Toxin Antagonists of the Neuronal Nicotinic Acetylcholine Receptor

McIntosh, J. Michael

doi:10.1007/978-3-642-57079-7_17

Cited by 11 publications

(15 citation statements)

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“…This includes some activity at nicotinic receptors containing α2, α3, and β4 subunits as well as those containing α4 and β2 (Harvey et al 1996). Both α and β subunits appear to be necessary for the binding of DHβE (McIntosh 2000), therefore it is useful for distinguishing nicotinic receptors containing α and β subunits versus homomeric α nicotinic receptors like α7.…”

Section: Discussionmentioning

confidence: 97%

Chronic inhibition of α4β2 nicotinic receptors in the ventral hippocampus of rats: impacts on memory and nicotine response

Arthur

Levin

2002

Psychopharmacology

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These results indicate that chronic inhibition of a subset of nicotinic receptors in the hippocampus results in a significant impairment in the spatial memory choice accuracy. The ability of nicotine to attenuate the impairment supports the development of nicotinic agonist therapy of syndromes, such as Alzheimer's disease, that involve a chronic decrease in the activity of the alpha4beta2 nicotinic receptors and memory impairment.

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Section: Discussionmentioning

confidence: 97%

Chronic inhibition of α4β2 nicotinic receptors in the ventral hippocampus of rats: impacts on memory and nicotine response

Arthur

Levin

2002

Psychopharmacology

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“…The ACh ligand sites (also the binding site for other agonists) are located at interfaces between ␣-and non-␣-subunits, and two ACh must bind before gating of the ion channel from a closed to an open state can occur. A wide variety of competitive antagonists that compete for binding to the ACh site have been characterized (4,117). The classical competitive nicotinic antagonists are the well-known snake toxin from the banded krait, ␣-bungarotoxin, and the South American Indian poison arrow alkaloid, curare.…”

Section: B ␣-Conotoxins and Nachrs: Matching A Family Of Conopeptidementioning

confidence: 99%

ConusVenoms: A Rich Source of Novel Ion Channel-Targeted Peptides

Terlau

Olivera

2004

Physiological Reviews

863

828

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Terlau, Heinrich, and Baldomero M. Olivera. Conus Venoms: A Rich Source of Novel Ion Channel-Targeted Peptides. Physiol Rev 84: 41–68, 2004; 10.1152/physrev.00020.2003.—The cone snails (genus Conus) are venomous marine molluscs that use small, structured peptide toxins (conotoxins) for prey capture, defense, and competitor deterrence. Each of the 500 Conus can express ∼100 different conotoxins, with little overlap between species. An overwhelming majority of these peptides are probably targeted selectively to a specific ion channel. Because conotoxins discriminate between closely related subtypes of ion channels, they are widely used as pharmacological agents in ion channel research, and several have direct diagnostic and therapeutic potential. Large conotoxin families can comprise hundreds or thousands of different peptides; most families have a corresponding ion channel family target (i.e., ω-conotoxins and Ca channels, α-conotoxins and nicotinic receptors). Different conotoxin families may have different ligand binding sites on the same ion channel target (i.e., μ-conotoxins and δ-conotoxins to sites 1 and 6 of Na channels, respectively). The individual peptides in a conotoxin family are typically each selectively targeted to a diverse set of different molecular isoforms within the same ion channel family. This review focuses on the targeting specificity of conotoxins and their differential binding to different states of an ion channel.

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“…Traditionally, the main group is that of competitive antagonists that selectively block α7 and other homomeric receptors, namely α-bungarotoxin, methyllycaconitine (at low concentrations) and α-conotoxin ImI. For a recent review of toxin antagonists of neuronal nicotinic receptors see (McIntosh, 2000) α-bungarotoxin is one of the components of the poison of the banded krait, Bungarus multicinctus (74 amino acids, MW 8000). The affinity of this toxin for the homomeric α7 receptor appears to be high in binding assays (1-2 nM, Davies et al, 1999), but considerably lower than that for muscle-type receptors.…”

Section: Antagonistsmentioning

confidence: 99%

“…The Conus genus of marine snails provides an enormous variety of small peptide toxins (estimated at 200-500 per species). These are active on disparate voltage-and ligand-gated ion channels (for reviews see McIntosh et al, 1999;McIntosh, 2000;McIntosh & Jones, 2001). The venom is used by the snail to hunt its prey, which, depending on the snail species, can be worm, mollusc or fish.…”

Section: Conotoxinsmentioning

confidence: 99%

“…Conotoxins that are competitive antagonists of nicotinic receptors belong to the A superfamily (see McIntosh et al, 1999). Interestingly, the exquisite specificity of these compounds means that the data reported for receptors of a particular species cannot be extrapolated even to a related mammalian species, given that small differences in the binding domain sequences can markedly change the sensitivity to a conotoxin (McIntosh, 2000).…”

Section: Conotoxinsmentioning

confidence: 99%

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