Quaternary forms of classical muscarinic antagonists distinguish subpopulations of muscarinic receptors: Correlation with gallamine-defined subpopulations

John Ellis, Robert H. Lenox

Research output: Contribution to journalArticle

13 Citations (Scopus)

Abstract

Atropine and scopolamine inhibit the binding of [3H] quinuclidinyl benzilate (QNB) to muscarinic receptors of rat forebrain in a manner that suggests homogeneity of the binding sites. Under the same conditions, the inhibition by N-methyl-atropine (NMA) and N-methylscopolamine (NMS) of the binding of [3H]QNB is consistent with the presence of subpopulations of receptors that differ greatly in affinities toward these quaternary ligands. The subpopulations that are defined according to the affinities of NMA and NMS correlate very well with those that are defined by the use of gallamine. It is suggested that the heterogeneity in the binding of NMS explains some of the anomalous interactions between NMS and gallamine that have been reported previously.

Original languageEnglish (US)
Pages (from-to)1242-1250
Number of pages9
JournalBiochemical and Biophysical Research Communications
Volume126
Issue number3
DOIs
StatePublished - Feb 15 1985

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N-Methylscopolamine
Gallamine Triethiodide
Muscarinic Antagonists
Muscarinic Receptors
Quinuclidinyl Benzilate
Scopolamine Hydrobromide
Prosencephalon
Atropine
Rats
Binding Sites
Ligands

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

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abstract = "Atropine and scopolamine inhibit the binding of [3H] quinuclidinyl benzilate (QNB) to muscarinic receptors of rat forebrain in a manner that suggests homogeneity of the binding sites. Under the same conditions, the inhibition by N-methyl-atropine (NMA) and N-methylscopolamine (NMS) of the binding of [3H]QNB is consistent with the presence of subpopulations of receptors that differ greatly in affinities toward these quaternary ligands. The subpopulations that are defined according to the affinities of NMA and NMS correlate very well with those that are defined by the use of gallamine. It is suggested that the heterogeneity in the binding of NMS explains some of the anomalous interactions between NMS and gallamine that have been reported previously.",
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