Evidence map›Paper›PMID 25445147›Full record

ArticleScientific reports2014

Activation of NLRP3 inflammasome by crystalline structures via cell surface contact.

Aswin Hari, Yifei Zhang, Zhongyuan Tu, Pascal Detampel, Melanie Stenner, Anutosh Ganguly, Yan Shi

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
63citing papers in PubMed, 1 pooled it
3.8field-weighted citation impact, top 6% 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

63 citing papers in PubMed, 1 synthesis or guideline pooled it, 104 citations in OpenAlex.

  1. Pooled it
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  13. The role of inflammation in silicosis.Frontiers in pharmacology · 2024
    Review
  14. Review
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  19. Review
  20. Article

3 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

7 authors at 3 institutions in 3 countries.

Aswin HariDepartment of Microbiology, Immunology &Infectious Diseases and Snyder Institute, University of Calgary, Calgary, Alberta, Canada.
Yifei ZhangDepartment of Basic Medical Sciences, School of Medicine; Tsinghua-Peking Center for Life Sciences, Tsinghua University, Beijing, China.
Zhongyuan TuDepartment of Microbiology, Immunology &Infectious Diseases and Snyder Institute, University of Calgary, Calgary, Alberta, Canada.
Pascal DetampelDepartment of Microbiology, Immunology &Infectious Diseases and Snyder Institute, University of Calgary, Calgary, Alberta, Canada.
Melanie StennerDepartment of Microbiology, Immunology &Infectious Diseases and Snyder Institute, University of Calgary, Calgary, Alberta, Canada.
Anutosh GangulyDepartment of Microbiology, Immunology &Infectious Diseases and Snyder Institute, University of Calgary, Calgary, Alberta, Canada.
Yan Shi1] Department of Microbiology, Immunology &Infectious Diseases and Snyder Institute, University of Calgary, Calgary, Alberta, Canada [2] Department of Basic Medical Sciences, School of Medicine; Tsinghua-Peking Center for Life Sciences, Tsinghua University, Beijing, China.
University of Calgary · CACenter for Life Sciences · CNKing Center · US

Funding

Adjuvants' mechanismsR01AI098995 · NIAID · UNIVERSITY OF CALGARY · PI SHI, YAN · 2012 to 2016
$1.0M
Canadian Institutes of Health Research MOP-119295NIAID NIH HHS R01 AI098995NIAID NIH HHS R01AI098995
6 · The paper itself

Abstract

Crystalline structures activate the NLRP3 inflammasome, leading to the production of IL-1β, however, the molecular interactions responsible for NLRP3 activation are not fully understood. Cathepsin B release from the ruptured phagolysosome and potassium ion efflux have been suggested to be critical for this activation. Here, we report that Cathepsin B redistribution was not a crucial event in crystal-induced IL-1β production. Silica and monosodium urate crystal-treated macrophages with undisturbed lysosomes demonstrated strong co-localization of ASC and Caspase-1, indicative of NLRP3 inflammasome activation. Importantly, we provided evidence to suggest that macrophage cell membrane binding to immobilized crystals was sufficient to induce IL-1β release, and this activation of the NLRP3 inflammasome was inhibited by blocking potassium efflux. Therefore, this work reveals additional complexity in crystalline structure-mediated NLRP3 inflammasome regulations.

Indexed as

AnimalsCarrier ProteinsCaspase 1Cathepsin BCell MembraneCells, CulturedInflammasomesInterleukin-1betaLysosomesMacrophagesMiceMice, Inbred C57BLNLR Family, Pyrin Domain-Containing 3 ProteinCarrier ProteinsCaspase 1Cathepsin BInflammasomesInterleukin-1betaNLR Family, Pyrin Domain-Containing 3 ProteinNlrp3 protein, mouse

Identifiers

PMID25445147
PMCPMC4250918
OpenAlexW2071591126

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.