Binding of thiamine to nicotinic acetylcholine receptor in torpedo marmorata and the frog end plate.
Thiamine was found to bind to the isolated nicotinic receptor (nAChR) from Torpedo marmorata (KD = 3--5 X 10(-5) M). The binding was reversible and inhibited by alpha-neurotoxin from Naja naja siamensis. Acetylcholine binding was not inhibited by thiamine. When thiamine (5 X 10(-4) M) was applied to frog sartorius muscles a decrease of miniature end plate potential amplitudes was seen. This effect was readily reversible after the perfusion fluid of the muscle was changed to normal Ringer solution. Thus both biological and electrophysiological studies indicated a binding of thiamine to the nAChR.
D000109:Acetylcholine / Q000378:metabolism; D000200:Action Potentials; D000818:Animals; D001001:Anura; D005399:Fishes; D009045:Motor Endplate / Q000378:metabolism*; D009132:Muscles / Q000502:physiology; D009469:Neuromuscular Junction / Q000378:metabolism*; D009498:Neurotoxins; D011894:Rana pipiens; D011950:Receptors, Cholinergic / Q000378:metabolism*; D011978:Receptors, Nicotinic / Q000378:metabolism*; D013831:Thiamine / Q000378:metabolism*
D009498:Neurotoxins; D011950:Receptors, Cholinergic; D011978:Receptors, Nicotinic; D000109:Acetylcholine; D013831:Thiamine