Omega-conotoxin GVIA binding to a high-affinity receptor in brain: characterization, calcium sensitivity, and solubilization. Academic Article uri icon

Overview

abstract

  • We describe unique, high-affinity binding sites for omega[125I]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 (KD) 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.

publication date

  • September 1, 1988

Research

keywords

  • Calcium
  • Calcium Channels
  • Mollusk Venoms
  • Receptors, Neurotransmitter

Identity

PubMed Central ID

  • PMC6569423

Scopus Document Identifier

  • 0023811637

Digital Object Identifier (DOI)

  • 10.1523/JNEUROSCI.08-09-03354.1988

PubMed ID

  • 2845019

Additional Document Info

volume

  • 8

issue

  • 9