[3H]noscapine binding sites in brain: Relationship to indoleamines and the phosphoinositide and adenylyl cyclase messenger systems

R. J. Mourey, T. M. Dawson, R. K. Barrow, A. E. Enna, S. H. Snyder

Research output: Contribution to journalArticle

Abstract

High affinity [3H]noscapine binding sites are brain specific, ion insensitive, and present in a variety of species and show strict structure- activity requirements. Among neurotransmitter-related structures, indoleamines and β-carbolines display highest affinity for [3H]noscapine sites. Noscapine inhibits carbachol-stimulated phosphoinositide turnover in guinea pig and rat brain slices, with structural analogs possessing similar relative potencies for binding to [3H]noscapine binding sites and inhibiting phosphoinositide turnover. Noscapine and its derivatives also markedly enhance the ability of forskolin to augment cAMP levels in brain slices, with relative potencies paralleling affinities for noscapine binding sites.

Original languageEnglish (US)
Pages (from-to)619-626
Number of pages8
JournalMolecular Pharmacology
Volume42
Issue number4
StatePublished - Dec 1 1992

ASJC Scopus subject areas

  • Molecular Medicine
  • Pharmacology

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