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Journal of Neuroscience, Vol 8, 3354-3359, Copyright © 1988 by Society for Neuroscience
Omega-conotoxin GVIA binding to a high-affinity receptor in brain: characterization, calcium sensitivity, and solubilization
JA Wagner, AM Snowman, A Biswas, BM Olivera and SH Snyder
Department of Neuroscience, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205.
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.
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