Tumor suppressor death-associated protein kinase is required for full IL-1β production

Chuang, Ya-Ting; Lin, Yu-Chuang; Lin, Kuan‐Hung; Chou, Ting-Fang; Kuo, Wen-Chih; Yang, Kaiting; Wu, Pei‐Rung; Chen, Ruey‐Hwa; Kimchi, Adi; Lai, Ming‐Zong

doi:10.1182/blood-2010-08-303115

Cited by 60 publications

(57 citation statements)

References 50 publications

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“…It was reported that knockdown of DAPK1 attenuated interleukin 1β production in macrophages. 16 On the other hand, it was shown that DAPK1 and DAPK3 had negative regulatory roles in the expression of inflammatory genes, including ribosomal protein L13a, extracellular signal-regulated kinase, and interferon-γ-activated inhibitor of translation in macrophages.…”

Section: October 2012mentioning

confidence: 99%

Death-Associated Protein Kinase 3 Mediates Vascular Inflammation and Development of Hypertension in Spontaneously Hypertensive Rats

et al. 2012

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C almodulin (CaM) is recognized as a key regulatory molecule for diverse biological functions, such as muscular contraction.1 In addition, a recent study demonstrated that CaM-dependent protein kinases, such as CaM-dependent protein kinase II, may regulate hypertension through the mechanisms including promotion of vascular smooth muscle hypertrophy. 2 In the previous study, we compared expression levels of several CaM-related proteins with almost unknown functions in vasculature. As a result, we demonstrated that protein expression of eukaryotic elongation factor 2 kinase (also known as CaM-dependent protein kinase III), histone deacetylase 4, and death associated protein kinase (DAPK) 3 increased in the mesenteric artery from spontaneously hypertensive rats (SHRs) compared with Wistar Kyoto rats (WKYs). 3 In the recent study, we also showed that histone deacetylase 4 promotes reactive oxygen species (ROS)-dependent vascular inflammation and mediates the development of hypertension in SHRs. 4 However, it remains to be clarified how DAPK3, might affect vascular patholophysiology and control the development of hypertension. The DAPK protein has been considered as a Ca 2+ /CaMregulated serine/threonine kinase that mainly mediates cell death. 5 The DAPK protein consists of multiple domains, including an N-terminal kinase domain (known as a Ca 2+ /CaM regulatory region), ankyrin repeats, a cytoskeleton binding region, and a C-terminal death domain.6 Various stimulation-induced intracellular calcium spikes promote the CaM binding to the CaM regulatory region of DAPK, which in turn activates DAPK.7 Five protein kinases, including DAPK1, DAPK2, DAPK3 (also known as Zipper-interacting protein kinase), DAPK-related apoptosis-inducing protein kinase 1, and DAPK-related apoptosis-inducing protein kinase 2, are known as DAPK family proteins.8 DAPK1, DAPK2, and DAPK3 are all ubiquitously expressed in various tissues from mice and rats.6 Recently, the functions of DAPK3 were gradually clarified. The mutation of DAPK3 Abstract-Death-associated protein kinase (DAPK) is a Ca 2+ /calmodulin-regulated serine/threonine kinase that mediates cell death. Our recent study demonstrated that DAPK3 protein increases in the mesenteric artery from spontaneously hypertensive rats compared with Wistar Kyoto rats. Pathogenesis of hypertension is modulated at least in part by vascular inflammation. We examined whether DAPK3 mediates vascular inflammatory responses and development of hypertension. In rat mesenteric arterial smooth muscle cells, small interfering RNA against DAPK3 inhibited vascular cell adhesion molecule 1 expression and monocyte adhesion induced by tumor necrosis factor-α. DAPK3 small interfering RNA inhibited phosphorylation of c-Jun amino-terminal kinase, p38, and Akt, as well as reactive oxygen species (ROS) production induced by tumor necrosis factor-α. In human umbilical vein endothelial cells, expressions of vascular cell adhesion molecule 1, endothelial selectin, and cyclooxygenase 2, as well as ROS production induced ...

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Section: October 2012mentioning

confidence: 99%

Death-Associated Protein Kinase 3 Mediates Vascular Inflammation and Development of Hypertension in Spontaneously Hypertensive Rats

et al. 2012

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“…To test this hypothesis, two sets of experiments were performed. First, we examined the effect of the V protein on IL-1␤ secretion of HEK293T cells transiently transfected with plasmids encoding components of the NLRP3 inflammasome: NLRP3, ASC, procaspase-1, and pro-IL-1␤ (10). In this experiment, HEK293T cells were used, as they are human cells that can be transfected at a high efficiency.…”

Section: V Protein Inhibits Mv-induced Il-1␤ Secretionmentioning

confidence: 99%

Measles Virus V Protein Inhibits NLRP3 Inflammasome-Mediated Interleukin-1β Secretion

Komune

Ichinohe

Ito

et al. 2011

J Virol

103

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Measles is an acute contagious disease that remains a major cause of childhood mortality worldwide, especially in developing countries (6). Measles virus (MV), a member of the family Paramyxoviridae, is an enveloped virus with a nonsegmented single-stranded negative-sense RNA genome (15). Upon MV infection, cells produce alpha/beta interferon (IFN-␣/␤) following recognition of the virus by RNA helicases encoded by retinoic acid-inducible gene I (RIG-I) and melanoma differentiation-associated gene 5 (MDA5) (22, 43) or Toll-like receptor (TLR) 7 (51). MV encodes phosphoprotein (P) and V and C proteins, which can counteract the host IFN response (11,34,36,54,64). Among these viral proteins, the V protein is the most versatile antagonist. It blocks IFN-␣/␤ signal transduction in infected cells (9,11,13,36,38,47,59,64) and inhibits TLR7-mediated IFN-␣ production in human plasmacytoid dendritic cells (42). Furthermore, the MV V protein, like that of other paramyxoviruses, interacts with MDA5 and inhibits its function with respect to IFN induction (2). The N-terminal domain of the V protein (Vn), which is common to the P and V proteins, has been shown to interact with STAT1 (signal transducer and activator of transcription 1) and Jak1, which are involved in IFN signaling (9), whereas the unique cysteine-rich C-terminal domain of the V protein (Vc) was found to interact with MDA5 (39), STAT2 (47), and IB kinase ␣ (IKK␣), which is involved in the activation of interferon-regulatory factor 7 through TLR7 (42). Furthermore, Vc interacts with the NF-B subunit p65 (RelA) to suppress NF-B activity (53). The mechanism by which the MV C protein acts as an IFN antagonist is not well understood, but it probably suppresses IFN induction by regulating viral RNA synthesis (34).Secretion of the inflammatory cytokines interleukin-1␤ (IL-1␤) and IL-18 is tightly regulated by the inflammasomes known as caspase-1-activating molecular complexes (32). Recognition of pathogens by pattern recognition receptors such as TLRs induces pro-IL-1␤ and pro-IL-18 in the cytoplasm. The activation of the inflammasomes leads to the conversion of procaspase-1 to caspase-1, which cleaves procytokines into mature IL-1␤ and IL-18, which are then secreted. The best-characterized inflammasome is the NOD-like receptor (NLR)-family pyrin domain-containing 3 (NLRP3, also known as Nalp3 or cryopyrin) inflammasome, which can be activated by a wide range of stimuli, such as endogenous danger signals from damaged cells, bacterial components, and environmental irritants (52).Infection by RNA viruses such as influenza virus (1,19,20,61), encephalomyocarditis virus (EMCV) (44, 45), and vesicular stomatitis virus (VSV) (45) also stimulates NLRP3, which then recruits the apoptosis-associated speck-like protein containing a caspase recruitment domain (ASC) and procaspase-1, forming the NLRP3 inflammasome. How RNA viruses are recognized by NLRP3 is not well-known, but in the case of influenza virus, the proton-selective ion channel M2 protein, not genomic RNA, has been sho...

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“…3), we examined whether TIFA phosphorylation and oligomerization can induce the assembly and activation of NLRP3 inflammasome. To functionally link Akt phosphorylation of TIFA with inflammasome activation, we performed an NLRP3 inflammasome reconstitution assay in HEK293T cells lacking the endogenous inflammasome core proteins (23,24). HEK293T cells were cotransfected with NLRP3, ASC, procaspase-1, and pro-IL-1β together with Akt WT, TIFA siRNA, Akt K14R (i.e., loss-of-function mutant), or Akt E17K (i.e., gain-of-function mutant).…”

Section: Tifa Induces the Assembly And Activation Of Nlrp3 Inflammasomentioning

confidence: 99%

TIFA as a crucial mediator for NLRP3 inflammasome

Lin

Wei

et al. 2016

Proc. Natl. Acad. Sci. U.S.A.

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Toll-like receptor-mediated NF-κB activation is a major innate immune reaction of vascular endothelial cells (ECs) in response to prooxidative and proinflammatory stimuli. We identified that TNF-α receptor-associated factor-interacting protein with a forkhead-associated domain (TIFA) is a regulator of priming (signal 1) and activating (signal 2) signals of nucleotide oligomerization domain-like receptor family pyrin domain-containing protein 3 (NLRP3) inflammasome in ECs. Oxidative and inflammatory stresses such as atheroprone flow and hyperlipidemia induce and activate TIFA in vitro and in vivo. For the priming of signal 1, sterol regulatory element-binding protein 2 transactivates TIFA, which in turn induces NF-κB activation and augments the transcription of NLRP3 inflammasome components. For the activation of signal 2, Akt is involved in TIFA Thr9 phosphorylation, which is essential for TIFA-TIFA homophilic oligomerization. Thr9 phosphorylation-dependent TIFA oligomerization facilitates the higher-order assembly of NLRP3 inflammasome, as indicated by the interaction between TIFA and caspase-1 in the activated ECs. Our results suggest that TIFA is a crucial mediator in the endothelial innate immune response by potentiating and amplifying NLRP3 inflammasome via augmenting signals 1 and 2.endothelial cells | inflammasome | innate immunity | NLRP3 | TIFA

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Tumor suppressor death-associated protein kinase is required for full IL-1β production

Cited by 60 publications

References 50 publications

Death-Associated Protein Kinase 3 Mediates Vascular Inflammation and Development of Hypertension in Spontaneously Hypertensive Rats

Death-Associated Protein Kinase 3 Mediates Vascular Inflammation and Development of Hypertension in Spontaneously Hypertensive Rats

Measles Virus V Protein Inhibits NLRP3 Inflammasome-Mediated Interleukin-1β Secretion

TIFA as a crucial mediator for NLRP3 inflammasome

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