Evidence map›Paper›PMID 24624333›Full record

ArticleRedox biology2014

Identification of DUOX1-dependent redox signaling through protein S-glutathionylation in airway epithelial cells.

Milena Hristova, Carmen Veith, Aida Habibovic, Ying-Wai Lam, Bin Deng, Miklos Geiszt, Yvonne M W Janssen-Heininger, Albert van der Vliet

Open access · goldAbstract read
In one paragraph

Article in Redox biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
0.9field-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

21 citing papers in PubMed, 28 citations in OpenAlex.

  1. Mitoquinone mesylate attenuates pathological features of lean and obese allergic asthma in mice.American journal of physiology. Lung cellular and molecular physiology · 2023
    Article
  2. Article
  3. Article
  4. DUOX1 in mammalian disease pathophysiology.Journal of molecular medicine (Berlin, Germany) · 2021
    Review
  5. Article
  6. Review
  7. Article
  8. The role of dual oxidases in physiology and cancer.Genetics and molecular biology · 2020
    Article
  9. Article
  10. Article
  11. Proteomic Methods to Evaluate NOX-Mediated Redox Signaling.Methods in molecular biology (Clifton, N.J.) · 2019
    Article
  12. Article
  13. Exosomes from asbestos-exposed cells modulate gene expression in mesothelial cells.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2018
    Article
  14. Article
  15. Review
  16. Article
  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

8 authors at 2 institutions in 2 countries.

Milena HristovaDepartment of Pathology, Vermont Lung Center, College of Medicine, University of Vermont, Burlington, VT 05405, United States.
Carmen VeithDepartment of Pathology, Vermont Lung Center, College of Medicine, University of Vermont, Burlington, VT 05405, United States.
Aida HabibovicDepartment of Pathology, Vermont Lung Center, College of Medicine, University of Vermont, Burlington, VT 05405, United States.
Ying-Wai LamDepartment of Biology, College of Arts and Sciences, University of Vermont, Burlington, VT 05405, United States.
Bin DengDepartment of Biology, College of Arts and Sciences, University of Vermont, Burlington, VT 05405, United States.
Miklos GeisztDepartment of Physiology, Faculty of Medicine, and "Lendulet" Peroxidase Enzyme Research Group, Semmelweis University, Budapest, Hungary.
Yvonne M W Janssen-HeiningerDepartment of Pathology, Vermont Lung Center, College of Medicine, University of Vermont, Burlington, VT 05405, United States.
Albert van der VlietDepartment of Pathology, Vermont Lung Center, College of Medicine, University of Vermont, Burlington, VT 05405, United States.
University of Vermont · USSemmelweis University · HU

Funding

Vermont INBRE Administrative Supplement 2024 AWD 118P20GM103449 · NIGMS · UNIVERSITY OF VERMONT & ST AGRIC COLLEGE · PI CHRISTOPHER S FRANCKLYN · 2012 to 2026
$58.4M
WEIGHT LOSS & ASTHMAP20RR015557 · NCRR · UNIVERSITY OF VERMONT &ST AGRIC COLLEGE · PI RINCON, MERCEDES · 2000 to 2009
$21.4M
REGULATION OF NFKB IN LUNG EPITHELIUM BY ROS/RNSR01HL060014 · NHLBI · UNIVERSITY OF VERMONT &ST AGRIC COLLEGE · PI JANSSEN-HEININGER, YVONNE M. W. · 1999 to 2016
$5.9M
Dual Oxidase in Airway Epithelial Repair and RemodelingR01HL085646 · NHLBI · UNIVERSITY OF VERMONT & ST AGRIC COLLEGE · PI VAN DER VLIET, ALBERT · 2008 to 2020
$4.7M
Redox-based Fas Signaling in Allergic Airway DiseaseR01HL079331 · NHLBI · UNIVERSITY OF VERMONT &ST AGRIC COLLEGE · PI JANSSEN-HEININGER, YVONNE M. W. · 2005 to 2016
$4.2M
NCRR NIH HHS P20 RR015557NCRR NIH HHS P20RR15557NHLBI NIH HHS HL079331NHLBI NIH HHS HL085646NHLBI NIH HHS R01 HL060014NHLBI NIH HHS R01 HL079331NHLBI NIH HHS R01 HL085646NIGMS NIH HHS 8P20GM103449NIGMS NIH HHS P20 GM103449
6 · The paper itself

Abstract

The NADPH oxidase homolog dual oxidase 1 (DUOX1) plays an important role in innate airway epithelial responses to infection or injury, but the precise molecular mechanisms are incompletely understood and the cellular redox-sensitive targets for DUOX1-derived H2O2 have not been identified. The aim of the present study was to survey the involvement of DUOX1 in cellular redox signaling by protein S-glutathionylation, a major mode of reversible redox signaling. Using human airway epithelial H292 cells and stable transfection with DUOX1-targeted shRNA as well as primary tracheal epithelial cells from either wild-type or DUOX1-deficient mice, DUOX1 was found to be critical in ATP-stimulated transient production of H2O2 and increased protein S-glutathionylation. Using cell pre-labeling with biotin-tagged GSH and analysis of avidin-purified proteins by global proteomics, 61 S-glutathionylated proteins were identified in ATP-stimulated cells compared to 19 in untreated cells. Based on a previously established role of DUOX1 in cell migration, various redox-sensitive proteins with established roles in cytoskeletal dynamics and/or cell migration were evaluated for S-glutathionylation, indicating a critical role for DUOX1 in ATP-stimulated S-glutathionylation of β-actin, peroxiredoxin 1, the non-receptor tyrosine kinase Src, and MAPK phosphatase 1. Overall, our studies demonstrate the importance of DUOX1 in epithelial redox signaling through reversible S-glutathionylation of a range of proteins, including proteins involved in cytoskeletal regulation and MAPK signaling pathways involved in cell migration.

Indexed as

Oxidation-ReductionAnimalsCell MovementCells, CulturedDual OxidasesEpithelial CellsGene Expression RegulationGlutathioneHumansLungMAP Kinase Signaling SystemMiceNADPH OxidasesProteomicsSignal TransductionTracheaDual OxidasesDUOX1 protein, humanDuox1 protein, mouseGlutathioneNADPH OxidasesCell migrationCysteineDUOX1NADPH oxidaseProteomicsS-glutathionylation

Identifiers

PMID24624333
PMCPMC3949091
OpenAlexW2091795975

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.