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A comparison of GABAC and ρ subunit receptors from the white perch retina

Published online by Cambridge University Press:  02 June 2009

Aohua Qian ,
George Hyatt ,
Andres Schanzer ,
Rohan Hazra ,
Abigail S. Hackam ,
Garry R. Cutting  and
John E. Dowling
Aohua Qian
Affiliation:
Department of Molecular and Cellular Biology, Harvard University, Cambridge
George Hyatt
Affiliation:
Department of Molecular and Cellular Biology, Harvard University, Cambridge
Andres Schanzer
Affiliation:
Department of Molecular and Cellular Biology, Harvard University, Cambridge
Rohan Hazra
Affiliation:
Center for Medical Genetics, Johns Hopkins University School of Medicine, Baltimore
Abigail S. Hackam
Affiliation:
Center for Medical Genetics, Johns Hopkins University School of Medicine, Baltimore
Garry R. Cutting
Affiliation:
Center for Medical Genetics, Johns Hopkins University School of Medicine, Baltimore
John E. Dowling
Affiliation:
Department of Molecular and Cellular Biology, Harvard University, Cambridge
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Abstract

There is increasing evidence that GABAC receptors are composed of GABA ρ subunits. In this study, we compared the properties of native GABAC receptors with those of receptors composed of a GABA ρ subunit. A homologue of the GABA ρ gene was cloned from a white perch (Roccus americana) retinal cDNA library. The clone (perch-s) has an open reading frame of 1422 nucleotide base pairs and encodes a predicted protein of 473 amino acids. It is highly homologous to GABA ρ subunits cloned from human and rat retinas. The receptors (perch-s receptor) expressed by this gene in Xenopus oocytes show properties similar to those of the GABAC receptors present on white perch retinal neurons. GABA induced a sustained response that had a reversal potential of –27.1 +minus; 3.6 mV. The EC50 for the response was 1.74 +− 1.25 μM, a value similar to that reported for GABAC receptors. Pharmacologically, the responses were bicuculline insensitive and not modulated by either diazepam or pentobarbital as is the case for GABAc receptors. There were, however, some distinct differences between native GABAc and perch-s receptors. I4AA acts as a partial agonist on perch-s receptors whereas it is strictly an antagonist on native GABAC receptors. Picrotoxin inhibition is noncompetitive on perch-s receptors, but both competitive and noncompetitive on GABAC receptors. We conclude that GABAC receptors are formed by GABA p subunits but that native GABAc receptors probably consist of a mixture of GABA ρ subunits.

Keywords

GABAC receptorsGABA ρ subunitsWhite perchRetinaGABALigand-gated receptorsHorizontal cells
Type
Research Articles
Information
Visual Neuroscience , Volume 14 , Issue 5 , September 1997 , pp. 843 - 851
Copyright
Copyright © Cambridge University Press 1997

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