Evidence map›Paper›PMID 21340459›Full record

ArticlePflugers Archiv : European journal of physiology2011

Bimodal effect of alkalization on the polycystin transient receptor potential channel, PKD2L1.

Takahiro Shimizu, Taiga Higuchi, Takuto Fujii, Bernd Nilius, Hideki Sakai

Abstract read
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In one paragraph

Article in Pflugers Archiv : European journal of physiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
0.8field-weighted citation impact, top 29% 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

15 citing papers in PubMed, 25 citations in OpenAlex.

  1. Review
  2. Article
  3. Polycystin Channel Complexes.Annual review of physiology · 2023
    Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. A proton current associated with sour taste: distribution and functional properties.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2015
    Article
  12. Article
  13. Article
  14. Article
  15. 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

5 authors at 2 institutions in 2 countries.

Takahiro ShimizuDepartment of Pharmaceutical Physiology, Graduate School of Medicine and Pharmaceutical Sciences, University of Toyama, 2630 Sugitani, Toyama, 9300194, Japan. takshimi@pha.u-toyama.ac.jp
Taiga Higuchi
Takuto Fujii
Bernd Nilius
Hideki Sakai
University of Toyama · JPKU Leuven · BE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Polycystic kidney disease 2-like 1(PKD2L1), previously called transient receptor potential polycystin 3 (TRPP3), forms constitutively active voltage-dependent nonselective cation channels in the plasma membrane. The mechanism of regulation of PKD2L1 channels, however, has been poorly understood. In the present study, we found a bell-shaped alkaline pH dependence of PKD2L1 channel activity at the single-channel and whole-cell levels in patch-clamp recordings in HEK293T cells overexpressing mouse PKD2L1: alkalization to pH 8.0-9.0 increased the PKD2L1 currents, but alkalization to pH 10.0 decreased them. Single-channel analysis revealed that alkalization changed the open probability of PKD2L1 channels, but not their single-channel conductance. In addition, the voltage dependence of PKD2L1 channels was negatively and positively shifted by treatment with solutions of pH 8.0-9.0 and pH 10.0, respectively. These results indicate that the voltage-dependent gating of PKD2L1 channels was modulated by alkalization through two different mechanisms. Interestingly, we observed rebound activation of the PKD2L1 channel on washout of the alkaline solution after PKD2L1 channel inhibition at pH 10.0, suggesting that alkalization to pH 10.0 decreased PKD2L1 currents by inactivating the channels. Consistently, the PKD2L1 tail currents were accelerated by alkalization. These results suggest that alkalization is a bimodal modulator of mouse PKD2L1 channels.

Indexed as

AnimalsCalcium ChannelsHEK293 CellsHumansHydrogen-Ion ConcentrationIon Channel GatingMiceReceptors, Cell SurfaceCalcium ChannelsPkd2l1 protein, mouseReceptors, Cell Surface

Identifiers

PMID21340459
OpenAlexW2048638441

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.