Evidence map›Paper›PMID 17210449›Full record

ArticleFree radical biology & medicine2007

Selective protection of nuclear thioredoxin-1 and glutathione redox systems against oxidation during glucose and glutamine deficiency in human colonic epithelial cells.

Young-Mi Go, Thomas R Ziegler, Jennifer M Johnson, Li Gu, Jason M Hansen, Dean P Jones

Open access · greenAbstract read
In one paragraph

Article in Free radical biology & medicine, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

42 citing papers in PubMed, 72 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Review
  8. Review
  9. Redox theory of aging: implications for health and disease.Clinical science (London, England : 1979) · 2017
    Review
  10. The cysteine proteome.Free radical biology & medicine · 2015
    Review
  11. Integrated redox proteomics and metabolomics of mitochondria to identify mechanisms of cd toxicity.Toxicological sciences : an official journal of the Society of Toxicology · 2014
    Article
  12. Article
  13. Review
  14. Review
  15. Article
  16. Review
  17. Annexin A2: the importance of being redox sensitive.International journal of molecular sciences · 2013
    Article
  18. Increased nuclear thioredoxin-1 potentiates cadmium-induced cytotoxicity.Toxicological sciences : an official journal of the Society of Toxicology · 2013
    Article
  19. Article
  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

6 authors at 1 institution in 1 country.

Young-Mi GoDivision of Pulmonary Medicine, Emory University, Atlanta, GA 30322, USA.
Thomas R Ziegler
Jennifer M Johnson
Li Gu
Jason M Hansen
Dean P Jones
Emory University · US

Funding

Thioredoxin-2 protection against mitochondrial oxidative toxicityR01ES009047 · NIEHS · EMORY UNIVERSITY · PI JONES, DEAN PAUL · 1998 to 2013
$3.9M
Nuclear and Cytoplasmic Redox in Oxidative StressR01ES011195 · NIEHS · EMORY UNIVERSITY · PI JONES, DEAN PAUL · 2001 to 2011
$3.3M
NIEHS NIH HHS ES011195NIEHS NIH HHS ES09047NIEHS NIH HHS R01 ES009047NIEHS NIH HHS R01 ES011195
6 · The paper itself

Abstract

Little is known about the relative sensitivities of antioxidant systems in nuclei, mitochondria, and cytoplasm. The present study examined the oxidation of the thiol-dependent antioxidant systems in these subcellular compartments under conditions of limited energy supply of human colonic epithelial HT-29 cells induced by depletion of glucose (Glc) and glutamine (Gln) from the culture medium. Increased oxidation of dichlorofluoroscein (DCF) indicated an increased level of reactive oxygen species (ROS). Redox Western blot analysis showed oxidation of cytosolic thioredoxin-1 (Trx1) and mitochondrial thioredoxin-2 (Trx2) by 24 h, but little oxidation of nuclear Trx1. The Trx1 substrate, redox factor-1 (Ref-1), was also oxidized in cytosol but was reduced in nuclei. Protein S-glutathionylation (PrSSG), expressed as a ratio of protein thiol (PrSH), was also increased in the cytosol, while nuclear PrSSG/PrSH was not. Taken together, the data show that oxidative stress induced by depletion of Glc and Gln affects the redox states of proteins in the cytoplasm and mitochondria more than those in the nucleus. These results indicate that the nuclear compartment has better protection against oxidative stress than cytoplasm or mitochondria. These results further suggest that energy and/or substrate supply may contribute to sensitivity of mitochondrial and cytoplasmic systems to oxidative damage.

Indexed as

Cell LineCell NucleusColonCytosolDNA-(Apurinic or Apyrimidinic Site) LyaseEpithelial CellsFluoresceinsFluorescent DyesGlucoseGlutamineGlutathioneHumansMembrane ProteinsMitochondriaMitochondrial ProteinsOxidation-Reduction2',7'-dichlorofluoresceinAPEX1 protein, humanDNA-(Apurinic or Apyrimidinic Site) LyaseFluoresceinsFluorescent DyesGlucoseGlutamineGlutathioneMembrane ProteinsMitochondrial ProteinsReactive Oxygen SpeciesSulfhydryl CompoundsThioredoxinsTXN protein, human

Identifiers

PMID17210449
PMCPMC1800831
OpenAlexW2100702622

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.