Open AccessImmunological distinction between acetylcholine receptor and the alpha-bungarotoxin-binding component on sympathetic neurons.
Author(s) -
Jim Patrick,
William B. Stallcup
Publication year - 1977
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.74.10.4689
Subject(s) - acetylcholine receptor , acetylcholine , alpha 4 beta 2 nicotinic receptor , nicotinic acetylcholine receptor , medicine , agonist , endocrinology , muscarinic acetylcholine receptor m5 , bungarotoxin , chemistry , nicotinic agonist , receptor , ganglion type nicotinic receptor , biology , muscarinic acetylcholine receptor m3 , biochemistry
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.