Specific binding sites for alcohols and anesthetics on ligand-gated ion channels

Mascia, MP; Trudell, JR; Harris, RA

HERO ID

783556

Reference Type

Journal Article

Year

2000

Language

English

PMID

10908659

HERO ID 783556
In Press No
Year 2000
Title Specific binding sites for alcohols and anesthetics on ligand-gated ion channels
Authors Mascia, MP; Trudell, JR; Harris, RA
Journal Proceedings of the National Academy of Sciences of the United States of America
Volume 97
Issue 16
Page Numbers 9305-9310
Abstract Ligand-gated ion channels are a target for inhaled anesthetics and alcohols in the central nervous system. The inhibitory strychnine-sensitive glycine and gamma-aminobutyric acid type A receptors are positively modulated by anesthetics and alcohols, and site-directed mutagenesis techniques have identified amino acid residues important for the action of volatile anesthetics and alcohols in these receptors. A key question is whether these amino acids are part of an alcohol/anesthetic-binding site. In the present study, we used an alkanethiol anesthetic to covalently label its binding site by mutating selected amino acids to cysteine. We demonstrated that the anesthetic propanethiol, or alternatively, propyl methanethiosulfonate, covalently binds to cysteine residues introduced into a specific second transmembrane site in glycine receptor and gamma-aminobutyric acid type A receptor subunits and irreversibly enhances receptor function. Moreover, upon permanent occupation of the site by propyl disulfide, the usual ability of octanol, enflurane, and isoflurane to potentiate the function of the ion channels was lost. This approach provides strong evidence that the actions of anesthetics in these receptors are due to binding at a single site.
Doi 10.1073/pnas.160128797
Pmid 10908659
Wosid WOS:000088608000097
Is Certified Translation No
Dupe Override No
Is Public Yes
Language Text English
Is Qa No