Evidence map›Paper›PMID 23401562›Full record

ArticleFASEB journal : official publication of the Federation of American Societies for Experimental Biology2013

p67(phox) terminates the phospholipase A(2)-derived signal for activation of NADPH oxidase (NOX2).

Saikumari Y Krishnaiah, Chandra Dodia, Sheldon I Feinstein, Aron B Fisher

Abstract read
In one paragraph

Article in FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

17 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Genetic inactivation of the phospholipase AAmerican journal of physiology. Lung cellular and molecular physiology · 2019
    Article
  6. The Role of Peroxiredoxin 6 in Cell Signaling.Antioxidants (Basel, Switzerland) · 2018
    Review
  7. The phospholipase AJournal of lipid research · 2018
    Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. 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

4 authors at 1 institution in 1 country.

Saikumari Y KrishnaiahInstitute for Environmental Medicine, University of Pennsylvania Perelman School of Medicine, Philadelphia, PA 19104, USA.
Chandra Dodia
Sheldon I Feinstein
Aron B Fisher
University of Pennsylvania · US

Funding

Role of Prdx6 in the activation of NADPH oxidaseR01HL105509 · NHLBI · UNIVERSITY OF PENNSYLVANIA · PI FISHER, ARON B. · 2011 to 2015
$2.6M
NHLBI NIH HHS HL 105509NHLBI NIH HHS R01 HL105509
6 · The paper itself

Abstract

The phospholipase A2 (PLA2)activity of phosphorylated peroxiredoxin 6 (Prdx6) is required for activation of NADPH oxidase (NOX2). We investigated the interaction of Prdx6 with p67(phox) and its effect on NOX2 activity. With the use of specific antibodies, coimmunoprecipitation of p67(phox) and phosphorylated Prdx6 was demonstrated with lysates of mouse pulmonary microvascular endothelial cells (MPMVECs) that were stimulated with angiotensin II; the interaction of p67(phox) with nonphosphorylated Prdx6 was relatively weak. Association of p67(phox) and phosphoPrdx6 in intact MPMVECs after angiotensin II stimulation was demonstrated by proximity ligation assay and was abolished by U0126, a MAP kinase inhibitor. By isothermal titration calorimetry, p67(phox) bound strongly to phosphoPrdx6 but bound poorly to Prdx6; phosphorylated p67(phox) did not bind to either Prdx6 or phosphoPrdx6. PLA2 activity of recombinant phosphoPrdx6 was decreased by >98% in the presence of p67(phox); the calculated dissociation constant (Kd) of the p67(phox): phosphoPrdx6 complex was 65 nM. PLA2 activity (MJ33 sensitive) in cell lysates following angiotensin II treatment of MPMVECs was increased by 85% following knockdown of p67(phox) with siRNA. These data indicate that p67(phox) binds to phosphoPrdx6 and inhibits its PLA2 activity, an interaction that could function to terminate the PLA2-mediated NOX2 activation signal.-Krishnaiah, S. Y., Dodia, C., Feinstein, S. I., and Fisher, A. B. p67(phox) terminates the phospholipase A2-derived signal for activation of NADPH oxidase (NOX2).

Indexed as

Angiotensin IIAnimalsButadienesEndothelial CellsHumansKineticsMembrane GlycoproteinsMiceNADPH Oxidase 2NADPH OxidasesNitrilesPeroxiredoxin VIPhospholipase A2 InhibitorsPhosphoproteinsPhosphorylationAngiotensin IIButadienesCybb protein, mouseMembrane GlycoproteinsNADPH Oxidase 2NADPH Oxidasesneutrophil cytosol factor 67KNitrilesPeroxiredoxin VIPhospholipase A2 InhibitorsPhosphoproteinsU 0126

Identifiers

PMID23401562
PMCPMC3633811
OpenAlexW2153437220

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.