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Journal of Neuroscience, Vol 7, 4005-4016, Copyright © 1987 by Society for Neuroscience
Structurally different neuronal nicotinic acetylcholine receptor subtypes purified and characterized using monoclonal antibodies
PJ Whiting, R Liu, BJ Morley and JM Lindstrom
Salk Institute for Biological Studies, San Diego, California 92138.
Acetylcholine receptors that bind nicotine with high affinity but do not
bind alpha-bungarotoxin have recently been immunoaffinity purified from
brains of chickens and rats (Whiting and Lindstrom, 1986a, b; Whiting and
Lindstrom, 1987a). Antisera to these receptors bind to the nicotinic
receptors that regulate cation channel opening on chick ciliary ganglion
neurons (Stollberg et al., 1986) and rat PC12 cells (Whiting et al.,
1987c). Here we report the preparation and characterization of monoclonal
antibodies to chicken brain acetylcholine receptors. These monoclonal
antibodies are used to identify 2 nicotinic receptor subtypes in the
chicken brain. The 2 subtypes have very similar affinities for nicotine and
other cholinergic agonists and antagonists. However, they are structurally
distinct, having very similar or identical alpha subunits (Mr 49,000), but
different beta subunits (Mr 59,000, or for beta' subunit, Mr 75,000).
Evidence is presented that suggests that the subunit stoichiometry of these
neuronal nicotinic acetylcholine receptors is alpha n = 2 - 3 beta n = 2 -
3. Different levels of receptor subtype expression were detected in
embryonic, compared to adult, chicken brain.
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