Reactive Oxygen Species and p38 Mitogen-activated Protein Kinase Mediate Tumor Necrosis Factor α-Converting Enzyme (TACE/ADAM-17) Activation in Primary Human Monocytes

Scott, Alasdair; O’Dea, Kieran P.; O’Callaghan, David; Williams, Lynn M.; Dokpesi, Justina O.; Tatton, Louise; Handy, Jonathan; Hogg, Philip J.; Takata, Masao

doi:10.1074/jbc.m111.277434

Cited by 104 publications

(87 citation statements)

References 66 publications

(82 reference statements)

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“…It is thought that endothelial TACE is activated by mitochondrial reactive oxygen species in response to changes in calcium levels. In other models and in CHO or HL-60 cells, TACE activation has been shown to be ATP-(60), calcium-, or mitogen-activated protein kinase-dependent (61)(62)(63). Nitrosylation of TACE in macrophages has been shown to be involved in TACE activation for TNF␣ maturation (33).…”

Section: Discussionmentioning

confidence: 99%

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A Role for cGMP in Inducible Nitric-oxide Synthase (iNOS)-induced Tumor Necrosis Factor (TNF) α-converting Enzyme (TACE/ADAM17) Activation, Translocation, and TNF Receptor 1 (TNFR1) Shedding in Hepatocytes

Chanthaphavong

Loughran

Lee

et al. 2012

Journal of Biological Chemistry

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Background: iNOS/NO blocks TNF␣-induced apoptosis by cGMP-dependent and cGMP-independent mechanisms in hepatocytes. Result: TLR4-dependent iNOS expression in hepatocytes leads to NO/cGMP/PKG-dependent TACE/ADAM17 and iRhom2 phosphorylation and interaction, TACE/ADAM17 activation/surface translocation, and TNFR1 shedding. Conclusion: iNOS expression leads to rapid TNFR1 shedding through NO/cGMP/PKG-dependent translocation and activation of TACE/ADAM17. Significance: This novel mechanism for iNOS/NO/cGMP-induced TACE activation and translocation may limit TNF␣-mediated signaling.

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Section: Discussionmentioning

confidence: 99%

“…Other studies have shown that TACE can be phosphorylated by kinases, such as p38 MAPK. This kinase has been found to phosphorylate TACE in lymphocytes and monocytes (62). Phosphorylation of the cytoplasmic domain of TACE can occur not only on a threonine but also on a serine (55)(56)(57)(58).…”

Section: Discussionmentioning

confidence: 99%

A Role for cGMP in Inducible Nitric-oxide Synthase (iNOS)-induced Tumor Necrosis Factor (TNF) α-converting Enzyme (TACE/ADAM17) Activation, Translocation, and TNF Receptor 1 (TNFR1) Shedding in Hepatocytes

Chanthaphavong

Loughran

Lee

et al. 2012

Journal of Biological Chemistry

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“…We next examined mechanisms for NOD2-induced early TACE activation. The MAPK p38 can induce TACE activity (27). ERK, p38, JNK, and NF-κB activation were required for NOD2-induced early TACE activity and TNFSF15 processing (Fig.…”

Section: Tnfsf15 Stimulates Dr3 To Initiate Downstream Signaling Requmentioning

confidence: 99%

A TNFSF15 disease-risk polymorphism increases pattern-recognition receptor-induced signaling through caspase-8–induced IL-1

Hedl

Abraham

2014

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

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Inflammatory diseases are characterized by dysregulated cytokine production. Altered functions for most risk loci, including the inflammatory bowel disease and leprosy-associated tumor necrosis factor ligand superfamily member 15 (TNFSF15) region, are unclear. Regulation of pattern-recognition-receptor (PRR)-induced signaling and cytokines is crucial for immune homeostasis; TNFSF15:death receptor 3 (DR3) contributions to PRR responses have not been described. We found that human macrophages expressed DR3 and that TNFSF15:DR3 interactions were critical for amplifying PRR-initiated MAPK/NF-κB/PI3K signaling and cytokine secretion in macrophages. Mechanisms mediating TNFSF15:DR3 contributions to PRR outcomes included TACE-induced TNFSF15 cleavage to soluble TNFSF15; soluble TNFSF15 then led to TRADD/FADD/MALT-1-and caspase-8-mediated autocrine IL-1 secretion. Notably, TNFSF15 treatment also induced cytokine secretion through a caspase-8-dependent pathway in intestinal myeloid cells. Importantly, rs6478108 A disease risk-carrier macrophages demonstrated increased TNFSF15 expression and PRR-induced signaling and cytokines. Taken together, TNFSF15:DR3 interactions amplify PRR-induced signaling and cytokines, and the rs6478108 TNFSF15 disease-risk polymorphism results in a gain of function.Crohn disease | ulcerative colitis | genetics | NOD2 | TLR

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“…Trovafloxacin Increases LPS-Induced TNF Release in RAW Cells involve p38 at several levels: activation of trans-acting factors, stabilization of TNF mRNA, and shedding of membrane-bound TNF (Deleault et al, 2008;Rowlett et al, 2008;Scott et al, 2011). Surprisingly, p38 inhibition failed to alter the TVXmediated increase in TNF mRNA (Fig.…”

Section: Discussionmentioning

confidence: 93%

Trovafloxacin Potentiation of Lipopolysaccharide-Induced Tumor Necrosis Factor Release from RAW 264.7 Cells Requires Extracellular Signal-Regulated Kinase and c-Jun N-Terminal Kinase

Poulsen

Albee

Ganey

et al. 2014

J Pharmacol Exp Ther

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Trovafloxacin (TVX) is a fluoroquinolone antibiotic known to cause idiosyncratic, drug-induced liver injury (IDILI) in humans. The mechanism underlying this toxicity remains unknown. Previously, an animal model of IDILI in mice revealed that TVX synergizes with inflammatory stress from bacterial lipopolysaccharide (LPS) to produce a hepatotoxic interaction. The liver injury required prolongation of the appearance of tumor necrosis factor-a (TNF) in the plasma. The results presented here describe a model of TVX/LPS coexposure in RAW 264.7 cells acting as a surrogate for TNFreleasing cells in vivo. Pretreating cells with TVX for 2 hours before LPS addition led to increased TNF protein release into culture medium in a concentration-and time-dependent manner relative to cells treated with LPS or TVX alone. During the pretreatment period, TVX increased TNF mRNA, but this was less apparent when cells were exposed to TVX after LPS addition, suggesting that the pivotal signaling events that increase TNF expression occurred during the TVX pretreatment period. Indeed, TVX exposure increased activation of extracellular signal-regulated kinase (ERK), c-Jun N-terminal kinase (JNK), and p38 mitogen-activated protein kinase. Inhibition of either ERK or JNK decreased the TVX-mediated increase in TNF mRNA and LPS-induced TNF protein release, but p38 inhibition did not. These results demonstrated that the increased TNF appearance from TVX-LPS interaction in vivo can be reproduced in vitro and occurs in an ERK-and JNK-dependent manner.

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Reactive Oxygen Species and p38 Mitogen-activated Protein Kinase Mediate Tumor Necrosis Factor α-Converting Enzyme (TACE/ADAM-17) Activation in Primary Human Monocytes

Cited by 104 publications

References 66 publications

A Role for cGMP in Inducible Nitric-oxide Synthase (iNOS)-induced Tumor Necrosis Factor (TNF) α-converting Enzyme (TACE/ADAM17) Activation, Translocation, and TNF Receptor 1 (TNFR1) Shedding in Hepatocytes

A Role for cGMP in Inducible Nitric-oxide Synthase (iNOS)-induced Tumor Necrosis Factor (TNF) α-converting Enzyme (TACE/ADAM17) Activation, Translocation, and TNF Receptor 1 (TNFR1) Shedding in Hepatocytes

A TNFSF15 disease-risk polymorphism increases pattern-recognition receptor-induced signaling through caspase-8–induced IL-1

Trovafloxacin Potentiation of Lipopolysaccharide-Induced Tumor Necrosis Factor Release from RAW 264.7 Cells Requires Extracellular Signal-Regulated Kinase and c-Jun N-Terminal Kinase

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