Characterization of zebrafish GABA A receptor subunits.

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  • Additional Information
    • Source:
      Publisher: Nature Publishing Group Country of Publication: England NLM ID: 101563288 Publication Model: Electronic Cited Medium: Internet ISSN: 2045-2322 (Electronic) Linking ISSN: 20452322 NLM ISO Abbreviation: Sci Rep Subsets: MEDLINE
    • Publication Information:
      Original Publication: London : Nature Publishing Group, copyright 2011-
    • Subject Terms:
    • Abstract:
      γ-Aminobutyric acid (GABA), the major inhibitory neurotransmitter in the central nervous system, exerts its effect through the activation of GABA receptors. GABA A receptors are ligand-gated chloride channels composed of five subunit proteins. Mammals have 19 different GABA A receptor subunits (α1-6, β1-3, γ1-3, δ, ε, π, θ, and ρ1-3), the physiological properties of which have been assayed by electrophysiology. However, the evolutionary conservation of the physiological characteristics of diverged GABA A receptor subunits remains unclear. Zebrafish have 23 subunits (α1, α2a, α2b, α3-5, α6a, α6b, β1-4, γ1-3, δ, π, ζ, ρ1, ρ2a, ρ2b, ρ3a, and ρ3b), but the electrophysiological properties of these subunits have not been explored. In this study, we cloned the coding sequences for zebrafish GABA A receptor subunits and investigated their expression patterns in larval zebrafish by whole-mount in situ hybridization. We also performed electrophysiological recordings of GABA-evoked currents from Xenopus oocytes injected with one or multiple zebrafish GABA A receptor subunit cRNAs and calculated the half-maximal effective concentrations (EC50s) for each. Our results revealed the spatial expressions and electrophysiological GABA sensitivities of zebrafish GABA A receptors, suggesting that the properties of GABA A receptor subunits are conserved among vertebrates.
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    • Accession Number:
      0 (Protein Subunits)
      0 (Receptors, GABA-A)
      0 (Recombinant Proteins)
      0 (Zebrafish Proteins)
      56-12-2 (gamma-Aminobutyric Acid)
    • Publication Date:
      Date Created: 20210319 Date Completed: 20211015 Latest Revision: 20211015
    • Publication Date:
      20231215
    • Accession Number:
      PMC7973766
    • Accession Number:
      10.1038/s41598-021-84646-3
    • Accession Number:
      33737538