Evidence map›Paper›PMID 12034764›Full record

ArticleThe Journal of general physiology2002

Absence of proton channels in COS-7 cells expressing functional NADPH oxidase components.

Deri Morgan, Vladimir V Cherny, Marianne O Price, Mary C Dinauer, Thomas E DeCoursey

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of general physiology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

26 citing papers in PubMed, 48 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Review
  5. Review
  6. Voltage-gated proton channels.Comprehensive Physiology · 2012
    Review
  7. NOX5 in human spermatozoa: expression, function, and regulation.The Journal of biological chemistry · 2012
    Article
  8. Review
  9. Article
  10. Review
  11. Article
  12. Voltage-gated proton channels maintain pH in human neutrophils during phagocytosis.Proceedings of the National Academy of Sciences of the United States of America · 2009
    Article
  13. Article
  14. Article
  15. Biodiversity of voltage sensor domain proteins.Pflugers Archiv : European journal of physiology · 2007
    Review
  16. Article
  17. Article
  18. Electron and proton transport by NADPH oxidases.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2005
    Review
  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

5 authors at 2 institutions in 1 country.

Deri MorganDepartment of Molecular Biophysics and Physiology, Rush Presbyterian St. Luke's Medical Center, 1750 W Harrison, Chicago, IL 60612, USA.
Vladimir V Cherny
Marianne O Price
Mary C Dinauer
Thomas E DeCoursey
Rush University Medical Center · USRiley Hospital for Children · US

Funding

STRUCTURE/FUNCTION ANALYSIS OF PHAGOCYTE PROTEINSR01HL045635 · NHLBI · INDIANA UNIV-PURDUE UNIV AT INDIANAPOLIS · PI DINAUER, MARY C · 1991 to 2009
$3.0M
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 HL 45635NHLBI NIH HHS HL 52671NHLBI NIH HHS HL 61437NHLBI NIH HHS R01 HL045635NHLBI NIH HHS R01 HL052671NHLBI NIH HHS R01 HL061437
6 · The paper itself

Abstract

Nicotinamide adenine dinucleotide phosphate (NADPH) oxidase is an enzyme of phagocytes that produces bactericidal superoxide anion (O(2)(-)) via an electrogenic process. Proton efflux compensates for the charge movement across the cell membrane. The proton channel responsible for the H(+) efflux was thought to be contained within the gp91(phox) subunit of NADPH oxidase, but recent data do not support this idea (DeCoursey, T.E., V.V. Cherny, D. Morgan, B.Z. Katz, and M.C. Dinauer. 2001. J. Biol. Chem. 276:36063-36066). In this study, we investigated electrophysiological properties and superoxide production of COS-7 cells transfected with all NADPH oxidase components required for enzyme function (COS(phox)). The 7D5 antibody, which detects an extracellular epitope of the gp91(phox) protein, labeled 96-98% of COS(phox) cells. NADPH oxidase was functional because COS(phox) (but not COS(WT)) cells stimulated by phorbol myristate acetate (PMA) or arachidonic acid (AA) produced superoxide anion. No proton currents were detected in either wild-type COS-7 cells (COS(WT)) or COS(phox) cells studied at pH(o) 7.0 and pH(i) 5.5 or 7.0. Anion currents that decayed at voltages positive to 40 mV were the only currents observed. PMA or AA did not elicit detectable H(+) current in COS(WT) or COS(phox) cells. Therefore, gp91(phox) does not function as a proton channel in unstimulated cells or in activated cells with a demonstrably functional oxidase.

Indexed as

ProtonsAnimalsChloridesCOS CellsMembrane GlycoproteinsMembrane PotentialsNADPH Oxidase 2NADPH OxidasesPhagocytesRespiratory BurstSuperoxidesChloridesCYBB protein, humanMembrane GlycoproteinsNADPH Oxidase 2NADPH OxidasesProtonsSuperoxides

Identifiers

PMID12034764
PMCPMC2233867
OpenAlexW1989432026

What OpenQuestion holds

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LicenceCC BY-NC-SA
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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.