The Inflammasome

Martinon, Fabio; Burns, Kimberly; Tschopp, Jürg

doi:10.1016/s1097-2765(02)00599-3

Cited by 6,066Inflammasome and immune disordersImmune Response and InflammationCell death mechanisms and regulation

The Inflammasome

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Martinon, Fabio, Burns, Kimberly, Tschopp, Jürg·2002·Molecular Cell

DOI 10.1016/s1097-2765(02)00599-3

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Abstract

Generation of Interleukin (IL)-1beta via cleavage of its proform requires the activity of caspase-1 (and caspase-11 in mice), but the mechanism involved in the activation of the proinflammatory caspases remains elusive. Here we report the identification of a caspase-activating complex that we call the inflammasome. The inflammasome comprises caspase-1, caspase-5, Pycard/Asc, and NALP1, a Pyrin domain-containing protein sharing structural homology with NODs. Using a cell-free system, we show that proinflammatory caspase activation and proIL-1beta processing is lost upon prior immunodepletion of Pycard. Moreover, expression of a dominant-negative form of Pycard in differentiated THP-1 cells blocks proIL-1beta maturation and activation of inflammatory caspases induced by LPS in vivo. Thus, the inflammasome constitutes an important arm of the innate immunity.

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Caspase-1, activated inside the inflammasome, cleaves proIL-1β to yield mature IL-1β.
“Mature IL-1β is produced by cleavage of the inactive proIL-1β precursor by caspase-1, which is activated within a large multi-protein complex, termed the inflammasome (8).”
From Innate Immune Activation Through Nalp3 Inflammasome Sensing of Asbestos and Silica (2008) · cites this paper as [8]
The Nalp3 inflammasome contains Nalp3, Cardinal, ASC, and caspase-1, and has been linked to mature IL-1β generation after diverse stimuli.
“The Nalp3 inflammasome, composed of the Nod-like receptor (NLR) protein Nalp3 (Cryopyrin/NLRP3), Cardinal, the adaptor ASC and caspase-1, is implicated in the production of mature IL-1β in response to a variety of signals.”
From Innate Immune Activation Through Nalp3 Inflammasome Sensing of Asbestos and Silica (2008) · cites this paper as [8]
Caspase-1 belongs to the inflammatory caspases and leads to the processing and secretion of IL-1β and IL-18 into their active forms.
“Caspase-1 belongs to the inflammatory caspases and leads to the processing and secretion of the pro-inflammatory cytokines interleukin-1 beta (IL-1β) and IL-18 into their active forms (21).”
From Volcanic Ash Activates the NLRP3 Inflammasome in Murine and Human Macrophages (2018) · cites this paper as [21]
The inflammasome is a high-molecular-weight complex present in the cytosol of immune cells.
“Among the different types of PRRs, the newest described is the inflammasome, a high-molecular-weight complex, present in the cytosol of immune cells [132].”
From P2X7 Receptor Signaling in Stress and Depression (2019) · cites this paper as [132]
Caspase-1 requires cleavage from pro-caspase-1 via formation of a multimeric protein complex termed the inflammasome.
“Caspase-1 is also regulated in a similar manner and requires cleavage from pro-caspase-1.This occurs via the formation of a multimeric protein complex termed the inflammasome.”
From Repeated Social Defeat, Neuroinflammation, and Behavior: Monocytes Carry the Signal (2017) · cites this paper as Martinon et al, 2002

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“A newly identified PRR, first described in detail in 2002, is the inflammasome (Martinon et al., 2002; Gentile et al., 2015; Jorgensen and Miao, 2015; Sanders et al., 2015).”
Background
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Authors: Martinon, F., Burns, K., & Tschopp, J.
Affiliations: University of Lausanne (CH)
Corresponding author: Tschopp, Jürg
ORCID: Martinon, Fabio
Venue: Molecular Cell
Publisher: Elsevier BV
Published: 2002-08
Volume: 10
Issue: 2
Pages: 417-426
ISSN: 1097-2765 (ISSN-L)
DOI: 10.1016/s1097-2765(02)00599-3
OpenAlex: W1529674879
Cited by: 6,066
References: 49
Citations by year: 2026: 260 · 2025: 343 · 2024: 431 · 2023: 450 · 2022: 466 · 2021: 417 · 2020: 457 · 2019: 397 · 2018: 315 · 2017: 315 · 2016: 285 · 2015: 300 · 2014: 256 · 2013: 230 · 2012: 200
FWCI: 16.27
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 4003 d)
Locations: Molecular Cell (publishedVersion)
PubMed (publishedVersion)
IRIS (submittedVersion)
SERVAL (Université de Lausanne) (submittedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Inflammasome and immune disorders
Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
Keywords: inflammasome, caspase-1, caspase-5, PYCARD, ASC, NALP1, interleukin-1β processing, caspase activation, innate immunity, pyrin domain, THP-1 cells, lipopolysaccharide, dominant-negative mutant
MeSH terms: NLR Proteins, Cell Line, Cell-Free System, Cytoskeletal Proteins, Enzyme Activation, HeLa Cells, Humans, Inflammation, Interleukin-1, Lipopolysaccharides, Protein Precursors, Protein Processing, Post-Translational, Proteins, Blotting, Western, Caspases, Caspase 1, Macromolecular Substances, Adaptor Proteins, Signal Transducing, Apoptosis Regulatory Proteins, CARD Signaling Adaptor Proteins

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