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Abstract

Rat beta 3 subunits expressed in human embryonic kidney 293 cells form high affinity [35S]t-butylbicyclophosphorothionate binding sites modulated by several allosteric ligands of gamma-aminobutyric acid type A receptors.

A Slany, J Zezula, V Tretter and W Sieghart
Molecular Pharmacology September 1995, 48 (3) 385-391;
A Slany
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J Zezula
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V Tretter
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W Sieghart
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Abstract

Human embryonic kidney 293 cells transiently transfected with beta 3 subunits of gamma-aminobutyric acid type A receptors from the rat exhibited a specific high affinity binding for [35S]t-butylbicyclophosphorothionate (TBPS) that could be inhibited by pentobarbital, etazolate, (+)-etomidate, alphaxalone, propofol, chlormethiazole, and Ro 5-4864. The potency of these compounds for inhibition of [35S]TBPS binding was similar in membranes from beta 3 subunit-transfected human embryonic kidney 293 cells and in cerebellar membranes. In contrast to maximally inhibiting concentrations of unlabeled TBPS or picrotoxin, which caused a monophasic and rather slow dissociation of [35S]TBPS, maximally inhibiting concentrations of pentobarbital, etazolate, alphaxalone, propofol, chlormethiazole, and Ro 5-4864 accelerated the dissociation of [35S]TBPS from beta 3 subunit-containing membranes. Immunoaffinity chromatography and Western blot analysis with subunit-specific antibodies indicated that other endogenous subunits possibly present in these cells were not associated with beta 3 subunits. These results appear to indicate that most of the allosteric binding sites present on gamma-aminobutyric acid type A receptors can be formed by the beta subunit of these receptors. Homo-oligomeric beta 3 receptors therefore are an excellent model system for the structural investigation of gamma-aminobutyric acid type A receptors.

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Molecular Pharmacology
Vol. 48, Issue 3
1 Sep 1995
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Abstract

Rat beta 3 subunits expressed in human embryonic kidney 293 cells form high affinity [35S]t-butylbicyclophosphorothionate binding sites modulated by several allosteric ligands of gamma-aminobutyric acid type A receptors.

A Slany, J Zezula, V Tretter and W Sieghart
Molecular Pharmacology September 1, 1995, 48 (3) 385-391;

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Abstract

Rat beta 3 subunits expressed in human embryonic kidney 293 cells form high affinity [35S]t-butylbicyclophosphorothionate binding sites modulated by several allosteric ligands of gamma-aminobutyric acid type A receptors.

A Slany, J Zezula, V Tretter and W Sieghart
Molecular Pharmacology September 1, 1995, 48 (3) 385-391;
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