Sensing pathogens and danger signals by the inflammasome

Pedra, Joao HF; Cassel, Suzanne L; Sutterwala, Fayyaz S

doi:10.1016/j.coi.2009.01.006

Cited by 233Inflammasome and immune disordersImmune Response and Inflammationinterferon and immune responses

Sensing pathogens and danger signals by the inflammasome

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Pedra, Joao HF, Cassel, Suzanne L, Sutterwala, Fayyaz S·2009·Current Opinion in Immunology

DOI 10.1016/j.coi.2009.01.006PMC PMC2701640

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Abstract

The NLR (nucleotide-binding domain leucine-rich repeat containing) family of intracellular sensors is a crucial component of the innate immune system. A number of NLR family members can form multiprotein complexes, called inflammasomes, and are capable of activating the cysteine protease caspase-1 in response to a wide range of stimuli including both microbial and self-molecules. Caspase-1 activation leads to processing and secretion of the proinflammatory cytokines interleukin-1beta (IL-1beta) and IL-18, which play crucial roles in host defense to infectious insults. Dysregulation of the inflammasome has also been linked to a number of autoinflammatory and autoimmune disorders. Recent advances in the inflammasome field will be discussed in this review.

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Proinflammatory danger signals induce activity of the NLRP-3 inflammasome.
“Proinflammatory danger signals induce activity of a multiprotein complex called the Nod-like receptor protein (NLRP)-3 inflammasome (16–18).”
From Sustained Inflammasome Activity in Macrophages Impairs Wound Healing in Type 2 Diabetic Humans and Mice (2014) · cites this paper as [18]
During inflammasome activation, the proform of caspase-1 is recruited to the NLRP-3 complex and cleaved to produce active caspase-1, which then cleaves and activates IL-1β and IL-18.
“During inflammasome activation, the proform of caspase-1 is recruited to the NLRP-3 complex and cleaved to produce active caspase-1, which then cleaves and activates the potent proinflammatory cytokines IL-1β and IL-18.”
From Sustained Inflammasome Activity in Macrophages Impairs Wound Healing in Type 2 Diabetic Humans and Mice (2014) · cites this paper as [18]

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Authors: Pedra, J. H., Cassel, S. L., & Sutterwala, F. S.
Affiliations: University of California, Riverside (US)
University of Iowa (US)
Corresponding author: Pedra, Joao HF
Sutterwala, Fayyaz S
ORCID: Pedra, Joao HF
Sutterwala, Fayyaz S
Venue: Current Opinion in Immunology
Publisher: Elsevier BV
Published: 2009-02
Volume: 21
Issue: 1
Pages: 10-16
ISSN: 0952-7915 (ISSN-L)
DOI: 10.1016/j.coi.2009.01.006
PMC: PMC2701640
OpenAlex: W2171309698
Cited by: 233
References: 65
Citations by year: 2026: 1 · 2025: 5 · 2024: 4 · 2023: 9 · 2022: 9 · 2021: 7 · 2020: 13 · 2019: 12 · 2018: 13 · 2017: 8 · 2016: 19 · 2015: 11 · 2014: 20 · 2013: 22 · 2012: 29
FWCI: 2.04
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
Locations: Current Opinion in Immunology (publishedVersion)
PubMed (publishedVersion)
PubMed Central (acceptedVersion)
Funders: National Institutes of Health
Centers for Disease Control and Prevention (K01CK000101)
National Institute of Allergy and Infectious Diseases (K08AI067736, K08AI065517)
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 › Immunology and Microbiology › Immunology › interferon and immune responses
Keywords: inflammasome, caspase-1 activation, IL-1β, IL-18, innate immunity, pathogen recognition, damage-associated molecular patterns, autoinflammatory disease, autoimmune disease, host defense
MeSH terms: NLR Proteins, Animals, Autoimmune Diseases, Bacterial Infections, Calcium-Binding Proteins, Gene Expression Regulation, Humans, Immunity, Innate, Polymorphism, Genetic, Signal Transduction, Genetic Predisposition to Disease, Caspase 1, Intercellular Signaling Peptides and Proteins, Adaptor Proteins, Signal Transducing, Apoptosis Regulatory Proteins, CARD Signaling Adaptor Proteins, Interleukin-1beta, Host-Pathogen Interactions

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