Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
The influence exerted by the beta 3 subunit on MVIIA omega-conotoxin binding to neuronal N-type calcium channels
Autore:
Luchian, T;
Indirizzi:
Alexandru I Cuza Univ, Dept Biophys & Med Phys, Fac Phys, R-6600 Iasi, Romania Alexandru I Cuza Univ Iasi Romania R-6600 Fac Phys, R-6600 Iasi, Romania
Titolo Testata:
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES
fascicolo: 2, volume: 1512, anno: 2001,
pagine: 329 - 334
SICI:
0005-2736(20010606)1512:2<329:TIEBTB>2.0.ZU;2-F
Fonte:
ISI
Lingua:
ENG
Soggetto:
DEPENDENT CA2+ CHANNELS; ION PERMEATION; DIVERSITY; POTENTIATION; DETERMINANTS; EXPRESSION; GVIA;
Keywords:
Neuronal calcium channel; Xenopus oocyte; omega-conotoxin; two-electrode voltage clamp;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
25
Recensione:
Indirizzi per estratti:
Indirizzo: Luchian, T Alexandru I Cuza Univ, Dept Biophys & Med Phys, Fac Phys, Blvd Carol I 11,R-6600 Iasi, Romania Alexandru I Cuza Univ Blvd Carol I 11 IasiRomania R-6600 ania
Citazione:
T. Luchian, "The influence exerted by the beta 3 subunit on MVIIA omega-conotoxin binding to neuronal N-type calcium channels", BBA-BIOMEMB, 1512(2), 2001, pp. 329-334

Abstract

In the present study, two-electrode voltage-clamp techniques have been used to assess the interaction between the MVIIA omega -conotoxin and an isoform of the N-type Ca2+ channel alpha subunit (alpha (1B-d)). Cloned alpha (1B-d) Ca2+ channels were expressed in Xenopus laevis oocytes in the presenceand absence of the beta (3) subunit. Coexpression of the beta (3) subunit significantly shifted the IC50 value for MVIIA inhibition of central N-typeCa2+ channel current. Analysis of the peak conductance vs. depolarising voltage dependence suggested that the beta (3) subunit has no apparent effecton the gating charge which accompanies the closed-open transition of the channels. Instead, coexpression of the beta (3) subunit led to an approx. 10mV shift to more hyperpolarised potentials in the voltage-dependent activation of N-type Ca2+ channels. We conclude that MVIIA alters the surface charge on the N-type Ca2+ channels and might induce allosteric changes on the structure of the channel, leading to an increase in the dissociation constant of MVIIA binding. (C) 2001 Elsevier Science B.V. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 29/09/20 alle ore 03:51:24