Evidence map›Paper›PMID 26210445›Full record

ArticleRedox biology2015

Redox regulation of metabolic and signaling pathways by thioredoxin and glutaredoxin in NOS-3 overexpressing hepatoblastoma cells.

Raúl González, M José López-Grueso, Jordi Muntané, J Antonio Bárcena, C Alicia Padilla

Open access · goldAbstract read
In one paragraph

Article in Redox biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

15 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
  2. The Redox Enzyme Thioredoxin Is Increased in Plasma Extracellular Vesicles From Endurance-Trained Females in Response to Acute Exercise.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025
    Article
  3. Review
  4. A Prognostic Activity of Glutaredoxin 1 Protein (Grx1) in Colon Cancer.International journal of molecular sciences · 2024
    Article
  5. Glutathione-Related Enzymes and Proteins: A Review.Molecules (Basel, Switzerland) · 2023
    Review
  6. Article
  7. Article
  8. Review
  9. Review
  10. Progress in the mechanism and targeted drug therapy for COPD.Signal transduction and targeted therapy · 2020
    Review
  11. Article
  12. 6-Phosphofructo-2-Kinase/Fructose-2,6-Biphosphatase-2 Regulates TP53-Dependent Paclitaxel Sensitivity in Ovarian and Breast Cancers.Clinical cancer research : an official journal of the American Association for Cancer Research · 2019
    Article
  13. Article
  14. Article
  15. 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 3 institutions in 1 country.

Raúl GonzálezDepartamento de Bioquímica y Biología Molecular, Universidad de Córdoba, Córdoba, Spain; Instituto Maimónides de Investigación Biomédica de Córdoba (IMIBIC), Córdoba, Spain. Electronic address: raulangello@hotmail.com.
M José López-GruesoDepartamento de Bioquímica y Biología Molecular, Universidad de Córdoba, Córdoba, Spain.
Jordi MuntanéDepartamento de Cirugía General, Hospital Universitario Virgen del Rocío/Instituto de Biomedicina de Sevilla (IBiS)/CSIC/Universidad de Sevilla, Sevilla, Spain; Centro de Investigación Biomédica en Red de Enfermedades Hepáticas y Digestivas (CIBERehd), Spain.
J Antonio BárcenaDepartamento de Bioquímica y Biología Molecular, Universidad de Córdoba, Córdoba, Spain; Instituto Maimónides de Investigación Biomédica de Córdoba (IMIBIC), Córdoba, Spain.
C Alicia PadillaDepartamento de Bioquímica y Biología Molecular, Universidad de Córdoba, Córdoba, Spain; Instituto Maimónides de Investigación Biomédica de Córdoba (IMIBIC), Córdoba, Spain.
Instituto Maimónides de Investigación Biomédica de Córdoba · ESCentro de Investigación Biomédica en Red de Enfermedades Hepáticas y Digestivas · ESUniversity of Córdoba · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nitric oxide (NO) plays relevant roles in signal transduction in physiopathology and its effects are dependent on several environmental factors. NO has both pro-apoptotic and anti-apoptotic functions but the molecular mechanisms responsible for these opposite effects are not fully understood. The action of NO occurs mainly through redox changes in target proteins, particularly by S-nitrosylation of reactive cysteine residues. Thioredoxin (Trx) and glutaredoxin (Grx) systems are the main cellular controllers of the thiolic redox state of proteins exerting controversial effects on apoptosis with consequences for the resistance to or the development of cancer. The aim of this study was to ascertain whether Trx and/or Grx systems mediate the antiproliferative effect of NO on hepatoblastoma cells by modulating the redox-state of key proteins. Proliferation decreased and apoptosis increased in HepG2 cells overexpressing Nitric Oxide Synthase-3 (NOS-3) as a result of multilevel cellular responses to the oxidative environment generated by NO. Enzyme levels and cysteine redox state at several metabolic checkpoints were consistent with prominence of the pentose phosphate pathway to direct the metabolic flux toward NADPH for antioxidant defense and lowering of nucleotide biosynthesis and hence proliferation. Proteins involved in cell survival pathways, proteins of the redoxin systems and phosphorylation of MAPK were all significantly increased accompanied by a shift of the thiolic redox state of Akt1, Trx1 and Grx1 to more oxidized. Silencing of Trx1 and Grx1 neutralized the increases in CD95, Akt1 and pAkt levels induced by NO and produced a marked increase in caspase-3 and -8 activities in both control and NOS-3 overexpressing cells concomitant with a decrease in the number of cells. These results demonstrate that the antiproliferative effect of NO is actually hampered by Trx1 and Grx1 and support the strategy of weakening the thiolic antioxidant defenses when designing new antitumoral therapies.

Indexed as

Gene Expression Regulation, NeoplasticCaspase 3Caspase 8Cell ProliferationCell SurvivalCysteinefas ReceptorGlutaredoxinsHep G2 CellsHumansNADPNitric OxideNitric Oxide Synthase Type IIIOxidation-ReductionPhosphorylationProto-Oncogene Proteins c-aktAKT1 protein, humanCASP3 protein, humanCASP8 protein, humanCaspase 3Caspase 8CysteineFAS protein, humanfas ReceptorGLRX protein, humanGlutaredoxinsNADPNitric OxideNitric Oxide Synthase Type IIINOS3 protein, humanProto-Oncogene Proteins c-aktRNA, Small InterferingThioredoxinsTXN protein, humanApoptosisCancerGlutaredoxinOxidative/nitrosative stressThioredoxin

Identifiers

PMID26210445
PMCPMC4528045
OpenAlexW1522839402

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.