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Titolo:
SPECIFIC INTERACTION OF 5-HT-MODULINE WITH HUMAN 5-HT1B AS WELL AS 5-HT1D RECEPTORS EXPRESSED IN TRANSFECTED CULTURED-CELLS
Autore:
ROUSSELLE JC; PLANTEFOL M; FILLION MP; MASSOT O; PAUWELS PJ; FILLION G;
Indirizzi:
INST PASTEUR,UNITE PHARMACOL NEUROIMMUNOENDOCRINIENNE,28 RUE DR ROUX F-75724 PARIS 15 FRANCE INST PASTEUR,UNITE PHARMACOL NEUROIMMUNOENDOCRINIENNE F-75724 PARIS 15 FRANCE CTR RECH PIERRE FABRE,DEPT CELLULAR & MOL NEUROBIOL F-81106 CASTRES FRANCE
Titolo Testata:
Naunyn-Schmiedeberg's archives of pharmacology
fascicolo: 3, volume: 358, anno: 1998,
pagine: 279 - 286
SICI:
0028-1298(1998)358:3<279:SIO5WH>2.0.ZU;2-Y
Fonte:
ISI
Lingua:
ENG
Soggetto:
GUINEA-PIG; ACETYLCHOLINE-RELEASE; FRONTAL-CORTEX; BINDING-SITES; RODENT BRAIN; 5-HYDROXYTRYPTAMINE; RAT; AUTORECEPTORS; SEROTONIN; HIPPOCAMPUS;
Keywords:
5-HT MODULINE; 5-HT1B RECEPTORS; 5-MT1D RECEPTORS; ALLOSTERIC MODULATOR; ENDOGENOUS PEPTIDE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
39
Recensione:
Indirizzi per estratti:
Citazione:
J.C. Rousselle et al., "SPECIFIC INTERACTION OF 5-HT-MODULINE WITH HUMAN 5-HT1B AS WELL AS 5-HT1D RECEPTORS EXPRESSED IN TRANSFECTED CULTURED-CELLS", Naunyn-Schmiedeberg's archives of pharmacology, 358(3), 1998, pp. 279-286

Abstract

5-HT1B receptors are the predominant auto- and heteroreceptors located on serotonergic and non-serotonergic terminals where they regulate the neuronal release of neurotransmitters. 5-HT-moduline (Leu-Ser-Ala-Leu) has been shown to specifically interact with a very high apparent affinity and in a non-competitive manner with 5-HT1B receptors (Massotet al. 1996; Rousselle et al. 1996). Using transfected cells expressing either 5-HT1B or 5-HT1D receptors, it was shown that 5-HT-moduline prevents the binding of [H-3]5-HT to 5-HT1B as well as to 5-HT1D receptors with similar biochemical characteristics: the IC50 of the peptidewas 1.2x10(-12) M for 5-MT1B and 9x10(-13) M for 5-HT1D receptors. The observed effect corresponds to a marked decrease of the maximal binding for [H-3]5-HT on 5-HT1B (-51.2+/-1%) as well as 5-HT1D binding (-47.2+/-7.7% of the control binding) whereas the affinity of 5-HT is increased by a factor close to 3. No effect is observed using the ''scrambled'' peptide (Ala-Leu-Leu-Ser). Parallel assays using transfected cells expressing 5-HT1A or 5-ht(6) receptors did not show any significant change induced by the peptide under similar assay conditions. The interaction of the peptide was also studied on the functional activity related to the stimulation of the receptors as measured by the increasein [S-35]GTP gamma S binding reflecting the coupling of the receptor to the G-protein. 5-HT-moduline yields an antagonistic effect on the 5-HT induced coupling with a corresponding IC50=1.2+/-0.7x10(-12) M for5-HT1B and 9.8+/-4.0x10(-12) M for 5-HT1D receptors, respectively. The present results demonstrate that 5-HT-moduline interacts with 5-HT1Das well as 5-HT1B receptors and possesses a non-competitive antagonistic activity, likely corresponding to its role of endogenous allosteric modulator, specific for both 5-HT1B and 5-HT1D receptors.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 03/04/20 alle ore 03:08:21