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

doi:10.1523/jneurosci.08-09-03354.1988

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

School of Medicine

Research output: Contribution to journal › Article › peer-review

127 Scopus citations

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 language	English (US)
Pages (from-to)	3354-3359
Number of pages	6
Journal	Journal of Neuroscience
Volume	8
Issue number	9
DOIs	https://doi.org/10.1523/jneurosci.08-09-03354.1988
State	Published - 1988

ASJC Scopus subject areas

General Neuroscience

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10.1523/jneurosci.08-09-03354.1988

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

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.",

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T1 - ω-Conotoxin GVIA binding to a high-affinity receptor in brain

T2 - Characterization, calcium sensitivity, and solubilization

AU - Wagner, J. A.

AU - Snowman, A. M.

AU - Biswas, A.

AU - Olivera, B. M.

AU - Snyder, S. H.

PY - 1988

Y1 - 1988

N2 - 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.

AB - 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.

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

Abstract

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