Evidence map›Paper›PMID 16195320›Full record

ArticleThe Journal of physiology2005

The pH dependence of NADPH oxidase in human eosinophils.

Deri Morgan, Vladimir V Cherny, Ricardo Murphy, Ben Z Katz, Thomas E DeCoursey

Open access · greenAbstract read
In one paragraph

Article in The Journal of physiology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
1.0field-weighted citation impact, top 26% 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

51 citing papers in PubMed, 93 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Transcendent Aspects of Proton Channels.Annual review of physiology · 2024
    Review
  6. LRRC8A anion channels modulate vascular reactivity via association with myosin phosphatase rho interacting protein.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2023
    Article
  7. Review
  8. Review
  9. Review
  10. Review
  11. Expression of HProceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  12. Article
  13. Article
  14. Article
  15. Voltage and pH sensing by the voltage-gated proton channel, HJournal of the Royal Society, Interface · 2018
    Review
  16. Article
  17. Article
  18. Article
  19. The Hv1 proton channel responds to mechanical stimuli.The Journal of general physiology · 2016
    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

5 authors at 2 institutions in 1 country.

Deri MorganDepartment of Molecular Biophysics and Physiology, Rush University Medical Center, 1750 West Harrison, Chicago, IL 60612, USA.
Vladimir V Cherny
Ricardo Murphy
Ben Z Katz
Thomas E DeCoursey
Rush University Medical Center · USLurie Children's Hospital · US

Funding

VOLTAGE-GATED PROTON CHANNELS IN HUMAN NEUTROPHILSR01HL061437 · NHLBI · RUSH UNIVERSITY MEDICAL CENTER · PI DECOURSEY, THOMAS E · 2000 to 2008
$2.6M
VOLTAGE-GATED PROTON CHANNELS IN ALVEOLAR EPITHELIUMR01HL052671 · NHLBI · RUSH UNIVERSITY MEDICAL CENTER · PI DECOURSEY, THOMAS E · 1995 to 2003
$1.3M
NHLBI NIH HHS HL52671NHLBI NIH HHS HL61437NHLBI NIH HHS R01 HL052671NHLBI NIH HHS R01 HL061437
6 · The paper itself

Abstract

NADPH oxidase generates reactive oxygen species that are essential to innate immunity against microbes. Like most enzymes, it is sensitive to pH, although the relative importance of pH(o) and pH(i) has not been clearly distinguished. We have taken advantage of the electrogenic nature of NADPH oxidase to determine its pH dependence in patch-clamped individual human eosinophils using the electron current to indicate enzyme activity. Electron current stimulated by PMA (phorbol myristate acetate) was recorded in both perforated-patch configuration, using an NH4+ gradient to control pH(i), and in excised, inside-out patches of membrane. No electron current was detected in cells or excised patches from eosinophils from a patient with chronic granulomatous disease. When the pH was varied symmetrically (pH(o) = pH(i)) in cells in perforated-patch configuration, NADPH oxidase-generated electron current was maximal at pH 7.5, decreasing drastically at higher or lower values. Varying pH(o) and pH(i) independently revealed that this pH dependence was entirely due to effects of pH(i) and that the oxidase is insensitive to pH(o). Surprisingly, the electron current in inside-out patches of membrane was only weakly sensitive to pH(i), indicating that the enzyme turnover rate per se is not strongly pH dependent. The most likely interpretation is that assembly or deactivation of the NADPH oxidase complex has one or more pH-sensitive steps, and that pH-dependent changes in electron current in intact cells mainly reflect different numbers of active complexes at different pH.

Indexed as

AdultEnzyme ActivationEosinophilsGranulomatous Disease, ChronicHumansHydrogen-Ion ConcentrationMembrane PotentialsNADPH OxidasesPatch-Clamp TechniquesRespiratory BurstTetradecanoylphorbol AcetateNADPH OxidasesTetradecanoylphorbol Acetate

Identifiers

PMID16195320
PMCPMC1464255
OpenAlexW1574274689

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.