Evidence map›Paper›PMID 20498235›Full record

ArticleThe Journal of physiology2010

Permeant anions contribute to voltage dependence of ClC-2 chloride channel by interacting with the protopore gate.

Jorge E Sánchez-Rodríguez, José A De Santiago-Castillo, Jorge Arreola

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of physiology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.1field-weighted citation impact, top 23% 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

14 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
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  5. Article
  6. Glial Chloride Channels in the Function of the Nervous System Across Species.Advances in experimental medicine and biology · 2021
    Article
  7. Article
  8. Article
  9. Research and progress on ClC‑2 (Review).Molecular medicine reports · 2017
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. 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
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 1 institution in 1 country.

Jorge E Sánchez-RodríguezInstituto de Física, Universidad Autónoma de San Luis Potosí, Av. Dr Manuel Nava no. 6, Zona Universitaria, San Luis Potosí, SLP 78290, México.
José A De Santiago-Castillo
Jorge Arreola
Autonomous University of San Luis Potosí · MX

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

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.

Indexed as

AnimalsCells, CulturedChloride ChannelsChloridesCLC-2 Chloride ChannelsIon Channel GatingMiceParotid GlandThiocyanatesChloride ChannelsChloridesCLC-2 Chloride ChannelsthiocyanateThiocyanates

Identifiers

PMID20498235
PMCPMC2916987
OpenAlexW2143712525

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.