Characterization of the binding of [3H]CGP54626 to GABAB receptors in the male bullfrog (Rana catesbeiana).

Abstract:

:Gamma-aminobutyric acid (GABA) is the main inhibitory neurotransmitter in the vertebrate brain. GABA activates both ionotropic (GABA(A)) and metabotropic (GABA(B)) receptors in mammals. Whether non-mammalian vertebrates possess receptors with similar characteristics is not well understood. We used a mammalian GABA(B)-specific antagonist to determine the pharmacology of putative receptors in the brain of an anuran amphibian, the male bullfrog (Rana catesbeiana). Receptor binding assays with the antagonist [(3)H]CGP54626 revealed a single class of high affinity binding sites (with a K(D) of 2.97 nM and a B(max) of 2619 fmol/mg protein). Binding was time- and temperature-dependent, saturable and specific. Specific binding of [(3)H]CGP54626 was inhibited by several mammalian GABA(B) receptor agonists and antagonists. The rank order potency of agonists was: GABA = SKF97541 > (R)-Baclofen > 3-APPA. The rank order for antagonists was: CGP54626 = CGP55845 > CGP52432 > CGP35348. The GABA(A) receptor ligands muscimol and SR95531 had very low affinity for [(3)H]CGP54626 binding sites, while bicuculline compounds had no affinity. Binding of GABA was positively modulated by CGP7930. Taurine did not allosterically modulate GABA binding but did inhibit [(3)H]CGP54626 binding in a linear fashion. Bullfrog brain thus possesses binding sites with significant similarity to mammalian GABA(B) receptors. These receptors differ from mammalian receptors, however, in dissociation kinetics, ligand specificity and allosteric modulation.

journal_name

Brain Res

journal_title

Brain research

authors

Asay MJ,Boyd SK

doi

10.1016/j.brainres.2006.03.008

subject

Has Abstract

pub_date

2006-06-13 00:00:00

pages

76-85

issue

1

eissn

0006-8993

issn

1872-6240

pii

S0006-8993(06)00668-8

journal_volume

1094

pub_type

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