Cloning, functional expression, and pharmacological characterization of inwardly rectifying potassium channels (Kir) from Apis mellifera.

Autor: Sourisseau F; CERVO Brain Research Centre, 2601, chemin de la Canardière, Quebec City, QC, G1J 2G3, Canada., Chahine C; CERVO Brain Research Centre, 2601, chemin de la Canardière, Quebec City, QC, G1J 2G3, Canada., Pouliot V; CERVO Brain Research Centre, 2601, chemin de la Canardière, Quebec City, QC, G1J 2G3, Canada., Cens T; Institut des Biomolécules Max Mousseron (IBMM), CNRS UMR 5247, 1919 Route de Mende, Montpellier, France., Charnet P; Institut des Biomolécules Max Mousseron (IBMM), CNRS UMR 5247, 1919 Route de Mende, Montpellier, France., Chahine M; CERVO Brain Research Centre, 2601, chemin de la Canardière, Quebec City, QC, G1J 2G3, Canada. Mohamed.Chahine@phc.ulaval.ca.; Department of Medicine, Faculty of Medicine, Université Laval, Quebec City, QC, Canada. Mohamed.Chahine@phc.ulaval.ca.
Jazyk: angličtina
Zdroj: Scientific reports [Sci Rep] 2024 Apr 03; Vol. 14 (1), pp. 7834. Date of Electronic Publication: 2024 Apr 03.
DOI: 10.1038/s41598-024-58234-0
Abstrakt: Potassium channels belong to the super family of ion channels and play a fundamental role in cell excitability. Kir channels are potassium channels with an inwardly rectifying property. They play a role in setting the resting membrane potential of many excitable cells including neurons. Although putative Kir channel family genes can be found in the Apis mellifera genome, their functional expression, biophysical properties, and sensitivity to small molecules with insecticidal activity remain to be investigated. We cloned six Kir channel isoforms from Apis mellifera that derive from two Kir genes, AmKir1 and AmKir2, which are present in the Apis mellifera genome. We studied the tissue distribution, the electrophysiological and pharmacological characteristics of three isoforms that expressed functional currents (AmKir1.1, AmKir2.2, and AmKir2.3). AmKir1.1, AmKir2.2, and AmKir2.3 isoforms exhibited distinct characteristics when expressed in Xenopus oocytes. AmKir1.1 exhibited the largest potassium currents and was impermeable to cesium whereas AmKir2.2 and AmKir2.3 exhibited smaller currents but allowed cesium to permeate. AmKir1 exhibited faster opening kinetics than AmKir2. Pharmacological experiments revealed that both AmKir1.1 and AmKir2.2 are blocked by the divalent ion barium, with IC 50 values of 10 -5 and 10 -6  M, respectively. The concentrations of VU041, a small molecule with insecticidal properties required to achieve a 50% current blockade for all three channels were higher than those needed to block Kir channels in other arthropods, such as the aphid Aphis gossypii and the mosquito Aedes aegypti. From this, we conclude that Apis mellifera AmKir channels exhibit lower sensitivity to VU041.
(© 2024. The Author(s).)
Databáze: MEDLINE
Externí odkaz: