Gasdermin D unlocks metabolic pathways to enhance tissue regeneration. [PDF]
Shubhra QTH.
europepmc +3 more sources
Posttranslational and Therapeutic Control of Gasdermin-Mediated Pyroptosis and Inflammation
Pyroptosis is a proinflammatory form of cell death, mediated by membrane pore-forming proteins called gasdermins. Gasdermin pores allow the release of the pro-inflammatory cytokines IL-1β and IL-18 and cause cell swelling and cell lysis leading to ...
Fabian A. Fischer +2 more
doaj +1 more source
Bacillus cereus non-haemolytic enterotoxin activates the NLRP3 inflammasome [PDF]
Inflammasomes are important for host defence against pathogens and homeostasis with commensal microbes. Here, we show non-haemolytic enterotoxin (NHE) from the neglected human foodborne pathogen Bacillus cereus is an activator of the NLRP3 inflammasome ...
Atmosukarto, Ines I. +21 more
core +5 more sources
Summary: Viral sensing in myeloid cells involves inflammasome activation leading to gasdermin pore formation, cytokine release, and cell death. However, less is known about viral sensing in barrier epithelial cells, which are critical to the innate ...
Coralie Guy +4 more
doaj +1 more source
ASC filament formation serves as a signal amplification mechanism for inflammasomes [PDF]
A hallmark of inflammasome activation is the ASC speck, a micrometre-sized structure formed by the inflammasome adaptor protein ASC (apoptosis-associated speck-like protein containing a CARD), which consists of a pyrin domain (PYD) and a caspase ...
Broz, Petr +4 more
core +1 more source
Molecular mechanisms of gasdermin D pore-forming activity
The regulated disruption of the plasma membrane, which can promote cell death, cytokine secretion or both is central to organismal health. The protein gasdermin D (GSDMD) is a key player in this process. GSDMD forms membrane pores that can promote cytolysis and the release of interleukin-1 family cytokines into the extracellular space.
Pascal Devant, Jonathan C. Kagan
openaire +2 more sources
Pyroptosis, inflammasome, and gasdermins in tumor immunity
The gasdermins (GSDM), a family of pore-forming proteins, consist of gasdermin A (GSDMA), gasdermin B (GSDMB), gasdermin C (GSDMC), gasdermin D (GSDMD), gasdermin E (GSDME) and DFNB59 (Pejvakin (PJVK)) in humans.
Xiaohu Ouyang +5 more
doaj +1 more source
Succination inactivates gasdermin D and blocks pyroptosis
Fumarate targets pyroptosis A form of inflammatory cell death called pyroptosis depends on the caspase-mediated cleavage of gasdermin D (GSDMD), the fragments of which assemble into permeability pores that then kill the cell. The mechanisms regulating this important cellular process are not yet fully understood. Humphries
Fiachra Humphries +16 more
openaire +4 more sources
Cleavage of DFNA5 by caspase-3 during apoptosis mediates progression to secondary necrotic/pyroptotic cell death. [PDF]
Apoptosis is a genetically regulated cell suicide programme mediated by activation of the effector caspases 3, 6 and 7. If apoptotic cells are not scavenged, they progress to a lytic and inflammatory phase called secondary necrosis.
Alnemri, Diana +5 more
core +2 more sources
Caspase-1 engagement and TLR-induced c-FLIP expression suppress ASC/caspase-8-dependent apoptosis by inflammasome sensors NLRP1b and NLRC4 [PDF]
The caspase activation and recruitment domain (CARD)-based inflammasome sensors NLRP1b and NLRC4 induce caspase-1-dependent pyroptosis independent of the inflammasome adaptor ASC.
D'Hont, Jinke +14 more
core +5 more sources

