Format

Send to

Choose Destination
Proc Natl Acad Sci U S A. 2004 Mar 2;101(9):3220-3. Epub 2004 Feb 23.

Expression of functional receptors by the human gamma-aminobutyric acid A gamma 2 subunit.

Author information

1
Laboratory of Cellular and Molecular Neurobiology, Department of Neurobiology and Behavior, University of California, McGaugh Hall 1115, Irvine, CA 92697-4550, USA. ataulfo@calli.cnb.unam.mx

Abstract

gamma-Aminobutyric acid A (GABA(A)) receptors are heteromeric membrane proteins formed mainly by various combinations of alpha, beta, and gamma subunits; and it is commonly thought that the gamma 2 subunit alone does not form functional receptors. In contrast, we found that cDNA encoding the gamma 2L subunit of the human GABA(A) receptor, injected alone into Xenopus oocytes, expressed functional GABA receptors whose properties were investigated by using the two-microelectrode voltage-clamp technique. GABA elicited desensitizing membrane currents that recovered after a few minutes' wash. Repetitive applications of GABA induced a "run-up" of GABA currents that nearly doubled the amplitude of the first response. The GABA currents inverted direction at about -30 mV, indicating that they are carried mainly by Cl(-) ions. The homomeric gamma 2L receptors were also activated by beta-alanine > taurine > glycine, and, like some types of heteromeric GABA(A) receptors, the gamma 2L receptors were blocked by bicuculline and were potentiated by pentobarbital and flunitrazepam. These results indicate that the human gamma 2L subunit is capable of forming fully functional GABA receptors by itself in Xenopus oocytes and suggest that the roles proposed for the various subunits that make up the heteromeric GABA(A) receptors in situ require further clarification.

PMID:
14981251
PMCID:
PMC365770
DOI:
10.1073/pnas.0308682101
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for HighWire Icon for PubMed Central
Loading ...
Support Center