complex(GO:"inflammasome complex")
Furthermore, autophagy can regulate both apoptosis and inflammasome assembly, and, depending on the conditions, can be either pro- or anti-apoptotic104 PubMed:23702978
For inflammasome activation and IL-1β release, autophagy is a negative regulator: PubMed:23702978
NLRP1 has been shown to bind directly to its ligand muramyl dipeptide in vitro and this was demonstrated to be sufficient to activate the assembly of an inflammasome. PubMed:23702978
However, a requirement for the interaction of NLRP1 with nucleotide-binding oligomerization domain-containing protein 2 (NOD2), which is another receptor for muramyl dipeptide, has been described. PubMed:23702978
Activators include bacteria, virus, fungus, protoza, microbial proteins, crystalline urea, RNA, Alum, ATP, potassium efflux, fatty acids, Aβ, and most recently, degraded mitochondrial DNA (Liu et al., 2013a; Mathew et al., 2012; Schmidt and Lenz, 2012) PubMed:24561250
Activators include bacteria, virus, fungus, protoza, microbial proteins, crystalline urea, RNA, Alum, ATP, potassium efflux, fatty acids, Aβ, and most recently, degraded mitochondrial DNA (Liu et al., 2013a; Mathew et al., 2012; Schmidt and Lenz, 2012) PubMed:24561250
Activators include bacteria, virus, fungus, protoza, microbial proteins, crystalline urea, RNA, Alum, ATP, potassium efflux, fatty acids, Aβ, and most recently, degraded mitochondrial DNA (Liu et al., 2013a; Mathew et al., 2012; Schmidt and Lenz, 2012) PubMed:24561250
Activators include bacteria, virus, fungus, protoza, microbial proteins, crystalline urea, RNA, Alum, ATP, potassium efflux, fatty acids, Aβ, and most recently, degraded mitochondrial DNA (Liu et al., 2013a; Mathew et al., 2012; Schmidt and Lenz, 2012) PubMed:24561250
Activators include bacteria, virus, fungus, protoza, microbial proteins, crystalline urea, RNA, Alum, ATP, potassium efflux, fatty acids, Aβ, and most recently, degraded mitochondrial DNA (Liu et al., 2013a; Mathew et al., 2012; Schmidt and Lenz, 2012) PubMed:24561250
In response to danger signals, inflammasomes assemble by self-oligomerizing the NLRs through interactions with the NACHT domain (van de Veerdonk et al., 2011) PubMed:24561250
Spinal cord injury elevates extracellular ATP levels during neuroinflammation, which may act on purinergic receptors to trigger the activation of inflammasome (de Rivero Vaccari et al., 2012; Minkiewicz et al., 2013) PubMed:24561250
Activators include bacteria, virus, fungus, protoza, microbial proteins, crystalline urea, RNA, Alum, ATP, potassium efflux, fatty acids, Aβ, and most recently, degraded mitochondrial DNA (Liu et al., 2013a; Mathew et al., 2012; Schmidt and Lenz, 2012) PubMed:24561250
The activators of the inflammasomes can be divided into two categories; pathogen associated molecular patterns (PAMPs) activate a host-defense reaction, and damage associated molecular patterns (DAMPs) activate a self-defense mechanism in response to danger signals (Salminen et al., 2008) PubMed:24561250
In response to danger signals, inflammasomes assemble by self-oligomerizing the NLRs through interactions with the NACHT domain (van de Veerdonk et al., 2011) PubMed:24561250
The activators of the inflammasomes can be divided into two categories; pathogen associated molecular patterns (PAMPs) activate a host-defense reaction, and damage associated molecular patterns (DAMPs) activate a self-defense mechanism in response to danger signals (Salminen et al., 2008) PubMed:24561250
Activators include bacteria, virus, fungus, protoza, microbial proteins, crystalline urea, RNA, Alum, ATP, potassium efflux, fatty acids, Aβ, and most recently, degraded mitochondrial DNA (Liu et al., 2013a; Mathew et al., 2012; Schmidt and Lenz, 2012) PubMed:24561250
Activators include bacteria, virus, fungus, protoza, microbial proteins, crystalline urea, RNA, Alum, ATP, potassium efflux, fatty acids, Aβ, and most recently, degraded mitochondrial DNA (Liu et al., 2013a; Mathew et al., 2012; Schmidt and Lenz, 2012) PubMed:24561250
Activators include bacteria, virus, fungus, protoza, microbial proteins, crystalline urea, RNA, Alum, ATP, potassium efflux, fatty acids, Aβ, and most recently, degraded mitochondrial DNA (Liu et al., 2013a; Mathew et al., 2012; Schmidt and Lenz, 2012) PubMed:24561250
Activators include bacteria, virus, fungus, protoza, microbial proteins, crystalline urea, RNA, Alum, ATP, potassium efflux, fatty acids, Aβ, and most recently, degraded mitochondrial DNA (Liu et al., 2013a; Mathew et al., 2012; Schmidt and Lenz, 2012) PubMed:24561250
In response to danger signals, inflammasomes assemble by self-oligomerizing the NLRs through interactions with the NACHT domain (van de Veerdonk et al., 2011) PubMed:24561250
Inflammasomes involve in the maturation of IL-1β and IL-18 are expressed in neurons (de Rivero Vaccari et al., 2008; Yang-Wei Fann et al., 2013; Zou and Crews, 2012) PubMed:24561250
Inflammasomes involve in the maturation of IL-1β and IL-18 are expressed in neurons (de Rivero Vaccari et al., 2008; Yang-Wei Fann et al., 2013; Zou and Crews, 2012) PubMed:24561250
P2X4 knock-out mice has been shown to decrease the level of IL-1β and to have impair inflammasome signaling (de Rivero Vaccari et al., 2012) PubMed:24561250
Trauma, a risk factor for AD, increases inflammasome expression in rat neurons (de Rivero Vaccari et al., 2009; de Rivero Vaccari et al., 2008) PubMed:24561250
Furthermore, postmortem brain tissues from stroke patients show increase protein levels of inflammasomes in primary cortical neurons (Yang- Wei Fann et al., 2013) PubMed:24561250
They appear to be involved in several pathological processes activated by microbes including Alzheimer’s disease (AD). PubMed:27314526
IL-1β and IL-18 are synthesized as inactive precursors, proIL-1β and proIL-18, respectively, and require inflammasomes for their maturation PubMed:24561250
Inflammasomes are key signalling platforms that detect pathogenic microorganisms and sterile stressors, and that activate the highly pro-inflammatory cytokines interleukin-1β (IL-1β) and IL-18. PubMed:23702978
Inflammasomes are key signalling platforms that detect pathogenic microorganisms and sterile stressors, and that activate the highly pro-inflammatory cytokines interleukin-1β (IL-1β) and IL-18. PubMed:23702978
Once the protein complexes have formed, the inflammasomes activate caspase 1, which proteolytically activates the pro-inflammatory cytokines interleukin-1β (IL-1β)3 and IL-18. PubMed:23702978
Indeed, inflammasomes (which induce pyroptosis through caspase 1 or caspase 11 activation) and apoptosomes (which activate caspase 9 in response to cytochrome c release from mitochondria) are two mechanisms by which compromised cells are eliminated. PubMed:23702978
In addition, inflammasome activation causes a rapid, proinflammatory form of cell death called pyroptosis4. PubMed:23702978
Indeed, inflammasomes (which induce pyroptosis through caspase 1 or caspase 11 activation) and apoptosomes (which activate caspase 9 in response to cytochrome c release from mitochondria) are two mechanisms by which compromised cells are eliminated. PubMed:23702978
Indeed, inflammasomes (which induce pyroptosis through caspase 1 or caspase 11 activation) and apoptosomes (which activate caspase 9 in response to cytochrome c release from mitochondria) are two mechanisms by which compromised cells are eliminated. PubMed:23702978
Inflammasomes involve in the maturation of IL-1β and IL-18 are expressed in neurons (de Rivero Vaccari et al., 2008; Yang-Wei Fann et al., 2013; Zou and Crews, 2012) PubMed:24561250
IL-1β and IL-18 are synthesized as inactive precursors, proIL-1β and proIL-18, respectively, and require inflammasomes for their maturation PubMed:24561250
However the maturation of IL-18 and IL-1β could be regulated by the same type of inflammasome PubMed:24561250
Inflammasomes involve in the maturation of IL-1β and IL-18 are expressed in neurons (de Rivero Vaccari et al., 2008; Yang-Wei Fann et al., 2013; Zou and Crews, 2012) PubMed:24561250
Like IL-1β, in most cases, the mature secretable form of IL-18 is generated by caspase-1 through the activation of inflammasome PubMed:24561250
However the maturation of IL-18 and IL-1β could be regulated by the same type of inflammasome PubMed:24561250
Like IL-1β, in most cases, the mature secretable form of IL-18 is generated by caspase-1 through the activation of inflammasome PubMed:24561250
Inflammasomes are responsible for the maturation of pro-inflammatory cytokines such as interleukin (IL)-1beta, IL-18, and IL-33 and activation of inflammatory cell death, pyroptosis. PubMed:27314526
Inflammasomes are responsible for the maturation of pro-inflammatory cytokines such as interleukin (IL)-1beta, IL-18, and IL-33 and activation of inflammatory cell death, pyroptosis. PubMed:27314526
Inflammasomes are responsible for the maturation of pro-inflammatory cytokines such as interleukin (IL)-1beta, IL-18, and IL-33 and activation of inflammatory cell death, pyroptosis. PubMed:27314526
Inflammasomes are responsible for the maturation of pro-inflammatory cytokines such as interleukin (IL)-1beta, IL-18, and IL-33 and activation of inflammatory cell death, pyroptosis. PubMed:27314526
They appear to be involved in several pathological processes activated by microbes including Alzheimer’s disease (AD). PubMed:27314526
Post activation of the inflammasome, caspase 1 enzyme initiates the maturation of pro-inflammatory cytokines particularly interleukin (IL)-1beta, IL-18, and IL-33 [4] (Fig. 1),and inflammation mediated cell death occurs via the nucleotide-binding domain and leucine-rich repeat(NLR) family of proteins [5]. PubMed:27314526
Both IL-1 beta and IL-18 are generated in their mature secreted form by caspase-1 through activa- tion of the inflammasome. PubMed:27314526
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If you find BEL Commons useful in your work, please consider citing: Hoyt, C. T., Domingo-Fernández, D., & Hofmann-Apitius, M. (2018). BEL Commons: an environment for exploration and analysis of networks encoded in Biological Expression Language. Database, 2018(3), 1–11.