Evidence map›Paper›PMID 15216414›Full record

ArticleThe Journal of membrane biology2004

Permeant anions control gating of calcium-dependent chloride channels.

P Perez-Cornejo, J A De Santiago, J Arreola

Abstract readComparative Study
PubMed Publisher
In one paragraph

Article in The Journal of membrane biology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
0.7field-weighted citation impact, top 32% of its field
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

24 citing papers in PubMed, 38 citations in OpenAlex.

  1. Article
  2. Article
  3. Structure-Function of TMEM16 Ion Channels and Lipid Scramblases.Advances in experimental medicine and biology · 2021
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  14. Four basic residues critical for the ion selectivity and pore blocker sensitivity of TMEM16A calcium-activated chloride channels.Proceedings of the National Academy of Sciences of the United States of America · 2015
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  15. Review
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  19. Voltage- and calcium-dependent gating of TMEM16A/Ano1 chloride channels are physically coupled by the first intracellular loop.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  20. Article
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

3 authors at 2 institutions in 2 countries.

P Perez-CornejoSchool of Medicine, Universidad Autonoma de San Luis Potosi, 78290, Mexico.
J A De Santiago
J Arreola
Autonomous University of San Luis Potosí · MXUniversity of Rochester Medical Center · US

Funding

MECHANISMS OF ANION TRANSPORT PROTEINS IN SALIVARY CELLSR01DE009692 · NIDCR · UNIVERSITY OF ROCHESTER · PI MELVIN, JAMES E · 1991 to 2010
$4.7M
NIDCR NIH HHS DE-09692
6 · The paper itself

Abstract

The effects of external anions (SCN(-), NO3-, I(-), Br(-), F(-), glutamate, and aspartate) on gating of Ca(2+)-dependent Cl(-) channels from rat parotid acinar cells were studied using the whole-cell configuration of the patch-clamp technique. Shifts in the reversal potential of the current induced by replacement of external Cl(-) with foreign anions, gave the following selectivity sequence based on permeability ratios ( P(x)/ P(Cl)): SCN(-)>I(-)>NO3->Br(-)>Cl(-)>F(-)>aspartate>glutamate. Using a continuum electrostatic model we calculated that this lyotropic sequence resulted from the interaction between anions and a polarizable tunnel with an effective dielectric constant of approximately 23. Our data revealed that anions with P(x)/P(Cl) > 1 accelerated activation kinetics in a voltage-independent manner and slowed deactivation kinetics. Moreover, permeant anions enhanced whole-cell conductance ( g, an index of the apparent open probability) in a voltage-dependent manner, and shifted leftward the membrane potential- g curves. All of these effects were produced by the anions with an effectiveness that followed the selectivity sequence. To explain the effects of permeant anions on activation kinetics and g(Cl) we propose that there are 2 different anion-binding sites in the channel. One site is located outside the electrical field and controls channel activation kinetics, while a second site is located within the pore and controls whole-cell conductance. Thus, interactions of permeant anions with these two sites hinder the closing mechanism and stabilize the channel in the open state.

Indexed as

AnimalsAnionsCalciumCell Membrane PermeabilityCells, CulturedChloride ChannelsChlorineIon Channel GatingKineticsMaleMembrane PotentialsParotid GlandRatsRats, WistarSensitivity and SpecificityAnionsCalciumChloride ChannelsChlorine

Identifiers

PMID15216414
OpenAlexW2073916104

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.