NDLI: Molecular and Pharmacological Characterization of Native Cortical γ-Aminobutyric AcidA Receptors Containing Both α1 and α3 Subunits

Content Provider	Journal of Biological Chemistry (JBC)
Author	Araujo, Francisco Tan, Suan Ruano, Diego Schoemaker, Hans Benavides, Jesus Vitorica, Javier
Abstract	We have investigated the existence, molecular composition, and benzodiazepine binding properties of native cortical α1-α3 γ-aminobutyric acidA (GABAA) receptors using subunit-specific antibodies.The co-existence of α1 and α3 subunits in native GABAA receptors was demonstrated by immunoblot analysis of the anti-α1- or anti-α3-immunopurified receptors and by immunoprecipitation experiments of the [3H]zolpidem binding activity. Furthermore, immunodepletion experiments indicated that the α1-α3 GABAA receptors represented 54.7 ± 5.0 and 23.6 ± 3.3% of the α3 and α1 populations, respectively. Therefore, α1 and α3 subunits are associated in the same native GABAA receptor complex, but, on the other hand, these α1-α3 GABAA receptors from the cortex constitute a large proportion of the total α3 population and a relatively minor component of the α1 population.The pharmacological analysis of the α1- or α3-immunopurified receptors demonstrated the presence of two different benzodiazepine binding sites in each receptor population with high (type I binding sites) and low (type II binding sites) affinities for zolpidem and Cl 218,872. These results indicate the existence of native GABAA receptors possessing both α1 and α3 subunits, with α1 and α3 subunits expressing their characteristic benzodiazepine pharmacology.The molecular characterization of the anti-α1-anti-α3 double-immunopurified receptors demonstrated the presence of stoichiometric amounts of α1 and α3 subunits, associated with β2/3, and γ2 subunits. The pharmacological analysis of α1-α3 GABAA receptors demonstrated that, despite the fact that each α subunit retained its benzodiazepine binding properties, the relative proportion between type I and II binding sites or between 51- and 59-61-kDa [3H]Ro15-4513-photolabeled peptides was 70:30. Therefore, the α1 subunit is pharmacologically predominant over the α3 subunit. These results indicate the existence of active and nonactive α subunits in the native α1-α3 GABAA receptors from rat cortex.
Related Links	http://www.jbc.org/content/271/44/27902.abstract
Ending Page	27911
Starting Page	27902
Page Count	10
File Format	HTM / HTML PDF
ISSN	00219258
Journal	Journal of Biological Chemistry (JBC)
Issue Number	44
Volume Number	271
DOI	10.1074/jbc.271.44.27902
e-ISSN	1083351X
Language	English
Publisher	American Society for Biochemistry and Molecular Biology
Publisher Date	1996-11-01
Access Restriction	Open
Subject Keyword	Protein Chemistry and Structure
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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