The modulatory effects of the anxiolytic etifoxine on GABAA receptors are mediated by the β subunit

  title={The modulatory effects of the anxiolytic etifoxine on GABAA receptors are mediated by the $\beta$ subunit},
  author={Alain Hamon and Alain Morel and Bernard Hue and Marc Verleye and Jean-marie Gillardin},

The Non-Benzodiazepine Anxiolytic Drug Etifoxine Causes a Rapid, Receptor-Independent Stimulation of Neurosteroid Biosynthesis

It is demonstrated that etifoxine stimulates neurosteroid production through a membrane receptor-independent mechanism, and the stimulatory effects of et ifoxine and the triakontatetraneuropeptide TTN were additive, indicating that these two compounds act through distinct mechanisms.

Limiting Activity at β1-Subunit-Containing GABAA Receptor Subtypes Reduces Ataxia

These findings provide an alternative strategy for designing anxioselective allosteric modulators of the GABAAR with BZ-like anxiolytic efficacy by reducing or eliminating activity at β1-subunit-containing GABAARs.

GABAA Receptor Subunit Composition Drives Its Sensitivity to the Insecticide Fipronil

Data show that FPN action is driven by the subunit composition of GABAARs—highlighting the role of the complementary subunit—and thus their localization within a physiological synapse, and has important significance for its toxicity on the mammalian nervous system, especially in acute exposure.



Interactions of etifoxine with the chloride channel coupled to the GABA(A) receptor complex.

Findings suggest that etifoxine exerts its effect by interacting with the Cl- channel of GABA(A) receptors and probably by facilitating GABAergic inhibition.

Subunit‐dependent interaction of the general anaesthetic etomidate with the γ‐aminobutyric acid type A receptor

It is concluded that the subtype of β‐subunit influences the potency with which etomidate potentiates GABA‐evoked currents and that the β isoform is a crucial determinant of the GABA‐mimetic activity of this compound.

The agonistic action of pentobarbital on GABAA β‐subunit homomeric receptors

The difference in the agonistic action of intravenous anaesthetics among these highly homologous β-subunits suggests that theβ-subunit homomeric receptors may be useful to further define the molecular sites of action of injectable general anesthetics and other functional domains on GABAA receptors.

Subunit‐selective modulation of GABAA receptors by the non‐steroidal anti‐inflammatory agent, mefenamic acid

Molecular comparisons of MFA, loreclezole and etomidate, agents which exhibit similar selectivity for GABAA receptors, revealed their ability to adopt similar structural conformations and indicates that N290 in TM2 of β2 and β3 subunits is important for the regulation of GAB AA receptor function by MFA.