The pyroptosome: a supramolecular assembly of ASC dimers mediating inflammatory cell death via caspase-1 activation
Open accessAbstract
Pyroptosis is a caspase-1-dependent inflammatory form of cell death. The adapter protein ASC binds directly to caspase-1 and is critical for caspase-1 activation in response to a broad range of stimuli. To elucidate the mechanism of activation of caspase-1 by ASC and its exact role in macrophage pyroptosis, we performed time-lapse confocal bioimaging analysis on human THP-1 macrophages stably expressing an ASC-GFP fusion protein. We show that stimulation of these cells with several proinflammatory stimuli trigger the formation of a large supramolecular assembly of ASC, termed here pyroptosome. Only one distinct pyroptosome in each stimulated cell is formed, which rapidly recruits and activates caspase-1 resulting in pyroptosis and the release of the intracellular proinflammatory cytokines. The pyroptosome is largely composed of oligomerized ASC dimers. Dimerization of ASC is driven by subphysiological concentrations of potassium as in vitro incubation of purified recombinant ASC in the presence of subphysiological concentrations of potassium induces the assembly of a functional pyroptosome. Furthermore, stimulation of potassium efflux in THP-1 cells with potassium-depleting agents induces formation of the pyroptosome, while increasing potassium concentrations in the culture medium or pharmacological inhibition of this efflux inhibits its assembly. Our results establish that macrophage pyroptosis is mediated by a unique pyroptosome, distinct from the inflammasome.
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Inflammasome activation can lead to pyroptosis, although sublethal inflammasome activation can also occur.
“Inflammasome activation can lead to a form of cell death called pyroptosis, although sublethal inflammasome activation can also occur [64, 65].”
From Microglial function, INPP5D/SHIP1 signaling, and NLRP3 inflammasome activation: implications for Alzheimer’s disease (2023) · cites this paper as [65]
Lowering intracellular K+ through efflux is required for Nalp3 activation by every known activator, including MSU.
“In favour of the latter assumption is the recent finding that potassium (K + ) efflux, lowering intracellular K + levels, is a requirement for Nalp3 inflammasome activation triggered by all known activators including MSU (13)(14)(15).”
From Innate Immune Activation Through Nalp3 Inflammasome Sensing of Asbestos and Silica (2008) · cites this paper as [15]
NLRP3 inflammasome formation elicits self-cleavage of procaspase-1, generating active caspase-1 and converting IL-1β and IL-18 to active forms that are secreted from activated immune cells.
“Formation of this complex elicit the self-cleavage of procaspase-1, generating the active caspase 1 and inducing the conversion of proinflammatory cytokines such as interleukin 1 beta (IL-1β) and interleukin 18 (IL-18) in their active forms, that will be secreted from activated immune cells (Figure 3B) [134,135].”
From P2X7 Receptor Signaling in Stress and Depression (2019) · cites this paper as [135]
Release of PAMPs and DAMPs causes an opening in NLRP3, allowing interaction between the PYD domain in NLRP3 and ASC.
“the release of PAMPs and DAMPs, causing an opening in NLRP3, which allows the interaction between the PYD domain in NLRP3 and ASC.”
From P2X7 Receptor Signaling in Stress and Depression (2019) · cites this paper as [135]
The CARD of ASC binds to the CARD of procaspase-1, forming the NLRP3 inflammasome.
“Subsequently, the caspase recruitment domain (CARD) of ASC binds to the CARD of procaspase-1, originating the NLRP3 inflammasome.”
From P2X7 Receptor Signaling in Stress and Depression (2019) · cites this paper as [135]
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Multidimensional profiling in the investigation of small-molecule-induced cell death
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- Authors
- Fernandes-Alnemri, T., Wu, J., Yu, J.-W., Datta, P., Miller, B., Jankowski, W., Rosenberg, S., Zhang, J., & Alnemri, E. S.
- Affiliations
- Thomas Jefferson University (US)
- Corresponding author
- Alnemri, E S
- Venue
- Cell Death & Differentiation
- Published
- 2007-06-29
- Volume
- 14
- Issue
- 9
- Pages
- 1590-1604
- ISSN
- 1350-9047 (ISSN-L)
- 1476-5403
- PMC
- PMC3345951
- OpenAlex
- W2067043938
- Cited by
- 1,026
- References
- 43
- Citations by year
- 2026: 33 · 2025: 46 · 2024: 61 · 2023: 77 · 2022: 77 · 2021: 69 · 2020: 60 · 2019: 61 · 2018: 55 · 2017: 64 · 2016: 62 · 2015: 59 · 2014: 60 · 2013: 57 · 2012: 40
- FWCI
- 14.95
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Cell Death and Differentiation (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- YUHSpace (Yonsei University Medical Library) (submittedVersion, cc-by-nc-nd)
- Funders
- National Institutes of Health (CA78890)
- National Institute on Aging (AG14357, R01AG014357)
- National Cancer Institute (CA78890, P01CA078890)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Inflammasome and immune disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
- Keywords
- pyroptosis, ASC, caspase-1 activation, macrophage cell death, potassium efflux, supramolecular self-assembly, THP-1 macrophages, inflammasome
- MeSH terms
- Cytoskeletal Proteins, Enzyme Activation, Humans, Inflammation, Lipopolysaccharides, Macrophages, Potassium, Recombinant Fusion Proteins, Apoptosis, Microscopy, Confocal, Dimerization, Caspase 1, Adaptor Proteins, Signal Transducing
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