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Abstract

Issue Title: Proceedings of the XIII International Symposium on Cholinergic Mechanisms

The diversity of nicotinic acetylcholine receptor (nAChR) subtypes was explored by measuring the effects of gene deletion and pharmacological diversity of epibatidine binding sites in mouse brain. All epibatidine binding sites require expression of either the α7, β2, or β4 subunit. In agreement with general belief, the α4β2*-nAChR and α7-nAChR subtypes are major components of the epibatidine binding sites. α4β2*-nAChR sites account for approximately 70% of total high- and low-affinity epibatidine binding sites, while α7-nAChR accounts for 16% of the total sites all of which have lower affinity for epibatidine. The other subtypes are structurally diverse. Although these minor subtypes account for only 14% of total binding in whole brain, they are expressed at relatively high concentrations in specific brain areas indicating unique functional roles.[PUBLICATION ABSTRACT]

Details

Title
John Daly's Compound, Epibatidine, Facilitates Identification of Nicotinic Receptor Subtypes
Author
Marks, Michael J; Laverty, Duncan S; Whiteaker, Paul; Salminen, Outi; Grady, Sharon R; Mcintosh, J Michael; Collins, Allan C
Pages
96-104
Publication year
2010
Publication date
Jan 2010
Publisher
Springer Nature B.V.
ISSN
08958696
e-ISSN
15591166
Source type
Scholarly Journal
Language of publication
English
ProQuest document ID
871575475
Copyright
Springer Science+Business Media, LLC 2010