ArticleBiophysical journal1999
Proton and zinc effects on HERG currents.
Article in Biophysical journal, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 54 citations in OpenAlex.
- Cell Settling, Migration, and Stochastic Cancer Gene Expression Suggest Potassium Membrane Flux May Initiate pH Reversal.Biomolecules · 2025Article
- Chloroquine chaos and COVID-19: Smart delivery perspectives through pH sensitive polymers/micelles and ZnO nanoparticles.Arabian journal of chemistry · 2023Review
- hERG1 channel subunit composition mediates proton inhibition of rapid delayed rectifier potassium current (IThe Journal of biological chemistry · 2023Article
- Metabolic and electrolyte abnormalities as risk factors in drug-induced long QT syndrome.Biophysical reviews · 2022Review
- Modulation of hERG KFrontiers in pharmacology · 2020Review
- Identification of a proton sensor that regulates conductance and open time of single hERG channels.Scientific reports · 2019Article
- Extracellular protons accelerate hERG channel deactivation by destabilizing voltage sensor relaxation.The Journal of general physiology · 2019Article
- The direct modulatory activity of zinc toward ion channels.Integrative medicine research · 2015Review
- External protons destabilize the activated voltage sensor in hERG channels.European biophysics journal : EBJ · 2014Article
- External pH modulates EAG superfamily K+ channels through EAG-specific acidic residues in the voltage sensor.The Journal of general physiology · 2013Article
- Extracellular proton modulation of the cardiac voltage-gated sodium channel, Nav1.5.Biophysical journal · 2011Article
- Modification of hERG1 channel gating by Cd2+.The Journal of general physiology · 2010Article
- Fluorescence-tracking of activation gating in human ERG channels reveals rapid S4 movement and slow pore opening.PloS one · 2010Article
- Extracellular pH modulates the voltage-dependent Ca2+ current and low threshold K+ current in hair cells.Neurochemical research · 2008Article
- Localization of the ergtoxin-1 receptors on the voltage sensing domain of hERG K+ channel by AFM recognition imaging.Pflugers Archiv : European journal of physiology · 2008Article
- The zinc binding site of the Shaker channel KDC1 from Daucus carota.Biophysical journal · 2008Article
- Kir2.3 isoform confers pH sensitivity to heteromeric Kir2.1/Kir2.3 channels in HEK293 cells.Heart rhythm · 2007Article
- Molecular mapping of a site for Cd2+-induced modification of human ether-à-go-go-related gene (hERG) channel activation.The Journal of physiology · 2005Article
- The HERG K+ channel: progress in understanding the molecular basis of its unusual gating kinetics.European biophysics journal : EBJ · 2004Review
- Saxitoxin is a gating modifier of HERG K+ channels.The Journal of general physiology · 2003Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
The proton and Zn2+ effects on the human ether-a-go-go related gene (HERG) channels were studied after expression in Xenopus oocytes and stable transfection in the mammalian L929 cell line. Experiments were carried out using the two-electrode voltage clamp at room temperature (oocytes) or the whole-cell patch clamp technique at 35 degrees C (L929 cells). In oocytes, during moderate extracellular acidification (pHo = 6.4), current activation was not shifted on the voltage axis, the time course of current activation was unchanged, but tail current deactivation was dramatically accelerated. At pHo < 6.4, in addition to accelerating deactivation, the time course of activation was slower and the midpoint voltage of current activation was shifted to more positive values. Protons and Zn2+ accelerated the kinetics of deactivation with apparent Kd values about one order of magnitude lower than for tail current inhibition. For protons, the Kd values for the effect on tail current amplitude versus kinetics were, respectively, 1.8 microM (pKa = 5.8) and 0.1 microM (pKa = 7.0). In the presence of Zn2+, the corresponding Kd values were, respectively, 1.2 mM and 169 microM. In L929 cells, acidification to pHo = 6.4 did not shift the midpoint voltage of current activation and had no effect on the time course of current activation. Furthermore, the onset and recovery of inactivation were not affected. However, the acidification significantly accelerated tail current deactivation. We conclude that protons and Zn2+ directly interact with HERG channels and that the interaction results, preferentially, in the regulation of channel deactivation mechanism.
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