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Activation of TREK currents by riluzole in three subgroups of cultured mouse nodose ganglion neurons.

Fernández-Fernández, Diego, Cadaveira-Mosquera, Alba, Rueda-Ruzafa, Lola, Herrera-Pérez, Salvador, Veale, Emma L., Reboreda, Antonio, Mathie, Alistair, Lamas, J Antonio (2018) Activation of TREK currents by riluzole in three subgroups of cultured mouse nodose ganglion neurons. PloS one, 13 (6). e0199282. ISSN 1932-6203. (doi:10.1371/journal.pone.0199282) (KAR id:75877)

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https://doi.org/10.1371/journal.pone.0199282

Abstract

Two-pore domain potassium channels (K2P) constitute major candidates for the regulation of background potassium currents in mammalian cells. Channels of the TREK subfamily are also well positioned to play an important role in sensory transduction due to their sensitivity to a large number of physiological and physical stimuli (pH, mechanical, temperature). Following our previous report describing the molecular expression of different K2P channels in the vagal sensory system, here we confirm that TREK channels are functionally expressed in neurons from the mouse nodose ganglion (mNG). Neurons were subdivided into three groups (A, Ah and C) based on their response to tetrodotoxin and capsaicin. Application of the TREK subfamily activator riluzole to isolated mNG neurons evoked a concentration-dependent outward current in the majority of cells from all the three subtypes studied. Riluzole increased membrane conductance and hyperpolarized the membrane potential by approximately 10 mV when applied to resting neurons. The resting potential was similar in all three groups, but C cells were clearly less excitable and showed smaller hyperpolarization-activated currents at -100 mV and smaller sustained currents at -30 mV. Our results indicate that the TREK subfamily of K2P channels might play an important role in the maintenance of the resting membrane potential in sensory neurons of the autonomic nervous system, suggesting its participation in the modulation of vagal reflexes.

Item Type: Article
DOI/Identification number: 10.1371/journal.pone.0199282
Subjects: Q Science
Divisions: Divisions > Division of Natural Sciences > Medway School of Pharmacy
Depositing User: Emma Veale
Date Deposited: 19 Aug 2019 21:39 UTC
Last Modified: 09 Dec 2022 08:43 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/75877 (The current URI for this page, for reference purposes)
Veale, Emma L.: https://orcid.org/0000-0002-6778-9929
Mathie, Alistair: https://orcid.org/0000-0001-6094-2890
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