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

doi:10.1016/0922-4106(93)90174-8

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

School of Medicine

Research output: Contribution to journal › Article › peer-review

81 Scopus citations

Abstract

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 I_m 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 language	English (US)
Pages (from-to)	83-84
Number of pages	2
Journal	European Journal of Pharmacology: Molecular Pharmacology
Volume	245
Issue number	1
DOIs	https://doi.org/10.1016/0922-4106(93)90174-8
State	Published - Mar 15 1993

Keywords

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

ASJC Scopus subject areas

Pharmacology

Access to Document

10.1016/0922-4106(93)90174-8

Cite this

@article{2090867de242494eb7efd9f429f7a42c,

title = "GABA ρ2 receptor pharmacological profile: GABA recognition site similarities to ρ1",

abstract = "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.",

keywords = "GABA (γ-aminobutyric acid), GABA ρ receptors, GABA ρ receptors, Inhibitory amino acids, Ligand-gated ion channel, Retina",

author = "Tadashi Kusama and Wang, {Tien Li} and Guggino, {William B.} and Cutting, {Garry R.} and Uhl, {George R.}",

note = "Funding Information: This work was performed by T.K. and G.R.U. using cDNAs constructed and provided by T.L.W., W.B.G. and G.R.C. We thank Dr. James Schaeffer for his generous donation of CAMP and TAMP, Charles Spivak for helpful advice, and the intramural program of the National Institute on Drug Abuse for support of this work.",

year = "1993",

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doi = "10.1016/0922-4106(93)90174-8",

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pages = "83--84",

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T1 - GABA ρ2 receptor pharmacological profile

T2 - GABA recognition site similarities to ρ1

AU - Kusama, Tadashi

AU - Wang, Tien Li

AU - Guggino, William B.

AU - Cutting, Garry R.

AU - Uhl, George R.

N1 - Funding Information: This work was performed by T.K. and G.R.U. using cDNAs constructed and provided by T.L.W., W.B.G. and G.R.C. We thank Dr. James Schaeffer for his generous donation of CAMP and TAMP, Charles Spivak for helpful advice, and the intramural program of the National Institute on Drug Abuse for support of this work.

PY - 1993/3/15

Y1 - 1993/3/15

N2 - 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.

AB - 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.

KW - GABA (γ-aminobutyric acid)

KW - GABA ρ receptors

KW - Inhibitory amino acids

KW - Ligand-gated ion channel

KW - Retina

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