ω-Conotoxin GVIA binding to a high-affinity receptor in brain: Characterization, calcium sensitivity, and solubilization

J. A. Wagner, A. M. Snowman, A. Biswas, B. M. Olivera, S. H. Snyder

Research output: Contribution to journalArticlepeer-review

Abstract

We describe unique, high-affinity binding sites for ω[125]conotoxin GVIA in membranes from rat brain and rabbit sympathetic ganglia which appear to be primarily associated with N-type voltage-dependent calcium channels. The dissociation constant (K(D)) for the toxin in rat brain membranes is 60 pM. Physiologic extracellular concentrations of calcium inhibit toxin binding noncompetitively (IC50 = 0.2 mM). The regional distribution of the binding sites in rat brain differs markedly from that of dihydropyridine calcium antagonist receptors associated with L-type calcium channels. In detergent-solubilized brain membranes, toxin binding retains the same affinity, specificity, and ionic sensitivity as in particulate preparations.

Original languageEnglish (US)
Pages (from-to)3354-3359
Number of pages6
JournalJournal of Neuroscience
Volume8
Issue number9
DOIs
StatePublished - 1988

ASJC Scopus subject areas

  • Neuroscience(all)

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