Evidence map›Paper›PMID 19720960›Full record

ArticleThe Journal of general physiology2009

Temperature dependence of proton permeation through a voltage-gated proton channel.

Miyuki Kuno, Hiroyuki Ando, Hirokazu Morihata, Hiromu Sakai, Hiroyuki Mori, Makoto Sawada, Shigetoshi Oiki

Open access · bronzeAbstract readEvaluation Study
In one paragraph

Article in The Journal of general physiology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

37 citing papers in PubMed, 55 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Temperature Dependent Activity of the Voltage-Gated Proton Channel.Advances in experimental medicine and biology · 2024
    Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. HistidineThe Journal of general physiology · 2018
    Article
  10. Review
  11. CrossTalk proposal: Proton permeation through HThe Journal of physiology · 2017
    Article
  12. Article
  13. Article
  14. The Hv1 proton channel responds to mechanical stimuli.The Journal of general physiology · 2016
    Article
  15. Review
  16. Review
  17. Article
  18. Article
  19. Article
  20. Review
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

7 authors at 4 institutions in 1 country.

Miyuki KunoDepartment of Physiology, Osaka City University Graduate School of Medicine, Abeno-ku, Osaka 545-8585, Japan.
Hiroyuki Ando
Hirokazu Morihata
Hiromu Sakai
Hiroyuki Mori
Makoto Sawada
Shigetoshi Oiki
Osaka City University · JPUniversity of Fukui · JPNagoya University · JPNational Institute for Physiological Sciences · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Voltage-gated proton channels are found in many different types of cells, where they facilitate proton movement through the membrane. The mechanism of proton permeation through the channel is an issue of long-term interest, but it remains an open question. To address this issue, we examined the temperature dependence of proton permeation. Under whole cell recordings, rapid temperature changes within a few milliseconds were imposed. This method allowed for the measurement of current amplitudes immediately before and after a temperature jump, from which the ratios of these currents (Iratio) were determined. The use of Iratio for evaluating the temperature dependence minimized the contributions of factors other than permeation. Temperature jumps of various degrees (DeltaT, -15 to 15 degrees C) were applied over a wide temperature range (4-49 degrees C), and the Q10s for the proton currents were evaluated from the Iratios. Q10 exhibited a high temperature dependence, varying from 2.2 at 10 degrees C to 1.3 at 40 degrees C. This implies that processes with different temperature dependencies underlie the observed Q10. A novel resistivity pulse method revealed that the access resistance with its low temperature dependence predominated in high temperature ranges. The measured temperature dependence of Q10 was decomposed into Q10 of the channel and of the access resistances. Finally, the Q10 for proton permeation through the voltage-gated proton channel itself was calculated and found to vary from 2.8 at 5 degrees C to 2.2 at 45 degrees C, as expected for an activation enthalpy of 64 kJ/mol. The thermodynamic features for proton permeation through proton-selective channels were discussed for the underlying mechanism.

Indexed as

ProtonsTemperatureAnimalsCells, CulturedCytosolIon ChannelsMicrogliaPatch-Clamp TechniquesRatsIon ChannelsProtons

Identifiers

PMID19720960
PMCPMC2740922
OpenAlexW2165682946

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.