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Journal articles
Isolation and characterization of an endogenous peptide from rat brain interacting specifically with the serotoninergic 1B receptor subtypes
Abstract : The existence of endogenous compounds interacting with the serotonergic system was previously postulated. In the present work, rat brain tissues were extracted by acidic and organic procedures. The resulting extract was tested for its capacity to interact with the binding of [3H]5-hydroxytryptamine ([3H]5-HT) to 5-HT1 receptors. Compounds responsible for the observed inhibitory activities were isolated and purified by high pressure liquid chromatography.
A tetrapeptide corresponding to a novel amino acid sequence Leu-Ser-Ala-Leu (LSAL) was identified. It reduces the binding of [3H]5-HT to 5-HT1 receptors at low concentration (IC50 = 10−10M). This effect corresponds to a specific interaction at 5-HT1B receptors since LSAL does not significantly affect other neurotransmitter bindings. LSAL appears heterogeneously distributed throughout the brain (hippocampus > cerebellum > striatum > brain stem) and in peripheral tissues (kidney > lung > stomach > blood > liver > spleen).
Two other peptides, Leu-Ser (LS) and Ala-Leu (AL), were also purified. They hardly affected [3H]5-HT binding compared with LSAL. They presumably represent degradation products of the functional peptide LSAL. The fact that LSAL interacts specifically with 5-HT1B receptors that inhibit the release of neurotransmitters and particularly that of 5-HT itself suggests that this peptide may be involved in mechanisms controlling 5-HT neurotransmission and, accordingly, may play an important role in pathophysiological functions related to 5-HT activity.
https://hal-pasteur.archives-ouvertes.fr/pasteur-00376428
Contributor : Cécile Roux <>
Submitted on : Friday, April 17, 2009 - 2:47:50 PM
Last modification on : Monday, January 13, 2020 - 5:08:14 PM
Contributor : Cécile Roux <>
Submitted on : Friday, April 17, 2009 - 2:47:50 PM
Last modification on : Monday, January 13, 2020 - 5:08:14 PM
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