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• W1968031887 startingPage "8950" @default.
• W1968031887 abstract "The inhibitory glycine receptor is a ligand-gated ion-channel protein existing in different homo- and heterooligomeric isoforms. Here we show that the chloride channel of the recombinant alpha 1-subunit homooligomeric glycine receptor is efficiently blocked by cyanotriphenylborate (CTB) with a concentration effecting 50% inhibition (IC50) of 1.3 microM in the presence of 50 microM glycine. The antagonistic effect of CTB is noncompetitive, use dependent, and more pronounced at positive membrane potentials, suggesting open-channel block. In contrast to alpha 1-subunit receptors, alpha 2-subunit homooligomers are resistant to CTB (IC50 >> 20 microM). By exchanging the channel-lining transmembrane segment M2 of the alpha 1 polypeptide by that of the alpha 2 polypeptide, we could transfer this resistance to alpha 1 channels, indicating that a single glycine residue at position 254 of the alpha 1 subunit is critical for CTB sensitivity. The blocker did not affect the cation-selective channel of the nicotinic acetylcholine receptor. Thus, CTB may prove useful as a tool to probe the subunit structure of native glycine receptors in mammalian neurons." @default.
• W1968031887 created "2016-06-24" @default.
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• W1968031887 date "1994-09-13" @default.
• W1968031887 modified "2023-09-25" @default.
• W1968031887 title "Cyanotriphenylborate: subtype-specific blocker of glycine receptor chloride channels." @default.
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• W1968031887 doi "https://doi.org/10.1073/pnas.91.19.8950" @default.
• W1968031887 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/44724" @default.
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