Chlordecone reduces hyperpolarization-activated-current (Ih) conductance in honeybee
2025
Bois, Patrick | Chavanieu, Alain | Magaud, Christophe | Fares, Nassim | Kaabeche, Mahira | Chatelier, Aurelien | Charnet, Pierre | Cens, Thierry | Physiopathologie et régulation des transports ioniques (PRéTI [Poitiers]) ; Université de Poitiers = University of Poitiers (UP) | Institut des Biomolécules Max Mousseron [Pôle Chimie Balard] (IBMM) ; Institut de Chimie - CNRS Chimie (INC-CNRS)-Centre National de la Recherche Scientifique (CNRS)-Université de Montpellier (UM)-Ecole Nationale Supérieure de Chimie de Montpellier (ENSCM) ; Université de Montpellier (UM) | Université Saint-Joseph de Beyrouth (USJ) | Abeilles et Environnement (AE) ; Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)
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Mostrar más [+] Menos [-]Inglés. The pacemaker channel (HCN) is responsible for electrical activity in a wide range of excitable cells, including those of invertebrates. Using Xenopus oocytes and HEK cell, we show here that HCN-channel from <i>Apis mellifera</i> is activated by hyperpolarization, modulated by cAMP, and blocked by cesium. Its PNa/PK relative permeability is 1:3, and its unitary conductance is 1.5 pS, which is similar to that of the mammalian HCN2 channel. Moreover, bee h-current is blocked by high concentrations of ZD7288, and organochlorine pesticide chlordecone reduces Ih amplitude in a dose-dependent manner (IC50 value was 9.37 µM) and diminishes HCN conductance, while preserving voltage dependence. In contrast, Deltamethrin exhibits no discernible impact. Molecular docking of Chlordecone in a homology model of bee HCN generated by AlphaFold3 suggests a binding site located at the end of the S6 helix that could explain the conductance inhibition caused by Chlordecone.
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