Cloning, functional expression, and pharmacological characterization of inwardly rectifying potassium channels (Kir) from Apis mellifera
Abstract 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. Alt...
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Nature Portfolio
2024-04-01
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| Series: | Scientific Reports |
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| Online Access: | https://doi.org/10.1038/s41598-024-58234-0 |
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| author | Fabien Sourisseau Chaimaa Chahine Valérie Pouliot Thierry Cens Pierre Charnet Mohamed Chahine |
| author_facet | Fabien Sourisseau Chaimaa Chahine Valérie Pouliot Thierry Cens Pierre Charnet Mohamed Chahine |
| author_sort | Fabien Sourisseau |
| collection | DOAJ |
| description | Abstract 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 IC50 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. |
| first_indexed | 2024-04-24T12:40:01Z |
| format | Article |
| id | doaj.art-fe85bd16e82a4b6da9e1c6bd16936272 |
| institution | Directory Open Access Journal |
| issn | 2045-2322 |
| language | English |
| last_indexed | 2024-04-24T12:40:01Z |
| publishDate | 2024-04-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Scientific Reports |
| spelling | doaj.art-fe85bd16e82a4b6da9e1c6bd169362722024-04-07T11:19:17ZengNature PortfolioScientific Reports2045-23222024-04-0114111410.1038/s41598-024-58234-0Cloning, functional expression, and pharmacological characterization of inwardly rectifying potassium channels (Kir) from Apis melliferaFabien Sourisseau0Chaimaa Chahine1Valérie Pouliot2Thierry Cens3Pierre Charnet4Mohamed Chahine5CERVO Brain Research CentreCERVO Brain Research CentreCERVO Brain Research CentreInstitut des Biomolécules Max Mousseron (IBMM), CNRS UMR 5247Institut des Biomolécules Max Mousseron (IBMM), CNRS UMR 5247CERVO Brain Research CentreAbstract 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 IC50 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.https://doi.org/10.1038/s41598-024-58234-0Potassium channelsKir channelsExpressionCloningInsectsApis mellifera |
| spellingShingle | Fabien Sourisseau Chaimaa Chahine Valérie Pouliot Thierry Cens Pierre Charnet Mohamed Chahine Cloning, functional expression, and pharmacological characterization of inwardly rectifying potassium channels (Kir) from Apis mellifera Scientific Reports Potassium channels Kir channels Expression Cloning Insects Apis mellifera |
| title | Cloning, functional expression, and pharmacological characterization of inwardly rectifying potassium channels (Kir) from Apis mellifera |
| title_full | Cloning, functional expression, and pharmacological characterization of inwardly rectifying potassium channels (Kir) from Apis mellifera |
| title_fullStr | Cloning, functional expression, and pharmacological characterization of inwardly rectifying potassium channels (Kir) from Apis mellifera |
| title_full_unstemmed | Cloning, functional expression, and pharmacological characterization of inwardly rectifying potassium channels (Kir) from Apis mellifera |
| title_short | Cloning, functional expression, and pharmacological characterization of inwardly rectifying potassium channels (Kir) from Apis mellifera |
| title_sort | cloning functional expression and pharmacological characterization of inwardly rectifying potassium channels kir from apis mellifera |
| topic | Potassium channels Kir channels Expression Cloning Insects Apis mellifera |
| url | https://doi.org/10.1038/s41598-024-58234-0 |
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