Immunological distinction between acetylcholine receptor and the alpha-bungarotoxin-binding component on sympathetic neurons.
Clone PC12 of a rat sympathetic neuron cell line binds alpha-bungarotoxin and exhibits carbamoylcholine-stimulated uptake of sodium ions. Concentrations of alpha-bungarotoxin that saturate the alpha-bungarotoxin-binding site have no effect on agonist-stimulated sodium uptake. Conversely, antibodies against eel acetylcholine receptor block the agonist-induced sodium flux but fail to recognize the alpha-bungarotoxin-binding component. Detergent extracts of the PC12 clone inhibit the ability of antibody to eel acetylcholine receptor to recognize 125I-alpha-bungarotoxin-acetylcholine receptor complexes derived from muscle. These results distinguish between a ganglionic nicotinic acetylcholine receptor and an alpha-bungarotoxin-binding component on these cells, and provide evidence for antigenic similarities between muscle acetylcholine receptor and ganglionic acetylcholine receptor.
D000109:Acetylcholine / Q000378:metabolism*; D001665:Binding Sites; D002038:Bungarotoxins / Q000378:metabolism*; D002460:Cell Line; D009474:Neurons / Q000378:metabolism*; D011950:Receptors, Cholinergic / Q000276:immunology*; D012964:Sodium / Q000378:metabolism; D013564:Sympathetic Nervous System / Q000378:metabolism*
D002038:Bungarotoxins; D011950:Receptors, Cholinergic; D012964:Sodium; D000109:Acetylcholine
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