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- W2056106698 abstract "The interactions of natural pyrethrins and nine pyrethroids with the nicotinic acetylcholine (ACh) receptor/channel complex of Torpedo electric organ membranes were studied. None caused significant reduction in [ 3 H]ACh binding to the receptor sites, but all inhibited [ 3 H]perhydrohistrionicotoxin ([ 3 H]H 12 -HTX) binding to the channel sites in presence of carbamylcholine. Allethrin inhibited [ 3 H]H 12 -HTX binding noncompetitively, but [ 3 H]imipramine binding competitively, suggesting that allethrin binds to the receptor's channel sites that bind imipramine. The pyrethroids were divided into two types according to their actions: type I, which included pyrethrins, allethrin, bioallethrin, resmethrin, and tetramethrin, was more potent in inhibiting [ 3 H]H 12 -HTX binding and acted more rapidly (i.e., in <30 sec). Type II, which included permethrin, fluvalinate, cypermethrin and fenvalerate, was less potent and their potency increased slowly with time. Also, inhibition of the initial rate of [ 3 H]H 12 -HTX binding by type I compounds increased greatly by the presence of the agonist carbamylcholine, but this was not so with type II compounds. The receptor-regulated 45 Ca 2+ flux into Torpedo microsacs was inhibited by pyrethrins and pyrethroids, suggesting that their action on this receptor function is inhibitory. There was very poor correlation between the potencies of pyrethrins and pyrethroids in inhibiting [ 3 H]H 12 -HTX binding and their toxicities to house flies, mosquitoes, and the American cockroach. However, the high affinities that several pyrethroids have for this nicotinic ACh receptor suggest that pyrethroids may have a synaptic site of action in addition to their well known effects on the axonal channels." @default.
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- W2056106698 date "1983-06-01" @default.
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- W2056106698 title "Pyrethroid action on the nicotinic acetylcholine receptor/channel" @default.
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