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• W2143712525 endingPage "2556" @default.
• W2143712525 startingPage "2545" @default.
• W2143712525 abstract "It has been shown that the voltage (V(m)) dependence of ClC Cl(-) channels is conferred by interaction of the protopore gate with H(+) ions. However, in this paper we present evidence which indicates that permeant Cl(-) ions contribute to V(m)-dependent gating of the broadly distributed ClC-2 Cl() channel. The apparent open probability (P(A)) of ClC-2 was enhanced either by changing the [Cl(-)](i) from 10 to 200 mM or by keeping the [Cl(-)](i) low (10 mM) and then raising [Cl(-)](o) from 10 to 140 mM. Additionally, these changes in [Cl(-)] slowed down channel closing at positive V(m) suggesting that high [Cl(-)] increased pore occupancy thus hindering closing of the protopore gate. The identity of the permeant anion was also important since the P(A)(V(m)) curves were nearly identical with Cl(-) or Br(-) but shifted to negative voltages in the presence of SCN() ions. In addition, gating, closing rate and reversal potential displayed anomalous mole fraction behaviour in a SCN(-)/Cl() mixture in agreement with the idea that pore occupancy by different permeant anions modifies the V(m) dependence ClC-2 gating. Based on the ec1-ClC anion pathway, we hypothesized that opening of the protopore gate is facilitated when Cl(-) ions dwell in the central binding site. In contrast, when Cl(-) ions dwell in the external binding site they prevent the gate from closing. Finally, this Cl(-)-dependent gating in ClC-2 channels is of physiological relevance since an increase in [Cl(-)](o) enhances channel opening when the [Cl(-)](i) is in the physiological range." @default.
• W2143712525 created "2016-06-24" @default.
• W2143712525 creator A5054784470 @default.
• W2143712525 creator A5057917562 @default.
• W2143712525 creator A5073251466 @default.
• W2143712525 date "2010-07-15" @default.
• W2143712525 modified "2023-10-15" @default.
• W2143712525 title "Permeant anions contribute to voltage dependence of ClC-2 chloride channel by interacting with the protopore gate" @default.
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• W2143712525 doi "https://doi.org/10.1113/jphysiol.2010.189175" @default.
• W2143712525 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2916987" @default.
• W2143712525 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/20498235" @default.
• W2143712525 hasPublicationYear "2010" @default.
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