Evidence map›Paper›PMID 22761781›Full record

ArticlePloS one2012

Peroxiredoxin 3 is a redox-dependent target of thiostrepton in malignant mesothelioma cells.

Kheng Newick, Brian Cunniff, Kelsey Preston, Paul Held, Jack Arbiser, Harvey Pass, Brooke Mossman, Arti Shukla, Nicholas Heintz

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
4.0field-weighted citation impact, top 5% 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

35 citing papers in PubMed, 72 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Thiostrepton as a Potential Therapeutic Agent for Hepatocellular Carcinoma.International journal of molecular sciences · 2024
    Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Review
  11. Article
  12. Review
  13. The Role of Peroxiredoxin Family in Cancer Signaling.Journal of cancer prevention · 2019
    Review
  14. Article
  15. Peroxiredoxins in Cancer and Response to Radiation Therapies.Antioxidants (Basel, Switzerland) · 2019
    Review
  16. Review
  17. Review
  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

9 authors at 4 institutions in 1 country.

Kheng NewickDepartment of Pathology, University of Vermont College of Medicine, Burlington, Vermont, United States of America.
Brian Cunniff
Kelsey Preston
Paul Held
Jack Arbiser
Harvey Pass
Brooke Mossman
Arti Shukla
Nicholas Heintz
University of Vermont · USEmory University · USGreen Tech Labs (United States) · USNYU Langone Health · US

Funding

ENVIRONMENTAL PATHOLOGY TRAINING PROGRAMT32ES007122 · NIEHS · UNIVERSITY OF VERMONT &ST AGRIC COLLEGE · PI VAN DER VLIET, ALBERT · 1985 to 2012
$4.2M
NIEHS NIH HHS T32 ES007122NIEHS NIH HHS T32 ES007122-29
6 · The paper itself

Abstract

Thiostrepton (TS) is a thiazole antibiotic that inhibits expression of FOXM1, an oncogenic transcription factor required for cell cycle progression and resistance to oncogene-induced oxidative stress. The mechanism of action of TS is unclear and strategies that enhance TS activity will improve its therapeutic potential. Analysis of human tumor specimens showed FOXM1 is broadly expressed in malignant mesothelioma (MM), an intractable tumor associated with asbestos exposure. The mechanism of action of TS was investigated in a cell culture model of human MM. As for other tumor cell types, TS inhibited expression of FOXM1 in MM cells in a dose-dependent manner. Suppression of FOXM1 expression and coincidental activation of ERK1/2 by TS were abrogated by pre-incubation of cells with the antioxidant N-acetyl-L-cysteine (NAC), indicating its mechanism of action in MM cells is redox-dependent. Examination of the mitochondrial thioredoxin reductase 2 (TR2)-thioredoxin 2 (TRX2)-peroxiredoxin 3 (PRX3) antioxidant network revealed that TS modifies the electrophoretic mobility of PRX3. Incubation of recombinant human PRX3 with TS in vitro also resulted in PRX3 with altered electrophoretic mobility. The cellular and recombinant species of modified PRX3 were resistant to dithiothreitol and SDS and suppressed by NAC, indicating that TS covalently adducts cysteine residues in PRX3. Reduction of endogenous mitochondrial TRX2 levels by the cationic triphenylmethane gentian violet (GV) promoted modification of PRX3 by TS and significantly enhanced its cytotoxic activity. Our results indicate TS covalently adducts PRX3, thereby disabling a major mitochondrial antioxidant network that counters chronic mitochondrial oxidative stress. Redox-active compounds like GV that modify the TR2/TRX2 network may significantly enhance the efficacy of TS, thereby providing a combinatorial approach for exploiting redox-dependent perturbations in mitochondrial function as a therapeutic approach in mesothelioma.

Indexed as

Anti-Bacterial AgentsDose-Response Relationship, DrugForkhead Box Protein M1Forkhead Transcription FactorsHumansLung NeoplasmsMesotheliomaMesothelioma, MalignantMitochondriaOxidation-ReductionPeroxiredoxin IIISignal TransductionSuperoxidesThiostreptonTumor Cells, CulturedAnti-Bacterial AgentsForkhead Box Protein M1Forkhead Transcription FactorsFOXM1 protein, humanPeroxiredoxin IIISuperoxidesThiostrepton

Identifiers

PMID22761781
PMCPMC3382597
OpenAlexW2042552693

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.