Nicotinic Acetylcholine Receptor Diversity: Agonist Binding And Functional Potency
This chapter discusses the nicotinic acetylcholine receptor diversity. [3H]Ach and 86Rb+ are binding assays and efflux assays respectively. These assays of acetylcholine receptor (nAChR) channel function take advantage of this receptor's permeability to monovalent cations as large as glucosamine and the cellular Na+-K+-ATPase's ability to concentrate 86Rb+ in TE671 and PC12 cells, and permits the assessment of nAChR-channel function by the measurement of 86Rb+ release during incubation of isotope-loaded cells in medium containing the appropriate cholinergic ligands. Membrane preparations from torpedo electroplax, TE671 cells and rat brain express highaffinity [3H]ACh binding sites with apparent macroscopic dissociation constants of about 10 nM and Hill coefficients of about 1.0. The utility of clonal cell line models that express different nAChR isotypes in the studies of the properties of those receptors has been demonstrated. Further use of those cell lines promises to illuminate the relationships between ligand binding sites and sites that regulate activation and inactivation of nAChR functional responses, and to provide insight into the effects of nicotine at neuronal synapses. Â© 1989 Academic Press Inc.
Progress in Brain Research
Digital Object Identifier (DOI)
Lukas, Ronald J., "Nicotinic Acetylcholine Receptor Diversity: Agonist Binding And Functional Potency" (1989). Translational Neuroscience. 255.