Structural requirements for activation of the glycine receptor that modulates the N-methyl-D-aspartate operated ion channel

Lawrence D. Snell; Robert S. Morter; Kenneth M. Johnson

doi:10.1016/0014-2999(88)90152-5

Structural requirements for activation of the glycine receptor that modulates the N-methyl-D-aspartate operated ion channel

Lawrence D. Snell
, Robert S. Morter
, Kenneth M. Johnson

Pharmacology & Toxicology

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

107 Scopus citations

Abstract

It has recently been demonstrated that glycine can potentiate several measures of N-methyl-D-aspartate (NMDA)-induced channel opening, including radioligand binding to the PCP receptor. These data suggest that the NMDA/PCP receptor complex may be allosterically modulated by a binding site for glycine. We report here that several other monocarboxylic amino acids enhance NMDA-induced [³H]TCP binding and displace [³H]glycine binding with similar apparent affinities and stereoisomerism. The results are discussed with relation to the structural requirements for compounds to bind to this site.

Original language	English (US)
Pages (from-to)	105-110
Number of pages	6
Journal	European Journal of Pharmacology
Volume	156
Issue number	1
DOIs	https://doi.org/10.1016/0014-2999(88)90152-5
State	Published - Oct 26 1988

Keywords

(Binding)
Glycine
N-Methyl-D-aspartate (NMDA)
Phencyclidine
[H]1-[1-(2-Thienyl)cyclohexyl]piperidine ([H]TCP)

ASJC Scopus subject areas

Pharmacology

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10.1016/0014-2999(88)90152-5

Cite this

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title = "Structural requirements for activation of the glycine receptor that modulates the N-methyl-D-aspartate operated ion channel",

abstract = "It has recently been demonstrated that glycine can potentiate several measures of N-methyl-D-aspartate (NMDA)-induced channel opening, including radioligand binding to the PCP receptor. These data suggest that the NMDA/PCP receptor complex may be allosterically modulated by a binding site for glycine. We report here that several other monocarboxylic amino acids enhance NMDA-induced [3H]TCP binding and displace [3H]glycine binding with similar apparent affinities and stereoisomerism. The results are discussed with relation to the structural requirements for compounds to bind to this site.",

keywords = "(Binding), Glycine, N-Methyl-D-aspartate (NMDA), Phencyclidine, [H]1-[1-(2-Thienyl)cyclohexyl]piperidine ([H]TCP)",

author = "Snell, \{Lawrence D.\} and Morter, \{Robert S.\} and Johnson, \{Kenneth M.\}",

note = "Funding Information: This work was supported by the U.S.D.H.H.S. Grant DA 02073-09\textasciitilde{}",

year = "1988",

month = oct,

day = "26",

doi = "10.1016/0014-2999(88)90152-5",

language = "English (US)",

volume = "156",

pages = "105--110",

journal = "European Journal of Pharmacology",

issn = "0014-2999",

publisher = "Elsevier B.V.",

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TY - JOUR

T1 - Structural requirements for activation of the glycine receptor that modulates the N-methyl-D-aspartate operated ion channel

AU - Snell, Lawrence D.

AU - Morter, Robert S.

AU - Johnson, Kenneth M.

N1 - Funding Information: This work was supported by the U.S.D.H.H.S. Grant DA 02073-09~

PY - 1988/10/26

Y1 - 1988/10/26

N2 - It has recently been demonstrated that glycine can potentiate several measures of N-methyl-D-aspartate (NMDA)-induced channel opening, including radioligand binding to the PCP receptor. These data suggest that the NMDA/PCP receptor complex may be allosterically modulated by a binding site for glycine. We report here that several other monocarboxylic amino acids enhance NMDA-induced [3H]TCP binding and displace [3H]glycine binding with similar apparent affinities and stereoisomerism. The results are discussed with relation to the structural requirements for compounds to bind to this site.

AB - It has recently been demonstrated that glycine can potentiate several measures of N-methyl-D-aspartate (NMDA)-induced channel opening, including radioligand binding to the PCP receptor. These data suggest that the NMDA/PCP receptor complex may be allosterically modulated by a binding site for glycine. We report here that several other monocarboxylic amino acids enhance NMDA-induced [3H]TCP binding and displace [3H]glycine binding with similar apparent affinities and stereoisomerism. The results are discussed with relation to the structural requirements for compounds to bind to this site.

KW - (Binding)

KW - Glycine

KW - N-Methyl-D-aspartate (NMDA)

KW - Phencyclidine

KW - [H]1-[1-(2-Thienyl)cyclohexyl]piperidine ([H]TCP)

UR - https://www.scopus.com/pages/publications/0023756296

UR - https://www.scopus.com/pages/publications/0023756296#tab=citedBy

U2 - 10.1016/0014-2999(88)90152-5

DO - 10.1016/0014-2999(88)90152-5

M3 - Article

C2 - 2463175

AN - SCOPUS:0023756296

SN - 0014-2999

VL - 156

SP - 105

EP - 110

JO - European Journal of Pharmacology

JF - European Journal of Pharmacology

IS - 1

ER -

Structural requirements for activation of the glycine receptor that modulates the N-methyl-D-aspartate operated ion channel

Abstract

Keywords

ASJC Scopus subject areas

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