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Titolo:
Thyrotropin releasing hormone (TRH) selectively binds and activates the melanocortin 1 receptor
Autore:
Schioth, HB; Prusis, P; Muceniece, R; Mutulis, F; Mutule, I; Wikberg, JES;
Indirizzi:
Uppsala Univ, Dept Pharmaceut Pharmacol, Uppsala, Sweden Uppsala Univ Uppsala Sweden Dept Pharmaceut Pharmacol, Uppsala, Sweden Latvian Acad Sci, Inst Organ Synth, Pharmacol Lab, LV-226006 Riga, Latvia Latvian Acad Sci Riga Latvia LV-226006 macol Lab, LV-226006 Riga, Latvia Latvian Acad Sci, Inst Organ Synth, Dept Med Chem, LV-226006 Riga, Latvia Latvian Acad Sci Riga Latvia LV-226006 Med Chem, LV-226006 Riga, Latvia
Titolo Testata:
PEPTIDES
fascicolo: 3, volume: 20, anno: 1999,
pagine: 395 - 400
SICI:
0196-9781(1999)20:3<395:TRH(SB>2.0.ZU;2-G
Fonte:
ISI
Lingua:
ENG
Soggetto:
MELANOCYTE-STIMULATING HORMONE; MOLECULAR-CLONING; RADIOLIGAND BINDING; PEPTIDES; SUBTYPES; MSH; IDENTIFICATION; LOCALIZATION; MELANOTROPIN; EXPRESSION;
Keywords:
TRH; melanocortin (MC) receptor subtypes; MSH (melanocyte stimulating hormone); ligand binding; cAMP;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
31
Recensione:
Indirizzi per estratti:
Indirizzo: Schioth, HB Uppsala Univ, Dept Pharmaceut Pharmacol, Uppsala, Sweden Uppsala Univ Uppsala Sweden ceut Pharmacol, Uppsala, Sweden
Citazione:
H.B. Schioth et al., "Thyrotropin releasing hormone (TRH) selectively binds and activates the melanocortin 1 receptor", PEPTIDES, 20(3), 1999, pp. 395-400

Abstract

We tested the endogenous tripeptide TRH (thyrotropin releasing hormone) ability to bind to MC (melanocortin) receptor subtypes. We discovered that TRH binds to the human MC1 receptor expressed in COS cells and to murine B16 melanoma cells with 5790 +/- 1010 nM and 6370 +/- 1260 nM Ki's, respectively. TRH did not bind to the human MC3, MC4 or MC5 receptor subtypes. Moreover, TRH also stimulated cAMP production in murine B16 melanoma cells reaching the same maximum level of cAMP as found for alpha-MSH. However, several analogues of TRH, including TRH-OH, TRH-Gly-NH2 and other analogues, where each of the three amino acid residues in TRH had been exchanged by a relatedresidue, did not bind to any of the MC receptors tested in this study. C alpha atoms of molecular models of TRH and the core of a MSH peptide were aligned with r.m.s. of 0.01 Angstrom. Moreover, TRH could be docked into a binding pocket of a molecular model of the MC1 receptor at only a little higher energy than a short cyclic MSH peptide. The data indicate a similarity in the mode of TRH and MSH activation of the MC1 receptor. (C) 1999 ElsevierScience Inc. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 08/08/20 alle ore 08:16:42