Evidence map›Paper›PMID 15452196›Full record

ArticleThe Journal of general physiology2004

New insights on the voltage dependence of the KCa3.1 channel block by internal TBA.

Umberto Banderali, Hélène Klein, Line Garneau, Manuel Simoes, Lucie Parent, Rémy Sauvé

Abstract readComparative StudyEvaluation Study
In one paragraph

Article in The Journal of general physiology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

6 citing papers in PubMed.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors.

Umberto BanderaliDépartement de Physiologie, Membrane Protein Study Group, Université de Montréal, Montréal, Québec H3C 3J7, Canada.
Hélène Klein
Line Garneau
Manuel Simoes
Lucie Parent
Rémy Sauvé

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We present in this work a structural model of the open IKCa (KCa3.1) channel derived by homology modeling from the MthK channel structure, and used this model to compute the transmembrane potential profile along the channel pore. This analysis showed that the selectivity filter and the region extending from the channel inner cavity to the internal medium should respectively account for 81% and 16% of the transmembrane potential difference. We found however that the voltage dependence of the IKCa block by the quaternary ammonium ion TBA applied internally is compatible with an apparent electrical distance delta of 0.49 +/- 0.02 (n = 6) for negative potentials. To reconcile this observation with the electrostatic potential profile predicted for the channel pore, we modeled the IKCa block by TBA assuming that the voltage dependence of the block is governed by both the difference in potential between the channel cavity and the internal medium, and the potential profile along the selectivity filter region through an effect on the filter ion occupancy states. The resulting model predicts that delta should be voltage dependent, being larger at negative than positive potentials. The model also indicates that raising the internal K+ concentration should decrease the value of delta measured at negative potentials independently of the external K+ concentration, whereas raising the external K+ concentration should minimally affect delta for concentrations >50 mM. All these predictions are born out by our current experimental results. Finally, we found that the substitutions V275C and V275A increased the voltage sensitivity of the TBA block, suggesting that TBA could move further into the pore, thus leading to stronger interactions between TBA and the ions in the selectivity filter. Globally, these results support a model whereby the voltage dependence of the TBA block in IKCa is mainly governed by the voltage dependence of the ion occupancy states of the selectivity filter.

Indexed as

Models, BiologicalAnimalsComputer SimulationDose-Response Relationship, DrugHumansIntermediate-Conductance Calcium-Activated Potassium ChannelsIon Channel GatingMembrane PotentialsPotassiumPotassium Channels, Calcium-ActivatedQuaternary Ammonium CompoundsIntermediate-Conductance Calcium-Activated Potassium ChannelsKCNN4 protein, humanPotassiumPotassium Channels, Calcium-ActivatedQuaternary Ammonium Compoundstetrabutylammonium

Identifiers

PMID15452196
PMCPMC2233899

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.