Acetylcholine operated ion channel and alpha-bungarotoxin binding site in a human neuroblastoma cell line reside on different molecules.
In neurons, alpha-bungarotoxin is often associated with nicotinic receptor but does not always block the acetylcholine operated channel. In a human neuroblastoma cell line, IMR 32, we have demonstrated a large number of alpha-Bungarotoxin binding sites (2640 per cell in non differentiated cells and 4660 per cell in differentiated cells) in presence of 0 to 4 Acetylcholine activated-channels per cell. This neuronal cell line promises to be an useful model for the study of structure and function of the alpha-Bungarotoxin binding site not related to the nicotinic receptor.
D000109:Acetylcholine / Q000378:metabolism; D001665:Binding Sites; D002038:Bungarotoxins / Q000378:metabolism*; D002460:Cell Line; D004553:Electric Conductivity; D006801:Humans; D007473:Ion Channels / Q000378:metabolism*; D046911:Macromolecular Substances; D009447:Neuroblastoma; D011978:Receptors, Nicotinic / Q000378:metabolism*
D002038:Bungarotoxins; D007473:Ion Channels; D046911:Macromolecular Substances; D011978:Receptors, Nicotinic; D000109:Acetylcholine