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CASP9 — NLRP3
Text-mined interactions from Literome
Hoffman et al., Lancet 2004
(Acute Disease...) :
Involvement of
cryopyrin in activation of
caspase 1 and NF-kappaB signalling suggests that it might have a role in many chronic inflammatory diseases
Yu et al., Cell Death Differ 2006
(Inflammation) :
However, both
cryopyrin and two disease associated cryopyrin mutants
induced ASC oligomerization and ASC dependent
caspase-1 activation, with the disease associated mutants being more potent than the wild-type ( WT ) cryopyrin, because of increased self-oligomerization
Kanneganti et al., Nature 2006
(Inflammation) :
Cryopyrin and ASC are
essential for
caspase-1 activation and IL-1beta and IL-18 production in response to bacterial RNA and the imidazoquinoline compounds R837 and R848
Mariathasan et al., Nature 2006
(Inflammation) :
Macrophages exposed to Gram positive Staphylococcus aureus or Listeria monocytogenes, however,
required both ASC and
cryopyrin to activate
caspase-1 and secrete IL-1beta
Kanneganti et al., J Biol Chem 2006
:
Critical
role for
Cryopyrin/Nalp3 in activation of
caspase-1 in response to viral infection and double stranded RNA
Dorfleutner et al., Infect Immun 2007
(Inflammation) :
cPOP2 binds to ASC and PAN1, thereby blocking formation of
cryopyrin and PAN1 containing inflammasomes,
activation of
caspase-1 , and subsequent processing and secretion of bioactive interleukin-1beta
Kanneganti et al., Immunity 2007
(Inflammation) :
Cryopyrin is
essential for
caspase-1 activation triggered by Toll-like receptor ( TLR ) ligands in the presence of adenosine triphosphate ( ATP ) ... Here we demonstrate that
cryopyrin mediated
caspase-1 activation proceeds independently of TLR signaling, thus dissociating caspase-1 activation and IL-1beta secretion
Marina-García et al., J Immunol 2008
:
Furthermore, the work provides evidence for distinct
roles of Nod2 and
Cryopyrin in the regulation of MDP induced
caspase-1 activation and IL-1beta secretion
Franchi et al., Immunol Rev 2009
(Autoimmune Diseases...) :
In this review, we focus on the role of Nod1 and Nod2 in host defense and in particular discuss recent finding regarding the
role of Nlrc4, Nlpr1, and
Nlrp3 inflammasomes in
caspase-1 activation and subsequent release of proinflammatory cytokines such as interleukin-1 beta
Lamkanfi et al., J Biol Chem 2009
(Inflammation) :
We previously showed that bacterial molecules such as lipopolysaccharide (LPS) and peptidoglycan induce
activation of
caspase-7 through the
Cryopyrin inflammasome ... Similarly,
Cryopyrin and ASC were
required for activation of
caspase-7 in macrophages stimulated with zymosan or mannan and ATP ... These results demonstrate that the conserved fungal components zymosan and mannan
require ASC and
Cryopyrin for
caspase-1 activation and IL-1beta secretion and suggest an important role for the Cryopyrin inflammasome during fungal infections
Franchi et al., J Immunol 2009
(Inflammation) :
In addition to TNF-alpha, IL-1alpha and IL-1beta promoted
caspase-1 activation via
Nlrp3 in response to ATP
Abdul-Sater et al., J Biol Chem 2009
(Uterine Cervical Neoplasms) :
Elevated levels of reactive oxygen species are responsible for
NLRP3 dependent
caspase-1 activation in the infected cells
He et al., J Immunol 2010
(Chlamydia Infections...) :
TLR2 was required for induction of pro-IL-1beta, whereas the
NLRP3/ASC was
required for
caspase-1 activation and pro-IL-1beta cleavage to produce mature IL-1beta
Brodsky et al., Cell Host Microbe 2010
:
Here we demonstrate that
caspase-1 activation in response to the Yersinia type III secretion system ( T3SS ) requires the adaptor ASC and
involves both
NLRP3 and NLRC4 inflammasomes
Wu et al., J Clin Immunol 2010
(Listeriosis) :
Here, we have used macrophages from AIM2-, NLRC4-, NLRP3-, and ASC-deficient mice to demonstrate that AIM2, NLRC4, and
NLRP3 inflammasomes as well as the adaptor protein ASC all
contribute to activation of
caspase-1 in Listeria infected macrophages
Verma et al., Arthritis Rheum 2010
(Cryopyrin-Associated Periodic Syndromes...) :
M299V is an activating mutation in
NLRP3 resulting in elevated spontaneous
caspase 1 activity and IL-1beta
levels
Jin et al., J Clin Immunol 2010
(Infection) :
NLRP3 , a member of the NLR family of cytosolic pattern recognition receptors, along with the adaptor protein ASC,
mediates caspase-1 activation via assembly of the inflammasome in response to various pathogen derived factors as well as danger associated molecules
Takeishi et al., Drug Discov Ther 2008
:
Cryopyrin/NALP3 mediated
caspase-1 activation is involved not only in the immune response to pathogens but also in the stress response to UV irradiation in human skin
Kuipers et al., Anesthesiology 2012
(Ventilator-Induced Lung Injury) :
The presence of uric acid in lung lavage,
activation of
caspase-1 , and
NLRP3 inflammasome gene expression in lung tissue were investigated
Rathinam et al., Cell 2012
:
TRIF licenses
caspase-11 dependent
NLRP3 inflammasome activation by gram negative bacteria
Compan et al., Immunity 2012
:
Increased extracellular osmolarity prevented
caspase-1 activation by different known
NLRP3 activators
Hiramoto et al., Exp Dermatol 2012
(Acute Disease...) :
This ROS activate NLRP3, and
NLRP3 leads to the production of
caspase-1 , which subsequently increases IL-1ß, thereby finally inducing inflammation
Carlström et al., Exp Dermatol 2012
(Genetic Predisposition to Disease...) :
Polymorphisms in
NLRP3 and caspase recruitment domain containing protein ( CARD)8, a negative
regulator of
caspase-1 activity, have been associated with susceptibility to common inflammatory diseases, such as Crohn 's disease and rheumatoid arthritis
Hedl et al., Am J Physiol Gastrointest Liver Physiol 2013
(Crohn Disease...) :
Importantly, we find that, during chronic Nod2 stimulation,
NLRP3/NLRP1 inflammasome
mediated caspase-1 activation with subsequent IL-1 secretion is essential for the subsequent bifurcation to downregulated proinflammatory cytokines and upregulated bacterial killing ... Importantly, we find that, during chronic Nod2 stimulation,
NLRP3/NLRP1 inflammasome
mediated caspase-1 activation with subsequent IL-1 secretion is essential for the subsequent bifurcation to downregulated proinflammatory cytokines and upregulated bacterial killing
Case et al., Proc Natl Acad Sci U S A 2013
(Necrosis) :
Legionella activation of caspase-11 stimulated
activation of
caspase-1 through
NLRP3 and ASC
Mao et al., Cell Res 2013
(Shock, Septic) :
Here we show that nitric oxide ( NO ) inhibited the
NLRP3 mediated ASC pyroptosome formation,
caspase-1 activation and IL-1ß secretion in myeloid cells from both mice and humans
Gomes et al., J Immunol 2013
(Brucellosis...) :
In contrast, we determined that AIM2, which senses Brucella DNA, and
NLRP3 are partially
required for
caspase-1 activation and IL-1ß secretion
Yan et al., Immunity 2013
(Diabetes Mellitus, Type 2...) :
Here we show that stimulation of macrophages with ?-3 FAs, including eicosapentaenoic acid ( EPA ), docosahexaenoic acid ( DHA ), and other family members, abolished
NLRP3 inflammasome activation and
inhibited subsequent
caspase-1 activation and IL-1ß secretion
Dotson et al., J Biol Chem 2013
(Tularemia) :
An enhanced activation of
caspase-1 and IL-1ß observed in FTL_0325 mutant infected macrophages at 24 h post-infection was
independent of both AIM2 and
NLRP3
Giordano et al., J Lipid Res 2013
:
NLRP3 dependent
caspase-1 activation in hypertrophic adipocytes likely induces obese adipocyte death by pyroptosis, a proinflammatory programmed cell death
Haasken et al., Eur J Immunol 2013
:
Activation of the
NLRP3 inflammasome
results in activation of the cysteine protease
caspase-1 and the subsequent processing and secretion of the proinflammatory cytokines IL-1ß and IL-18
Jin et al., Nature communications 2013
:
LRRFIP2 negatively
regulates NLRP3 inflammasome activation in macrophages by promoting Flightless-I mediated
caspase-1 inhibition
Kim et al., Immune network 2013
:
Of particular interest, CoCl2 induced hypoxic condition considerably inhibited
NLRP3 dependent
caspase-1 activation in mixed glial cells, but not in bone marrow derived macrophages