Evidence map›Paper›PMID 19465481›Full record

ArticleThe Journal of biological chemistry2009

Interleukin-33 is biologically active independently of caspase-1 cleavage.

Dominique Talabot-Ayer, Céline Lamacchia, Cem Gabay, Gaby Palmer

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 122 papers.

0numbers the graph read from it
0cells of the map it votes in
122citing papers in PubMed
11.5field-weighted citation impact, top 1% 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

122 citing papers in PubMed, 245 citations in OpenAlex.

  1. Targeting IL-33 in Precision Neuroimmunology: Cellular Mechanisms and Therapeutic Strategies for CNS Disorders.Journal of neuroimmune pharmacology : the official journal of the Society on NeuroImmune Pharmacology · 2026
    Review
  2. Review
  3. Review
  4. Article
  5. Article
  6. Review
  7. IL-33 Expression Is Lower in Current Smokers at both Transcriptomic and Protein Levels.American journal of respiratory and critical care medicine · 2023
    Article
  8. Review
  9. The Role of IL-33/ST2 in COPD and Its Future as an Antibody Therapy.International journal of molecular sciences · 2023
    Review
  10. Article
  11. Role of inflammasome in severe, steroid-resistant asthma.Current research in immunology · 2023
    Review
  12. Emerging Effects of IL-33 on COVID-19.International journal of molecular sciences · 2022
    Review
  13. Article
  14. Review
  15. Hepatic pannexin-1 mediates ST2Clinical and translational medicine · 2022
    Article
  16. Diverse Control Mechanisms of the Interleukin-1 Cytokine Family.Frontiers in cell and developmental biology · 2022
    Review
  17. Review
  18. Review
  19. The Paradigm Change of IL-33 in Vascular Biology.International journal of molecular sciences · 2021
    Review
  20. Article

62 more citing papers are in PubMed but not listed here.

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

4 authors at 2 institutions in 1 country.

Dominique Talabot-AyerDivision of Rheumatology, University Hospital, and Department of Pathology and Immunology, University of Geneva School of Medicine, 1211 Geneva 4, Switzerland.
Céline Lamacchia
Cem Gabay
Gaby Palmer
University Hospital of Geneva · CHUniversity of Geneva · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The new interleukin (IL)-1 family cytokine IL-33 is synthesized as a 30-kDa precursor. Like pro-IL-1beta, human pro-IL-33 was reported to be cleaved by caspase-1 to generate an 18-kDa fragment, which is sufficient to activate signaling by the IL-33 receptor T1/ST2. However, the proposed caspase-1 cleavage site is poorly conserved between species. In addition, it is not clear whether caspase-1 cleavage of pro-IL-33 occurs in vivo and whether, as for IL-1beta, this cleavage is a prerequisite for IL-33 secretion and bioactivity. In this study, we further investigated caspase-1 cleavage of mouse and human pro-IL-33 and assessed the potential bioactivity of the IL-33 precursor. We observed the generation of a 20-kDa IL-33 fragment in cell lysates, which was enhanced by incubation with caspase-1. However, in vitro assays of mouse and human pro-IL-33 indicated that IL-33 is not a direct substrate for this enzyme. Consistently, caspase-1 activation in THP-1 cells induced cleavage of pro-IL-1beta but not of pro-IL-33, and activated THP-1 cells released full-length pro-IL-33 into culture supernatants. Finally, addition of full-length pro-IL-33 induced T1/ST2-dependent IL-6 secretion in mast cells. However, we observed in situ processing of pro-IL-33 in mast cell cultures, and it remains to be determined whether full-length pro-IL-33 itself indeed represents the bioactive species. In conclusion, our data indicate that pro-IL-33 is not a direct substrate for caspase-1. In addition, our results clearly show that caspase-1 cleavage is not required for pro-IL-33 secretion and bioactivity, highlighting major differences between IL-1beta and IL-33.

Indexed as

AnimalsBlotting, WesternCaspase 1Cell LineCells, CulturedEnzyme ActivationGreen Fluorescent ProteinsHumansInterleukin-1betaInterleukin-33InterleukinsLipopolysaccharidesMiceMicroscopy, ConfocalMonocytesPeptide FragmentsCaspase 1Green Fluorescent ProteinsIL33 protein, humanIl33 protein, mouseInterleukin-1betaInterleukin-33InterleukinsLipopolysaccharidesPeptide FragmentsProtein PrecursorsTetradecanoylphorbol Acetate

Identifiers

PMID19465481
PMCPMC2740567
OpenAlexW2028832882

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.