Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Multiple Cathepsins Promote Pro-IL-1β Synthesis and NLRP3-Mediated IL-1β Activation.

Journal of immunology (Baltimore, Md. : 1950) - 15 Aug 2015

Orlowski Gregory M, Colbert Jeff D, Sharma Shruti, Bogyo Matthew, Robertson Stephanie A, Rock Kenneth L

Abstract excerpt

Sterile particles induce robust inflammatory responses that underlie the pathogenesis of diseases like silicosis, gout, and atherosclerosis. A key cytokine mediating this response is IL-1β. The generation of bioactive IL-1β by sterile particles is mediated by the NOD-like receptor containing a pyrin domain 3 (NLRP3) inflammasome, although exactly how this occurs is incompletely resolved. Prior studies have found...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Carrier Proteins
Share to Cathepsins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Enzyme Inhibitors

Share to Inflammasomes

Share to Interleukin-1beta

Share to Macrophages

Share to Mice, Knockout

Share to NLR Family, Pyrin Domain-Containing 3 Protein

Source

Open in PubMed Open full text

Identifiers

PMID: 26195813
DOI: 10.4049/jimmunol.1500509
PMCID: PMC4530060

Genes

NLRP3

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Multiple Cathepsins Promote Pro-IL-1β Synthesis and NLRP3-Mediated IL-1β Activation.PMID 26195813Read ↗

A broad cathepsin inhibitor blocks crystal-stimulated inflammasome-dependent and -independent inflammation, and gout arthritisSemantic proximity Read ↗

Non-redundant roles of cathepsins in promoting necrosis of human macrophagesSemantic proximity Read ↗

Release of acidic store calcium is required for effective priming of the NLRP3 inflammasomeSemantic proximity Read ↗

Cathepsin B-Mediated Activation of Trypsinogen in Endocytosing Macrophages Increases Severity of Pancreatitis in Mice.Semantic proximity Read ↗

<i>In vivo</i> cellular localisation and nanoscale organisation of NLRP3 inflammasomesSemantic proximity Read ↗

Lung macrophages utilize unique cathepsin K-dependent phagosomal machinery to degrade intracellular collagenSemantic proximity Read ↗

Autophagy inhibitors block pathogenic NET release in immune-mediated inflammatory disease without impairing host defenceSemantic proximity Read ↗

Sterile- or pathogen-induced endolysosomal damage activate the NLRP6 inflammasome in human intestinal epithelial cellsSemantic proximity Read ↗

Listeria monocytogenes and Shigella flexneri Activate the NLRP1B Inflammasome.Semantic proximity Read ↗

Tryptophol acetate and tyrosol acetate, small molecule metabolites identified in a probiotic mixture, inhibit hyperinflammationSemantic proximity Read ↗

Inhibitory Effects of Human β-Defensin 3 on <em>Porphyromonas gingivalis </em>Lipopolysaccharide-Induced Il-1β Production by Bv-2 Microglia through Suppression of Cathepsins B and LSemantic proximity Read ↗

Tmem178 negatively regulates IL-1β production through inhibition of the NLRP3 inflammasomeSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.