Purified ω-conotoxin GVIA receptor of rat brain resembles a dihydropyridine-sensitive L-type calcium channel

Maureen W. Mcenery; Adele M. Snowman; Alan H. Sharp; Michael E. Adams; Solomon H. Snyder

doi:10.1073/pnas.88.24.11095

Purified ω-conotoxin GVIA receptor of rat brain resembles a dihydropyridine-sensitive L-type calcium channel

Maureen W. Mcenery, Adele M. Snowman, Alan H. Sharp, Michael E. Adams, Solomon H. Snyder

School of Medicine

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

89 Scopus citations

Abstract

The ω-conotoxin GVIA (CTX) receptor has been purified 1900-fold to apparent. homogeneity by monitoring both reversible binding of ¹²⁵I-labeled CTX (¹²⁵I-CTX) and photoincorporation of N-hydroxysuccinimidyl-4-azidobenzoate-¹²⁵I-CTX (HSA-¹²⁵I-CTX). Photoincorporation of HSA¹²⁵I-CTX into a 230-kDa protein exhibits a pharmacologic and chromatographic profile indicating that the 230-kDa protein is the CTX-binding subunit of the receptor. The pharmacologic specificity of ¹²⁵I-CTX binding to the purified CTX receptor closely resembles that of the native membrane-bound form with respect to sensitivity towards CTX (K_d = 32 pM) and other peptide toxin antagonists. The purified CTX receptor comprises the 230-kDa protein (α₁) and four additional proteins with apparent molecular masses of 140 (α₂), 110, 70 (β₂2), and 60 (β₁) kDa. This subunit structure closely resembles that of the 1,4-dihydropyridine-sensitive L-type calcium channel.

Original language	English (US)
Pages (from-to)	11095-11099
Number of pages	5
Journal	Proceedings of the National Academy of Sciences of the United States of America
Volume	88
Issue number	24
DOIs	https://doi.org/10.1073/pnas.88.24.11095
State	Published - 1991

Keywords

Photoaffinity labeling
Voltage-dependent calcium channels
ω-agatoxin IIIA

ASJC Scopus subject areas

General

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10.1073/pnas.88.24.11095

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title = "Purified ω-conotoxin GVIA receptor of rat brain resembles a dihydropyridine-sensitive L-type calcium channel",

abstract = "The ω-conotoxin GVIA (CTX) receptor has been purified 1900-fold to apparent. homogeneity by monitoring both reversible binding of 125I-labeled CTX (125I-CTX) and photoincorporation of N-hydroxysuccinimidyl-4-azidobenzoate-125I-CTX (HSA-125I-CTX). Photoincorporation of HSA125I-CTX into a 230-kDa protein exhibits a pharmacologic and chromatographic profile indicating that the 230-kDa protein is the CTX-binding subunit of the receptor. The pharmacologic specificity of 125I-CTX binding to the purified CTX receptor closely resembles that of the native membrane-bound form with respect to sensitivity towards CTX (Kd = 32 pM) and other peptide toxin antagonists. The purified CTX receptor comprises the 230-kDa protein (α1) and four additional proteins with apparent molecular masses of 140 (α2), 110, 70 (β22), and 60 (β1) kDa. This subunit structure closely resembles that of the 1,4-dihydropyridine-sensitive L-type calcium channel.",

keywords = "Photoaffinity labeling, Voltage-dependent calcium channels, ω-agatoxin IIIA",

author = "Mcenery, {Maureen W.} and Snowman, {Adele M.} and Sharp, {Alan H.} and Adams, {Michael E.} and Snyder, {Solomon H.}",

year = "1991",

doi = "10.1073/pnas.88.24.11095",

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AU - Mcenery, Maureen W.

AU - Snowman, Adele M.

AU - Sharp, Alan H.

AU - Adams, Michael E.

AU - Snyder, Solomon H.

PY - 1991

Y1 - 1991

N2 - The ω-conotoxin GVIA (CTX) receptor has been purified 1900-fold to apparent. homogeneity by monitoring both reversible binding of 125I-labeled CTX (125I-CTX) and photoincorporation of N-hydroxysuccinimidyl-4-azidobenzoate-125I-CTX (HSA-125I-CTX). Photoincorporation of HSA125I-CTX into a 230-kDa protein exhibits a pharmacologic and chromatographic profile indicating that the 230-kDa protein is the CTX-binding subunit of the receptor. The pharmacologic specificity of 125I-CTX binding to the purified CTX receptor closely resembles that of the native membrane-bound form with respect to sensitivity towards CTX (Kd = 32 pM) and other peptide toxin antagonists. The purified CTX receptor comprises the 230-kDa protein (α1) and four additional proteins with apparent molecular masses of 140 (α2), 110, 70 (β22), and 60 (β1) kDa. This subunit structure closely resembles that of the 1,4-dihydropyridine-sensitive L-type calcium channel.

AB - The ω-conotoxin GVIA (CTX) receptor has been purified 1900-fold to apparent. homogeneity by monitoring both reversible binding of 125I-labeled CTX (125I-CTX) and photoincorporation of N-hydroxysuccinimidyl-4-azidobenzoate-125I-CTX (HSA-125I-CTX). Photoincorporation of HSA125I-CTX into a 230-kDa protein exhibits a pharmacologic and chromatographic profile indicating that the 230-kDa protein is the CTX-binding subunit of the receptor. The pharmacologic specificity of 125I-CTX binding to the purified CTX receptor closely resembles that of the native membrane-bound form with respect to sensitivity towards CTX (Kd = 32 pM) and other peptide toxin antagonists. The purified CTX receptor comprises the 230-kDa protein (α1) and four additional proteins with apparent molecular masses of 140 (α2), 110, 70 (β22), and 60 (β1) kDa. This subunit structure closely resembles that of the 1,4-dihydropyridine-sensitive L-type calcium channel.

KW - Photoaffinity labeling

KW - Voltage-dependent calcium channels

KW - ω-agatoxin IIIA

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Purified ω-conotoxin GVIA receptor of rat brain resembles a dihydropyridine-sensitive L-type calcium channel

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Keywords

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