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Titolo:
LABELING OF CRF1 AND CRF2 RECEPTORS USING THE NOVEL RADIOLIGAND, [H-3] UROCORTIN
Autore:
GOTTOWIK J; GOETSCHY V; HENRIOT S; KITAS E; FLUHMAN B; CLERC RG; MOREAU JL; MONSMA FJ; KILPATRICK GJ;
Indirizzi:
F HOFFMANN LA ROCHE & CO LTD,DIV PHARMA CH-4070 BASEL SWITZERLAND F HOFFMANN LA ROCHE & CO LTD,DIV PHARMA CH-4070 BASEL SWITZERLAND
Titolo Testata:
Neuropharmacology
fascicolo: 10, volume: 36, anno: 1997,
pagine: 1439 - 1446
SICI:
0028-3908(1997)36:10<1439:LOCACR>2.0.ZU;2-H
Fonte:
ISI
Lingua:
ENG
Soggetto:
CORTICOTROPIN-RELEASING FACTOR; RAT-BRAIN; IDENTIFICATION; BINDING; CLONING; HEART; EXPRESSION; SAUVAGINE; UROCORTIN; PROTEIN;
Keywords:
[H-3] UROCORTIN; CRF; CRH; CRF1 RECEPTORS; CRF2 RECEPTORS;
Tipo documento:
Article
Natura:
Periodico
Citazioni:
21
Recensione:
Indirizzi per estratti:
Citazione:
J. Gottowik et al., "LABELING OF CRF1 AND CRF2 RECEPTORS USING THE NOVEL RADIOLIGAND, [H-3] UROCORTIN", Neuropharmacology, 36(10), 1997, pp. 1439-1446

Abstract

The binding of the novel radioligand, [H-3]-rat urocortin to homogenates of rat cerebellum and homogenates of cells stably transfected withthe human CRF1, rat CRF2 alpha and rat CRF2 beta receptors was examined. In each case, specific reversible high affinity binding was observed (K(d)s between 0.18 and 0.31 nM). The density of sites was relatively low in the cerebellum (9 fmol/mg tissue) but high in the recombinant systems with expression levels of between 1.4 and 6.3 pmol/mg protein. Agents known to interact with CRF receptors potently competed for binding in each case. The pharmacological profile of binding to the recombinant receptors were consistent with data previously published using other radioligands. Thus, for the recombinant CRF1 receptor, bindingwas inhibited with similar affinity by Urocortin, sauvagine, Urotensin 1 and CRF. The non-peptidic CRF antagonists (e.g. CP 154,526 and SC 241) also potently inhibited binding. The CRF2 alpha, and CRF2 beta receptor recombinant systems had a very similar pharmacological profile with a clear rank order of potency for the peptide ligands (Urocortin > Sauvagine > Urotensin 1 > CRF), whereas the non-peptide CRF receptorantagonists had no measurable affinity. The pharmacological profile of specific [H-3]-urocortin binding to homogentates of rat cerebellum was consistent with specific labelling of a CRF1 receptor. We conclude that [H-3]-urocortin is a useful tool for the study of CRF receptors with the advantages that a filtration assay can be used, all CRF receptors can be labelled with the same ligand and the benefits associated with the low energy emitter, H-3. (C) 1997 Elsevier Science Ltd.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 29/01/20 alle ore 19:21:38