Evidence map›Paper›PMID 21704744›Full record

ArticleJournal of proteomics2011

Proteomic profiling of acrolein adducts in human lung epithelial cells.

Page C Spiess, Bin Deng, Robert J Hondal, Dwight E Matthews, Albert van der Vliet

Abstract readEvaluation StudyValidation Study
In one paragraph

Article in Journal of proteomics, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
2.9field-weighted citation impact, top 9% 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

34 citing papers in PubMed, 65 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Review
  6. Article
  7. Histone variant H2B.Z acetylation is necessary for maintenance ofbioRxiv : the preprint server for biology · 2023
    Article
  8. Article
  9. Chemical research in toxicology · 2020
    Article
  10. Cardiac toxicity of acrolein exposure in embryonic zebrafish (Danio rerio).Environmental science and pollution research international · 2020
    Article
  11. Article
  12. Review
  13. Review
  14. Determination of Protein Haptenation by Chemical Sensitizers Within the Complexity of the Human Skin Proteome.Toxicological sciences : an official journal of the Society of Toxicology · 2018
    Article
  15. Article
  16. Article
  17. Article
  18. Oxidative stress and lipotoxicity.Journal of lipid research · 2016
    Review
  19. Review
  20. 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

5 authors at 1 institution in 1 country.

Page C SpiessDepartment of Pathology, University of Vermont, Burlington, VT 05405, USA.
Bin Deng
Robert J Hondal
Dwight E Matthews
Albert van der Vliet
University of Vermont · US

Funding

VOLATILE SIGNALING IN PHARBITIS NILP20RR016462 · NCRR · UNIVERSITY OF VERMONT &ST AGRIC COLLEGE · PI KIRSHENBAUM, ARI PHILLIP · 2001 to 2011
$31.1M
ENVIRONMENTAL PATHOLOGY TRAINING PROGRAMT32ES007122 · NIEHS · UNIVERSITY OF VERMONT &ST AGRIC COLLEGE · PI VAN DER VLIET, ALBERT · 1985 to 2012
$4.2M
Cigarette Smoke-derived Electrophilic Aldehydes and Airway InflammationR01ES021476 · NIEHS · UNIVERSITY OF VERMONT & ST AGRIC COLLEGE · PI VAN DER VLIET, ALBERT · 2012 to 2016
$1.9M
TOXIC ALDEHYDES AS MODULATORS OF LUNG INFLAMMATIONR01HL068865 · NHLBI · UNIVERSITY OF VERMONT &ST AGRIC COLLEGE · PI VAN DER VLIET, ALBERT · 2003 to 2007
$1.5M
NCRR NIH HHS P20 RR016462NCRR NIH HHS P20-RR16462NHLBI NIH HHS R01 HL068865NHLBI NIH HHS R01-HL068865NIEHS NIH HHS R01 ES021476NIEHS NIH HHS T-28ES007122NIEHS NIH HHS T32 ES007122
6 · The paper itself

Abstract

Acrolein (2,3-propenal) is a major indoor and outdoor air pollutant originating largely from tobacco smoke or organic combustion. Given its high reactivity, the adverse effects of inhaled acrolein are likely due to direct interactions with the airway epithelium, resulting in altered epithelial function, but only limited information exists to date regarding the primary direct cellular targets for acrolein. Here, we describe a global proteomics approach to characterize the spectrum of airway epithelial protein targets for Michael adduction in acrolein-exposed bronchial epithelial (HBE1) cells, based on biotin hydrazide labeling and avidin purification of biotinylated proteins or peptides for analysis by LC-MS/MS. Identified protein targets included a number of stress proteins, cytoskeletal proteins, and several key proteins involved in redox signaling, including thioredoxin reductase, thioredoxin, peroxiredoxins, and glutathione S-transferase π. Because of the central role of thioredoxin reductase in cellular redox regulation, additional LC-MS/MS characterization was performed on purified mitochondrial thioredoxin reductase to identify the specific site of acrolein adduction, revealing the catalytic selenocysteine residue as the target responsible for enzyme inactivation. Our findings indicate that these approaches are useful in characterizing major protein targets for acrolein, and will enhance mechanistic understanding of the impact of acrolein on cell biology.

Indexed as

ProteomicsAcroleinAir PollutantsCells, CulturedChromatography, LiquidEpithelial CellsHumansLungMass SpectrometryMetabolomeModels, BiologicalProtein Processing, Post-TranslationalProteinsRespiratory MucosaAcroleinAir PollutantsProteins

Identifiers

PMID21704744
PMCPMC3196826
OpenAlexW2068425444

What OpenQuestion holds

Textmetadata
LicenceTDM
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.