Evidence map›Paper›PMID 26559977›Full record

ArticleThe Journal of biological chemistry2015

Interleukin-1β Processing Is Dependent on a Calcium-mediated Interaction with Calmodulin.

Joseph S Ainscough, G Frank Gerberick, Ian Kimber, Rebecca J Dearman

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
0.5field-weighted citation impact, top 33% 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

12 citing papers in PubMed, 18 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. The CaScience signaling · 2023
    Article
  7. Alterations in the CaExploration of targeted anti-tumor therapy · 2021
    Article
  8. The effect of Sirt1 deficiency on CaJournal of cellular and molecular medicine · 2020
    Article
  9. Article
  10. Article
  11. Inflammasome inhibition blocks cardiac glycoside cell toxicity.The Journal of biological chemistry · 2019
    Article
  12. 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

4 authors at 2 institutions in 2 countries.

Joseph S AinscoughFrom the Faculty of Life Sciences, University of Manchester, Manchester M13 9PT, United Kingdom and joseph.ainscough@postgrad.manchester.ac.uk.
G Frank Gerberickthe Procter & Gamble Co., Cincinnati, Ohio 45253.
Ian KimberFrom the Faculty of Life Sciences, University of Manchester, Manchester M13 9PT, United Kingdom and.
Rebecca J DearmanFrom the Faculty of Life Sciences, University of Manchester, Manchester M13 9PT, United Kingdom and.
University of Manchester · GBProcter & Gamble (United States) · US

Funding

Medical Research Council
6 · The paper itself

Abstract

The secretion of IL-1β is a central event in the initiation of inflammation. Unlike most other cytokines, the secretion of IL-1β requires two signals: one signal to induce the intracellular up-regulation of pro-IL-1β and a second signal to drive secretion of the bioactive molecule. The release of pro-IL-1β is a complex process involving proteolytic cleavage by caspase-1. However, the exact mechanism of secretion is poorly understood. Here we sought to identify novel proteins involved in IL-1β secretion and intracellular processing to gain further insights into the mechanism of IL-1 release. A human proteome microarray containing 19,951 unique proteins was used to identify proteins that bind human recombinant pro-IL-1β. Probes with a signal-to-noise ratio of >3 were defined as biologically relevant. In these analyses, calmodulin was identified as a particularly strong hit, with a signal-to-noise ratio of ∼ 11. Using an ELISA-based protein-binding assay, the interaction of recombinant calmodulin with pro-IL-1β, but not mature IL-1β, was confirmed and shown to be calcium-dependent. Finally, using small molecule inhibitors, it was demonstrated that both calcium and calmodulin were required for nigericin-induced IL-1β secretion in THP-1 cells and primary human monocytes. Together, these data suggest that, following calcium influx into the cell, pro-IL-1β interacts with calmodulin and that this interaction is important for IL-1β processing and release.

Indexed as

ProteolysisCalciumCalcium SignalingCalmodulinCell Line, TumorFemaleHumansInterleukin-1betaMaleMonocytesProtein Array AnalysisProtein PrecursorsProteomicsCalciumCalmodulinIL1B protein, humanInterleukin-1betaProtein Precursorscalciumcalmodulin (CaM)caspase 1 (CASP1)IL-1IL-1βinflammasome

Identifiers

PMID26559977
PMCPMC4692238
OpenAlexW2210910575

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.