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Titolo:
Inefficient cell-surface expression of hybrid complexes formed by the co-assembly of neuronal nicotinic acetylcholine receptor and serotonin receptorsubunits
Autore:
Harkness, PC; Millar, NS;
Indirizzi:
Univ Coll London, Dept Pharmacol, London WC1E 6BT, England Univ Coll London London England WC1E 6BT macol, London WC1E 6BT, England
Titolo Testata:
NEUROPHARMACOLOGY
fascicolo: 1, volume: 41, anno: 2001,
pagine: 79 - 87
SICI:
0028-3908(200107)41:1<79:ICEOHC>2.0.ZU;2-7
Fonte:
ISI
Lingua:
ENG
Soggetto:
ALPHA-BUNGAROTOXIN RECEPTORS; GATED ION-CHANNEL; FUNCTIONAL EXPRESSION; 5-HT3 RECEPTORS; PHARMACOLOGICAL CHARACTERIZATION; HETEROLOGOUS EXPRESSION; STABLE EXPRESSION; MOLECULAR-CLONING; RAT-BRAIN; ANTIBODIES;
Keywords:
acetylcholine receptor; nicotinic receptor; serotonin receptor; subunit assembly;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
46
Recensione:
Indirizzi per estratti:
Indirizzo: Millar, NS Univ Coll London, Dept Pharmacol, Mortimer St, London WC1E 6BT,England Univ Coll London Mortimer St London England WC1E 6BT , England
Citazione:
P.C. Harkness e N.S. Millar, "Inefficient cell-surface expression of hybrid complexes formed by the co-assembly of neuronal nicotinic acetylcholine receptor and serotonin receptorsubunits", NEUROPHARM, 41(1), 2001, pp. 79-87

Abstract

Previous studies have demonstrated that relatively low levels of alpha4 beta2 neuronal nicotinic acetylcholine receptors (nAChRs) are expressed on the cell surface of transfected mammalian cell lines but that surface expression levels can be dramatically up-regulated by co-expression of these subunits with chimeric subunits containing the N-terminal portion of the neuronal nAChR alpha4 or beta2 subunits together with the C-terminal domain of the5-HT3A subunit. Recent work has also suggested that the nAChR alpha4 subunit can co-assemble in a 'promiscuous' manner with the serotonin receptor 5-HT3A subunit to form functional hybrid receptors. In this study we have examined whether co-assembly of either alpha4 or beta2 with 5-HT3A itself (rather than with the alpha4/5-HT3A or beta2/5-HT3A subunit chimeras) can also facilitate cell surface expression of alpha4 and beta2 subunits in transfected mammalian cells. Evidence has been obtained by immunoprecipitation, cell-surface antibody binding and radioligand binding which indicates that the5-HT3A can co-assemble with both the alpha4 and beta2 nAChR subunits. We conclude, however, that co-assembly of 5-HT3A with either alpha4 or beta2 does not result in efficient cell surface expression of the nAChR subunits and that co-assembled hybrid (nAChR subunit + 5-HT3R subunit) receptor complexes are largely retained within the cell. (C) 2001 Elsevier Science Ltd. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 30/05/20 alle ore 12:56:40