Ciguatoxin and brevetoxins share a common receptor site on the neuronal voltage-dependent Na+ channel.
Binding studies indicate that ciguatoxin and brevetoxin allosterically enhance in a very similar way the binding of [3H]batrachotoxinin A 20-alpha-benzoate to the neuronal Na+ channel protein. Moreover ciguatoxin competitively inhibits the binding of [3H]brevetoxin-3 to rat brain membranes. The affinity of ciguatoxin for the Na+ channel is at least 20-50-times higher than that of brevetoxin. These results indicate that ciguatoxin and brevetoxins act at the same binding site on the sodium channel.
D000818:Animals; D001921:Brain / Q000378:metabolism*; D002922:Ciguatoxins / Q000494:pharmacology*; D007473:Ion Channels / Q000187:drug effects / Q000378:metabolism*; D007700:Kinetics; D008387:Marine Toxins / Q000494:pharmacology*; D009474:Neurons / Q000378:metabolism*; D009498:Neurotoxins / Q000378:metabolism; D035964:Oxocins; D051381:Rats; D011950:Receptors, Cholinergic / Q000187:drug effects / Q000378:metabolism*; D012964:Sodium / Q000378:metabolism*; D000095702:Polyether Toxins
D002922:Ciguatoxins; D007473:Ion Channels; D008387:Marine Toxins; D009498:Neurotoxins; D035964:Oxocins; D011950:Receptors, Cholinergic; D012964:Sodium; C053342:brevetoxin; D000095702:Polyether Toxins