Differential modulation of human GABA_C-ρ1 receptor by sulfur-containing compounds structurally related to taurine.

ABSTRACT:

Background

The amino acid taurine (2-Aminoethanesulfonic acid) modulates inhibitory neurotransmitter receptors. This study aimed to determine if the dual action of taurine on GABA_C-ρ1R relates to its structure. To address this, we tested the ability of the structurally related compounds homotaurine, hypotaurine, and isethionic acid to modulate GABA_C-ρ1R.

Results

In Xenopus laevis oocytes, hypotaurine and homotaurine partially activate heterologously expressed GABA_C-ρ1R, showing an increment in its deactivation time with no changes in channel permeability, whereas isethionic acid showed no effect. Competitive assays suggest that hypotaurine and homotaurine compete for the GABA-binding site. In addition, their effects were blocked by the ion-ch

SUBMITTER: Ochoa-de la Paz LD 

PROVIDER: S-EPMC6076408 | biostudies-literature | 2018 Aug

REPOSITORIES: biostudies-literature