Evidence map›Paper›PMID 26599267›Full record

ArticlePloS one2015

Monocyte Caspase-1 Is Released in a Stable, Active High Molecular Weight Complex Distinct from the Unstable Cell Lysate-Activated Caspase-1.

Obada R Shamaa, Srabani Mitra, Mikhail A Gavrilin, Mark D Wewers

Abstract read
In one paragraph

Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
–field-weighted citation impact
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

38 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Review
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. NLRP3 Ubiquitination-A New Approach to Target NLRP3 Inflammasome Activation.International journal of molecular sciences · 2021
    Review
  17. Article
  18. Article
  19. Article
  20. The intricate biophysical puzzle of caspase-1 activation.Archives of biochemistry and biophysics · 2021
    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

4 authors.

Obada R ShamaaDavis Heart and Lung Research Institute, Division of Pulmonary, Allergy, Critical Care and Sleep Medicine, Department of Internal Medicine, Wexner Medical Center, The Ohio State University, 473 W. 12th Avenue, 201 DHLRI, Columbus, OH, United States of America.
Srabani MitraDavis Heart and Lung Research Institute, Division of Pulmonary, Allergy, Critical Care and Sleep Medicine, Department of Internal Medicine, Wexner Medical Center, The Ohio State University, 473 W. 12th Avenue, 201 DHLRI, Columbus, OH, United States of America.
Mikhail A GavrilinDavis Heart and Lung Research Institute, Division of Pulmonary, Allergy, Critical Care and Sleep Medicine, Department of Internal Medicine, Wexner Medical Center, The Ohio State University, 473 W. 12th Avenue, 201 DHLRI, Columbus, OH, United States of America.
Mark D WewersDavis Heart and Lung Research Institute, Division of Pulmonary, Allergy, Critical Care and Sleep Medicine, Department of Internal Medicine, Wexner Medical Center, The Ohio State University, 473 W. 12th Avenue, 201 DHLRI, Columbus, OH, United States of America.

Funding

Macrophage Inflammasome RegulationR01HL076278 · NHLBI · OHIO STATE UNIVERSITY · PI WEWERS, MARK DAMIAN · 2005 to 2019
$4.5M
Regulation of lung host defense by inflammasome modifiersR21HL102724 · NHLBI · OHIO STATE UNIVERSITY · PI WEWERS, MARK DAMIAN · 2011 to 2012
$419k
NHLBI NIH HHS HL076278NHLBI NIH HHS HL102724NHLBI NIH HHS R01 HL076278NHLBI NIH HHS R21 HL102724
6 · The paper itself

Abstract

Mononuclear phagocytes utilize caspase-1 activation as a means to respond to danger signals. Although caspase-1 was discovered using highly concentrated cell extracts that spontaneously activate caspase-1, it is now clear that in live cell models caspase-1 activation occurs in the process of its cellular release and is not an intracellular event. Therefore, we compared the characteristics of caspase-1 activation in the cell lysate model to that of caspase-1 that is released in response to exogenous inflammasome activation. Whereas both models generated active caspase-1, the cell-lysate induced caspase-1 required highly concentrated cell lysates and had a short half-life (~15 min) whereas, the activation induced released caspase-1 required 2-3 log fold fewer cells and was stable for greater than 12 h. Both forms were able to cleave proIL-1beta but unexpectedly, the released activity was unable to be immunodepleted by caspase-1 antibodies. Size exclusion chromatography identified two antigenic forms of p20 caspase-1 in the activation induced released caspase-1: one at the predicted size of tetrameric, p20/p10 caspase-1 and the other at >200 kDa. However, only the high molecular weight form had stable functional activity. These results suggest that released caspase-1 exists in a unique complex that is functionally stable and protected from immunodepletion whereas cell-extract generated active caspase-1 is rapidly inhibited in the cytosolic milieu.

Indexed as

Enzyme StabilityApoptosisCaspase 1Cell ExtractsCell-Free SystemCell LineEnzyme ActivationEnzyme-Linked Immunosorbent AssayHumansInflammasomesIntracellular MembranesMonocytesProtease InhibitorsCaspase 1Cell ExtractsInflammasomesProtease Inhibitors

Identifiers

PMID26599267
PMCPMC4657934

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.