• Corpus ID: 20062422

Potentiation of gamma-aminobutyric acid-induced chloride currents by various benzodiazepine site agonists with the alpha 1 gamma 2, beta 2 gamma 2 and alpha 1 beta 2 gamma 2 subtypes of cloned gamma-aminobutyric acid type A receptors.

@article{Im1993PotentiationOG,
  title={Potentiation of gamma-aminobutyric acid-induced chloride currents by various benzodiazepine site agonists with the alpha 1 gamma 2, beta 2 gamma 2 and alpha 1 beta 2 gamma 2 subtypes of cloned gamma-aminobutyric acid type A receptors.},
  author={Haesook K. Im and Wha Bin Im and Beverly J. Hamilton and Donald B. Carter and Philip F. Vonvoigtlander},
  journal={Molecular pharmacology},
  year={1993},
  volume={44 4},
  pages={
          866-70
        }
}
Previous studies with cloned gamma-aminobutyric acid type A receptors expressed in human embryonic kidney cells have indicated that the alpha 1 beta 2 gamma 2 and alpha 1 gamma 2 (but not alpha 1 beta 2) subtypes have benzodiazepine sites. We found in this study that even the beta 2 gamma 2 subtype displays gamma-aminobutyric acid-induced Cl- currents that are potentiated by triazolam (a triazolobenzodiazepine). The maximal efficacy of the drug among the subtypes was highest with the alpha 1… 
Mutagenesis of the rat alpha1 subunit of the gamma-aminobutyric acid(A) receptor reveals the importance of residue 101 in determining the allosteric effects of benzodiazepine site ligands.
TLDR
The results indicate that the characteristics of the residue at position 101 of the alpha1 subunit play a crucial role in determining the efficacy of benzodiazepine-site ligands.
Molecular dissection of benzodiazepine binding and allosteric coupling using chimeric gamma-aminobutyric acidA receptor subunits.
TLDR
Two gamma2 subunit regions required for BZD binding that are distinct from domain or domains responsible for allosteric coupling of the BZd and GABA binding sites are identified by using gamma/alpha chimeras.
Mutagenesis of the Rat α1 Subunit of the γ-Aminobutyric AcidA Receptor Reveals the Importance of Residue 101 in Determining the Allosteric Effects of Benzodiazepine Site Ligands
TLDR
The results indicate that the characteristics of the residue at position 101 of the α1 subunit play a crucial role in determining the efficacy of benzodiazepine-site ligands.
Chloride Channel Expression with the Tandem Construct of α6-β2 GABAA Receptor Subunit Requires a Monomeric Subunit of α6 or γ2 (*)
TLDR
Data from a tandem construct of the α6 and β2 subunit cDNAs are consistent with the view that the polypeptides arising from the tandem construct were expressed with the high affinity GABA site, but unable to form GABA channels.
Two Tyrosine Residues on the α Subunit Are Crucial for Benzodiazepine Binding and Allosteric Modulation of γ-Aminobutyric Acid A Receptors
TLDR
Structural determinants required for the actions of the BZ diazepam (dzp) on recombinant α1β2γ2 GABAA receptors are investigated and it is suggested that Tyr159 and Tyr209 of the α1 subunit may be components ofThe BZ-binding site on α1 β-aminobutyric acid (GABA) receptors.
The diversity of GABAA receptors
TLDR
The pharmacology of putative receptor isoforms is summarized and the characteristics of functional channels are emphasized to further the understanding of GABA-related disorders and of the complex interaction of excitatory and inhibitory mechanisms in neuronal processing.
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