Evidence map›Paper›PMID 15102781›Full record

ArticleInfection and immunity2004

Nitric oxide-mediated regulation of gamma interferon-induced bacteriostasis: inhibition and degradation of human indoleamine 2,3-dioxygenase.

Christian Hucke, Colin R MacKenzie, Koku D Z Adjogble, Osamu Takikawa, Walter Däubener

Open access · greenAbstract read
In one paragraph

Article in Infection and immunity, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
3.6field-weighted citation impact, top 7% 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

47 citing papers in PubMed, 109 citations in OpenAlex.

  1. Article
  2. Review
  3. Engineering an indoleamine 2,3-dioxygenase immunotherapyMolecular systems design & engineering · 2025
    Article
  4. Review
  5. Article
  6. Role of Kynurenine and Its Derivatives in the Neuroimmune System.International journal of molecular sciences · 2024
    Review
  7. Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Review
  13. Article
  14. HJournal of experimental & clinical cancer research : CR · 2019
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  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 2 institutions in 2 countries.

Christian HuckeInstitute for Medical Microbiology, Heinrich Heine University, Düsseldorf, Germany.
Colin R MacKenzie
Koku D Z Adjogble
Osamu Takikawa
Walter Däubener
Heinrich Heine University Düsseldorf · DEHokkaido University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Tryptophan depletion resulting from indoleamine 2,3-dioxygenase (IDO) activity within the kynurenine pathway is one of the most prominent gamma interferon (IFN-gamma)-inducible antimicrobial effector mechanisms in human cells. On the other hand, nitric oxide (NO) produced by the inducible isoform of NO synthase (iNOS) serves a more immunoregulatory role in human cells and thereby interacts with tryptophan depletion in a number of ways. We investigated the effects of NO on IDO gene transcription, protein synthesis, and enzyme activity as well as on IDO-mediated bacteriostasis in the human epithelial cell line RT4. IFN-gamma-stimulated RT4 cells were able to inhibit the growth of Staphylococcus aureus in an IDO-mediated fashion, and this bacteriostatic effect was abolished by endogenously produced NO. These findings were supported by experiments which showed that IDO activity in extracts of IFN-gamma-stimulated cells is inhibited by the chemical NO donors diethylenetriamine diazeniumdiolate, S-nitroso-L-cysteine, and S-nitroso-N-acetyl-D,L-penicillamine. Furthermore, we found that both endogenous and exogenous NO strongly reduced the level of IDO protein content in RT4 cells. This effect was not due to a decrease in IDO gene transcription or mRNA stability. By using inhibitors of proteasomal proteolytic activity, we showed that NO production led to an accelerated degradation of IDO protein in the proteasome. This is the first report, to our knowledge, that demonstrates that the IDO is degraded by the proteasome and that NO has an effect on IDO protein stability.

Indexed as

Anti-Bacterial AgentsCell LineCysteine EndopeptidasesEnzyme StabilityHumansIndoleamine-Pyrrole 2,3,-DioxygenaseInterferon-gammaIn Vitro TechniquesMultienzyme ComplexesNitric OxideNitric Oxide DonorsProteasome Endopeptidase ComplexRNA, MessengerRNA StabilityStaphylococcus aureusTryptophan OxygenaseAnti-Bacterial AgentsCysteine EndopeptidasesIndoleamine-Pyrrole 2,3,-DioxygenaseInterferon-gammaMultienzyme ComplexesNitric OxideNitric Oxide DonorsProteasome Endopeptidase ComplexRNA, MessengerTryptophan Oxygenase

Identifiers

PMID15102781
PMCPMC387869
OpenAlexW2138416076

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.