Studies of nicotinic acetylcholine receptor protein from rat brain

Moore, William M.; Brady, Robert N.

doi:10.1016/0304-4165(77)90271-9

Cited by 28 publications

(12 citation statements)

References 15 publications

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“…On the basis of the binding kinetics of a-BuTX, its subcellular distribution, and the hydrodynamic properties of its receptor, it has been inferred that a-BuTX binds to neuronal AcCh receptors (1,(3)(4)(5)(6)(7)(8)(9)(10)(11). There is, however, little physiological evidence to support this inference.…”

mentioning

confidence: 88%

“…a-BuTX binds with a high affinity to neuronal as well as to muscle membranes, and this binding is competitively inhibited by cholinergic agonists and antagonists (1)(2)(3)(4)(5)(6)(7)(8)(9)(10)(11)(12). On the basis of the binding kinetics of a-BuTX, its subcellular distribution, and the hydrodynamic properties of its receptor, it has been inferred that a-BuTX binds to neuronal AcCh receptors (1,(3)(4)(5)(6)(7)(8)(9)(10)(11).…”

mentioning

confidence: 99%

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Nonequivalence of alpha-bungarotoxin receptors and acetylcholine receptors in chick sympathetic neurons.

Carbonetto¹,

Fambrough²,

Muller³

1978

Proc. Natl. Acad. Sci. U.S.A.

123

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ABSTRACTa-Bungarotoxin binds selectively to chick sympathetic neurons that are responsive to iontophoretically applied acetylcholine. a-Bungarotoxin (125 nM) does not affect the response of cultured neurons to acetylcholine, nor does it affect a cholinergic synaptic potential recorded from sympathetic ganglia. d-Tubocurarine (100 ,uM) inhibits a-bungarotoxin binding and blocks acetylcholine receptor function in both preparations, but a-bungarotoxin does not protect acetylcholine receptors against d-tubocurarine blockade of acetylcholine responses. The receptor for a-bungarotoxin can be extracted from neuronal membranes with nonionic detergents and, when assayed by velocity sedimentation in sucrose gradients, sediments at a rate faster than that of skeletal muscle acetylcholine receptors. Treatment of a-bungarotoxin-receptor complexes with glutaraldehyde (0.1%, wt/vol) increases their stability from a half-time for dissociation of 3.5 hr to greater than 6 days at 230. This permits a quantitative assay of a-bungarotoxin-receptor complexes after relatively long periods of velocity sedimentation.It is concluded that a-bungarotoxin does not bind to the acetylcholine-binding site of neuronal acetylcholine receptors. These results compel a reevaluation of studies that assume that a-bungarotoxin is a specific ligand for neuronal acetylcholine receptors.

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confidence: 88%

mentioning

confidence: 99%

Nonequivalence of alpha-bungarotoxin receptors and acetylcholine receptors in chick sympathetic neurons.

Carbonetto¹,

Fambrough²,

Muller³

1978

Proc. Natl. Acad. Sci. U.S.A.

123

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“…I]-␣BTx were discovered Ͼ20 years ago (Eterovic and Bennett, 1974;Polz-Tejera et al, 1975;Moore and Brady, 1976), but the inability to demonstrate f unctional responses that could be blocked by ␣BTx led to speculation that central […”

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confidence: 99%

Synaptic Potentials Mediated via α-Bungarotoxin-Sensitive Nicotinic Acetylcholine Receptors in Rat Hippocampal Interneurons

et al. 1998

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Exogenous application of acetylcholine elicits inward currents in hippocampal interneurons that are mediated via ␣-bungarotoxin-sensitive nicotinic acetylcholine receptors, but synaptic responses mediated via such receptors have never been reported in mammalian brain. In the present study, EPSCs were evoked in hippocampal interneurons in rat brain slices by electrical stimulation and were recorded by using whole-cell voltage-clamp techniques. Nicotinic EPSCs were isolated pharmacologically, using antagonists to block other known types of ligand-gated ion channels, and then were tested with either ␣-bungarotoxin or methyllycaconitine, which are selective antagonists for nicotinic acetylcholine receptors that contain the ␣7 receptor subunit. Each antagonist proved highly effective at reducing the remaining synaptic current. Evoked ␣7-mediated nicotinic EPSCs also were desensitized by superfusion with 1 M nicotine, had extrapolated reversal potentials near 0 mV, and showed strong inward rectification at positive potentials. In several interneurons, methyllycaconitine-sensitive spontaneous EPSCs also were observed that exhibited a biphasic decay rate very similar to that of the ␣7-mediated evoked response. These studies provide the first demonstration of a functional cholinergic synapse in the mammalian brain, in which the primary postsynaptic receptors are ␣-bungarotoxin-sensitive nicotinic acetylcholine receptors.

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“…However, in 1963 the discovery that a small protein (α-bungarotoxin) isolated from the venom of the Taiwanese banded krait Bungarus multicinctus bound strongly and almost irreversibly to the nAChR of the vertebrate neuromuscular junction proved to be an important step in the study of neurotransmitter receptors [29], and led to the identification and purification of these receptors in the electric organ of Torpedo and at the neuromuscular junction [30][31][32][33][34]. Since this discovery, a large number of closely related snake toxins that target nAChRs have been discovered and these are discussed below in more detail.…”

Section: Review -Hogg and Bertrandmentioning

confidence: 99%

Neurotoxins Acting at Nicotinic Receptors

Hogg

Bertrand

2008

Future Neurol.

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Neurotoxins include, in the most general sense, all molecules that destroy or inhibit the proper functioning of the nervous system. Neurotoxins from animals and plants include alkaloids and peptides, many of which interact with physiological processes in a selective manner. The majority of neurotoxins disrupt the transmission of signals in the nervous system by interfering with synaptic transmission. Neurotoxins can act presynaptically to inhibit the release, uptake and recycling of neurotransmitters or postsynaptically, binding to receptors on the postsynaptic membrane and preventing their activation by neurotransmitters. A class of neurotoxins from plants and animals interact with nicotinic acetylcholine receptors, either at the neuromuscular junction, peripherally at neuronal ganglia or centrally, to produce neurotoxic effects. In this article we review current knowledge of some of these neurotoxins, their structure, pharmacology, importance as pharmaceutical tools as well as future prospects for the development of therapeutic molecules.

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Studies of nicotinic acetylcholine receptor protein from rat brain

Cited by 28 publications

References 15 publications

Nonequivalence of alpha-bungarotoxin receptors and acetylcholine receptors in chick sympathetic neurons.

Nonequivalence of alpha-bungarotoxin receptors and acetylcholine receptors in chick sympathetic neurons.

Synaptic Potentials Mediated via α-Bungarotoxin-Sensitive Nicotinic Acetylcholine Receptors in Rat Hippocampal Interneurons

Neurotoxins Acting at Nicotinic Receptors

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