the properties of most isatin binding sites and their physiological ligands remain unknown. In the present study the effects of three endogenous oxidized indoles (oxindole, 5-hyxdoxyoxindole, and isatin) on [3H]isatin binding were investigated in rat brain sections. In most regions cold isatin (0.2 mM) significantly reduced [3H]isatin binding. In addition to isatin, the other endogenous oxidized indoles, 5-hydroxyoxindole and oxindole were effective in displacing [3H]isatin. Total irreversible inhibition of monoamine oxidases caused inhibition of specific [3H]isatin binding in 7 of 10 brain region studied. This was accompanied by altered sensitivity of [3H]isatin binding to these indoles, including regions where a decrease of specific binding was not detected. The combinations of the three oxidized indoles produced two clear effects: augmentation (potentiation) and attenuation (blockade) of inhibitory activity compared with the independent effects of these compounds. The different effects of oxidized indoles and their combinations (isatin + 5-hydroxyoxindole and isatin + oxindole) in various brain regions therefore suggest an interaction of [(3H]isatin with different and multiple isatin-binding sites, which exhibit different sensitivity to endogenous oxidizing indoles. |
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