https://dx.doi.org/10.1371/journal.pone.0021970">
 

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Creative Commons Attribution 4.0 International License
This work is licensed under a Creative Commons Attribution 4.0 International License.

Abstract

Together, acid-sensing ion channels (ASICs) and epithelial sodium channels (ENaC) constitute the majority of voltage-independent sodium channels in mammals. ENaC is regulated by a chloride channel, the cystic fibrosis transmembrane conductance regulator (CFTR). Here we show that ASICs were reversibly inhibited by activation of GABAA receptors in murine hippocampal neurons. This inhibition of ASICs required opening of the chloride channels but occurred with both outward and inward GABAA receptor-mediated currents. Moreover, activation of the GABAA receptors modified the pharmacological features and kinetic properties of the ASIC currents, including the time course of activation, desensitization and deactivation. Modification of ASICs by open GABAA receptors was also observed in both nucleated patches and outside-out patches excised from hippocampal neurons. Interestingly, ASICs and GABAA receptors interacted to regulate synaptic plasticity in CA1 hippocampal slices. The activation of glycine receptors, which are similar to GABAA receptors, also modified ASICs in spinal neurons. We conclude that GABAA receptors and glycine receptors modify ASICs in neurons through mechanisms that require the opening of chloride channels.

Department

Molecular, Cellular and Biomedical Sciences

Publication Date

7-18-2011

Journal Title

PLOS One

Publisher

PLOS

Digital Object Identifier (DOI)

https://dx.doi.org/10.1371/journal.pone.0021970

Document Type

Article

Rights

© 2011 Chen et al.

Comments

This is an article published by PLOS in PLOS One in 2011, available online: https://dx.doi.org/10.1371/journal.pone.0021970

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