ArticleThe Journal of general physiology2003
Rapid induction of P/C-type inactivation is the mechanism for acid-induced K+ current inhibition.
Article in The Journal of general physiology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Cell Settling, Migration, and Stochastic Cancer Gene Expression Suggest Potassium Membrane Flux May Initiate pH Reversal.Biomolecules · 2025Article
- Unmasking subtype-dependent susceptibility to C-type inactivation in mammalian Kv1 channels.Biophysical journal · 2024Article
- Article
- Shaker IR T449 mutants separate C- from U-type inactivation.The Journal of membrane biology · 2014Article
- ShakerIR and Kv1.5 mutant channels with enhanced slow inactivation also exhibit K⁺ o-dependent resting inactivation.Pflugers Archiv : European journal of physiology · 2013Article
- External Ba2+ block of human Kv1.5 at neutral and acidic pH: evidence for Ho+-induced constriction of the outer pore mouth at rest.Biophysical journal · 2008Article
- A direct demonstration of closed-state inactivation of K+ channels at low pH.The Journal of general physiology · 2007Article
- Na+ permeation and block of hERG potassium channels.The Journal of general physiology · 2006Article
- Single channel analysis reveals different modes of Kv1.5 gating behavior regulated by changes of external pH.Biophysical journal · 2006Article
- NH2-terminal inactivation peptide binding to C-type-inactivated Kv channels.The Journal of general physiology · 2004Article
- The external K+ concentration and mutations in the outer pore mouth affect the inhibition of kv1.5 current by Ni2+.Biophysical journal · 2004Article
- Mechanisms underlying modulation of neuronal KCNQ2/KCNQ3 potassium channels by extracellular protons.The Journal of general physiology · 2003Article
- Negative charges in the transmembrane domains of the HERG K channel are involved in the activation- and deactivation-gating processes.The Journal of general physiology · 2003Article
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4 authors.
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Abstract
Extracellular acidification is known to decrease the conductance of many voltage-gated potassium channels. In the present study, we investigated the mechanism of H(+)(o)-induced current inhibition by taking advantage of Na(+) permeation through inactivated channels. In hKv1.5, H(+)(o) inhibited open-state Na(+) current with a similar potency to K(+) current, but had little effect on the amplitude of inactivated-state Na(+) current. In support of inactivation as the mechanism for the current reduction, Na(+) current through noninactivating hKv1.5-R487V channels was not affected by [H(+)(o)]. At pH 6.4, channels were maximally inactivated as soon as sufficient time was given to allow activation, which suggested two possibilities for the mechanism of action of H(+)(o). These were that inactivation of channels in early closed states occurred while hyperpolarized during exposure to acid pH (closed-state inactivation) and/or inactivation from the open state was greatly accelerated at low pH. The absence of outward Na(+) currents but the maintained presence of slow Na(+) tail currents, combined with changes in the Na(+) tail current time course at pH 6.4, led us to favor the hypothesis that a reduction in the activation energy for the inactivation transition from the open state underlies the inhibition of hKv1.5 Na(+) current at low pH.
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