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• W2013817887 abstract "The nicotinic acetylcholine receptor (nAChR) of the electric organ of the electric ray.Torpedosp., the richest source of nAChR, with similar structure and pharmacology to the mammalian skeletal muscle nAChR, carries several binding sites for different ligands. Incubation ofTorpedomembrane-bound nAChRs with the agonist carbamylcholine (Carb) stimulated the binding of [3H]thienyl-cyclohexylpiperidine ([3H]TCP), which binds to the receptor's noncompetitive antagonist binding site in its ionic channel, with high affinity (Kdof 196 nm). The agonist-stimulated binding of [3H]TCP (i.e., binding to activated nAChRs) was inhibited in a concentration-dependent manner by four organophosphate (OP) anticholinesterases, chlorpyrifos oxon (CPO), chlorpyrifos (CPS), parathion (PS), and paraoxon (PO) with IC50 (concentration that inhibits 50% of the effect) values of 5, 150, 200, and 300 μm, respectively. The binding of CPO was totally reversible. The OPs had no effect on equilibrium binding of [α-125I]bungarotoxin ([α-125I]BGT) to the receptor's acetylcholine (ACh)-binding site, but preincubation of the membranes with the OPs increased this site's affinity for Carb. In absence of agonist, 100 μmof the OPs increased the binding of [3H]TCP by two- to fivefold with the following order of decreasing potency: PS > CPO > CPS > PO. The data suggest that in addition to inhibition of acetylcholinesterase, these OPs bind to a site on the nAChR that is different from the sites that bind ACh or TCP and that this binding induces nAChR desensitization. The relevance of this direct action of OPs on nAChRs on their acute toxicities is discussed." @default.
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• W2013817887 date "1997-10-01" @default.
• W2013817887 modified "2023-10-14" @default.
• W2013817887 title "Chlorpyrifos, Parathion, and Their Oxons Bind to and Desensitize a Nicotinic Acetylcholine Receptor: Relevance to Their Toxicities" @default.
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• W2013817887 doi "https://doi.org/10.1006/taap.1997.8201" @default.
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