Abstract：
:Interactions of the synthetic pyrethroid allethrin with the nicotinic acetylcholine (ACh) receptor/channel were studied in membranes from Torpedo electric organ. Allethrin did not inhibit binding of [3H]ACh to the receptor sites, but inhibited noncompetitively binding of [3H]perhydrohistrionicotoxin ([3H]H12-HTX) to the ionic channel sites in a dose-dependent manner. The inhibition constant (Ki) of [3H]H12-HTX binding in absence of receptor agonist was 30 micro M, while in presence of 100 micro M carbamylcholine it was 4 micro M. This inhibitory effect of allethrin had a negative temperature coefficient. The high affinity binding of allethrin to the channel sites of the nicotinic ACh-receptor may be indicative of a postsynaptic site of action for pyrethroids, in addition to their known action on the sodium channel.
journal_name
Life Scijournal_title
Life sciencesauthors
Abbassy MA,Eldefrawi ME,Eldefrawi ATdoi
10.1016/0024-3205(82)90045-5subject
Has Abstractpub_date
1982-10-11 00:00:00pages
1547-52issue
15eissn
0024-3205issn
1879-0631pii
0024-3205(82)90045-5journal_volume
31pub_type
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