GABA ρ2 receptor pharmacological profile: GABA recognition site similarities to ρ1

Tadashi Kusama, Tien Li Wang, William B. Guggino, Garry R. Cutting, George R. Uhl

Research output: Contribution to journalArticlepeer-review


The ρ2 receptor for γ-aminobutyric acid (GABA) induces GABA-gated currents when expressed as a homooligomer in Xenopus oocytes. ρ2 responses display pharmacological profiles similar to those of expressed ρ1 receptors, although responses were slower, most agonists were more potent at ρ2 and Im values for the partial agonist imidazole-4-acetic acid were 7-fold higher. Amino acids important for most aspects of GABA agonist ligand recognition may not be among those that differ between ρ1 and ρ2, including the 20% amino acid difference in the N-terminal region.

Original languageEnglish (US)
Pages (from-to)83-84
Number of pages2
JournalEuropean Journal of Pharmacology: Molecular Pharmacology
Issue number1
StatePublished - Mar 15 1993


  • GABA (γ-aminobutyric acid)
  • GABA ρ receptors
  • GABA ρ receptors
  • Inhibitory amino acids
  • Ligand-gated ion channel
  • Retina

ASJC Scopus subject areas

  • Pharmacology


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