ArticleFrontiers in microbiology2011
Asc-dependent and independent mechanisms contribute to restriction of legionella pneumophila infection in murine macrophages.
Article in Frontiers in microbiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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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.
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Who cites it
26 citing papers in PubMed, 41 citations in OpenAlex.
- Molecular Characterization, Expression, and Regulatory Signal Pathway Analysis of Inflammasome Component Apoptosis-Associated Speck-like Protein Containing a CARD Domain (ASC) in Large Yellow Croaker (International journal of molecular sciences · 2023Article
- cAbl Kinase Regulates Inflammasome Activation and Pyroptosis via ASC Phosphorylation.Journal of immunology (Baltimore, Md. : 1950) · 2021Article
- The PANoptosome: A Deadly Protein Complex Driving Pyroptosis, Apoptosis, and Necroptosis (PANoptosis).Frontiers in cellular and infection microbiology · 2020Review
- Gasdermin-D and Caspase-7 are the key Caspase-1/8 substrates downstream of the NAIP5/NLRC4 inflammasome required for restriction of Legionella pneumophila.PLoS pathogens · 2019Article
- Emerging Roles of Autophagy and Inflammasome in Ehrlichiosis.Frontiers in immunology · 2019Review
- Caspase-11 Mediates Neutrophil Chemotaxis and Extracellular Trap Formation During Acute Gouty Arthritis Through Alteration of Cofilin Phosphorylation.Frontiers in immunology · 2019Article
- Autoinflammatory mutation in NLRC4 reveals a leucine-rich repeat (LRR)-LRR oligomerization interface.The Journal of allergy and clinical immunology · 2018Article
- The inflammasomes, immune guardians at defence barriers.Immunology · 2018Review
- Inhibition of caspase-1 or gasdermin-D enable caspase-8 activation in the Naip5/NLRC4/ASC inflammasome.PLoS pathogens · 2017Article
- Enzymatically Inactive Procaspase 1 stabilizes the ASC Pyroptosome and Supports Pyroptosome Spreading during Cell Division.The Journal of biological chemistry · 2016Article
- Activation of phagocytic activity in astrocytes by reduced expression of the inflammasome component ASC and its implication in a mouse model of Alzheimer disease.Journal of neuroinflammation · 2016Article
- Shiga Toxins Activate the NLRP3 Inflammasome Pathway To Promote Both Production of the Proinflammatory Cytokine Interleukin-1β and Apoptotic Cell Death.Infection and immunity · 2016Article
- Programmed cell death and its role in inflammation.Military Medical Research · 2015Article
- Receptor interacting protein-2 plays a critical role in human lung epithelial cells survival in response to Fas-induced cell-death.PloS one · 2014Article
- Inflammasome-mediated cell death in response to bacterial pathogens that access the host cell cytosol: lessons from legionella pneumophila.Frontiers in cellular and infection microbiology · 2013Review
- AIM2 and NLRP3 inflammasomes activate both apoptotic and pyroptotic death pathways via ASC.Cell death and differentiation · 2013Article
- Inflammasome-mediated pyroptotic and apoptotic cell death, and defense against infection.Current opinion in microbiology · 2013Review
- Review
- Biofilm-derived Legionella pneumophila evades the innate immune response in macrophages.Frontiers in cellular and infection microbiology · 2013Article
- Tyrosine phosphatase inhibition induces an ASC-dependent pyroptosis.Biochemical and biophysical research communications · 2012Article
Corrections and comments
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Authors and funding
19 authors at 6 institutions in 2 countries.
Funding
Abstract
The apoptosis-associated speck-like protein containing a caspase recruitment domain (Asc) is an adaptor molecule that mediates inflammatory and apoptotic signals. Legionella pneumophila is an intracellular bacterium and the causative agent of Legionnaire's pneumonia. L. pneumophila is able to cause pneumonia in immuno-compromised humans but not in most inbred mice. Murine macrophages that lack the ability to activate caspase-1, such as caspase(-1-/-) and Nlrc4(-/-) allow L. pneumophila infection. This permissiveness is attributed mainly to the lack of active caspase-1 and the absence of its down stream substrates such as caspase-7. However, the role of Asc in control of L. pneumophila infection in mice is unclear. Here we show that caspase-1 is moderately activated in Asc(-/-) macrophages and that this limited activation is required and sufficient to restrict L. pneumophila growth. Moreover, Asc-independent activation of caspase-1 requires bacterial flagellin and is mainly detected in cellular extracts but not in culture supernatants. We also demonstrate that the depletion of Asc from permissive macrophages enhances bacterial growth by promoting L. pneumophila-mediated activation of the NF-κB pathway and decreasing caspase-3 activation. Taken together, our data demonstrate that L. pneumophila infection in murine macrophages is controlled by several mechanisms: Asc-independent activation of caspase-1 and Asc-dependent regulation of NF-κB and caspase-3 activation.
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Registered trials
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