Chicken GABAA receptor β4 subunits form robust homomeric GABA-gated channels in Xenopus oocytes

S C Liu; L Parent; Robert J Harvey; M G Darlison; E M Barnes Jr

doi:10.1016/S0014-2999(98)00453-1

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Chicken GABAA receptor β4 subunits form robust homomeric GABA-gated channels in Xenopus oocytes

Journal article

Peer reviewed

Chicken GABAA receptor β4 subunits form robust homomeric GABA-gated channels in Xenopus oocytes

S C Liu, L Parent, Robert J Harvey, M G Darlison and E M Barnes Jr

European Journal of Pharmacology, Vol.354(2-3), pp.253-259

1998

DOI: https://doi.org/10.1016/S0014-2999(98)00453-1

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Abstract

allosteric modulation

β4 subunit

chicken

GABAA receptor

homomeric receptor

xenopus oocyte

Chicken GABA(A) receptor β4L and β4S subunits were expressed in Xenopus oocytes by cRNA injection. Oocytes expressing either β4 subunit alone or in combination with the chicken α1 subunit were studied using the two-electrode voltage-clamp technique. Both the β4L and β4S subunits form homomeric GABA-gated Cl- channels with similar efficiencies. In comparison, oocytes expressing either the chicken α1 or β2S polypeptide show no or barely detectable GABA responses, as reported by others for most single-subunit vertebrate GABA(A) receptors. The GABA-gated currents due to the β4L-subunit homomer were not affected by the presence of actinomycin D during cRNA expression, indicating that nascent oocyte polypeptides are not required for channel formation. The homomeric β4L-subunit receptors show high affinity for GABA with an EC50 value of 4.3±0.4 μM and a Hill coefficient of 1.1±0.1 (n=6). In response to GABA application at the EC25 value, currents elicited from the β4L-subunit receptor are enhanced by 50 μM pentobarbital (110±10%, n=3) and 10 μM loreclezole (60±3%, n=3), inhibited by 10 μM picrotoxinin (93±3%, n=3), but not affected by 1 μM diazepam. These properties are similar to those found for oocytes expressing heteromeric chicken α1β4L and α1β2S receptors. Since the β subunits of GABA(A) receptors provide essential determinants for receptor assembly and subcellular localization, homomeric β4-subunit receptors are a useful model system for further study of the structure and function of GABA(A) receptors. Copyright (C) 1998 Elsevier Science B.V.

Details

Title: Chicken GABAA receptor β4 subunits form robust homomeric GABA-gated channels in Xenopus oocytes
Authors: S C Liu (Author) - Baylor College of Medicine, United States
L Parent (Author) - Baylor College of Medicine, United States
Robert J Harvey (Author) - Universität Hamburg, Germany
M G Darlison (Author) - Universität Hamburg, Germany
E M Barnes Jr (Author) - Baylor College of Medicine, United States
Publication details: European Journal of Pharmacology, Vol.354(2-3), pp.253-259
Publisher: Elsevier BV
Date published: 1998
DOI: 10.1016/S0014-2999(98)00453-1
ISSN: 0014-2999
Organisation Unit: School of Health; University of the Sunshine Coast, Queensland; School of Health and Sport Sciences - Legacy; Centre for Bioinnovation; School of Health and Behavioural Sciences - Legacy
Language: English
Record Identifier: 99451180602621
Output Type: Journal article

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