Activation of mitogen-activated protein kinase cascades during priming of human neutrophils by TNF-α and GM-CSF

McLeish, Kenneth R.; Knall, Cindy; Ward, Richard A.; Gerwins, Pär; Coxon, Patricia Y.; Klein, Jon B.; Johnson, Gary L.

doi:10.1002/jlb.64.4.537

Cited by 152 publications

(159 citation statements)

References 62 publications

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“…been linked to the inhibition of apoptosis in granulocytes [24]. This is in agreement with our data, which indicate that the Erk1/2 signaling pathway mediates the survival-promoting effect of CEACAM1 in rat granulocytes.…”

Section: Discussionsupporting

confidence: 93%

CEACAM1 (CD66a) mediates delay of spontaneous and Fas ligand-induced apoptosis in granulocytes

et al. 2005

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Granulocytes form the first and fastest line of defense against pathogenic infections. Their survival is limited by apoptosis, a process that is critical for the resolution of inflammation. Pro-apoptotic and pro-inflammatory cytokines, as well as several receptors, can alter the lifespan of granulocytes. Here we report that the carcinoembryonic antigen-related cell adhesion molecule 1 (CEACAM1, CD66a) is involved in the regulation of granulocyte survival. Until now CEACAM1 is described to control cell proliferation, cell migration, tumor growth, angiogenesis and diverse leukocyte functions. However, very little is known about its role in granulocytes. We found that CEACAM1 expression in resting rat granulocytes is significantly higher than in other leukocyte subtypes. Stimulation led to a strongly increased CEACAM1 cell surface expression and to release of soluble CEACAM1. DNA fragmentation assays and annexin V staining revealed that binding of CEACAM1-specific antibodies, Fab fragments and soluble CEACAM1-Fc constructs to cell surface-expressed CEACAM1 causes a delay of spontaneous and Fas ligand (CD95L)-induced apoptosis. Tyrosine phosphorylation of CEACAM1-L, its association with SHP-1, the activation of Erk1/2 and caspase-3 appeared to be crucial for the CEACAM1-mediated anti-apoptotic effect. These findings provide evidence that CEACAM1 influences the resolution of inflammation by prolonging the survival of rat granulocytes.

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Section: Discussionsupporting

confidence: 93%

CEACAM1 (CD66a) mediates delay of spontaneous and Fas ligand-induced apoptosis in granulocytes

et al. 2005

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“…As shown in Fig. 3A, both fMLF and GM-CSF potently elicited the phosphorylation of p38 MAPK, ERK1/2, and Akt, as expected (32,35,36); by contrast, JNK was not phosphorylated in response to these stimuli (data not shown). Inhibition of TAK1 resulted in the abrogation of inducible ERK phosphorylation across the entire time course, whereas P-Akt levels are unaffected by the inhibitor (Fig.…”

Section: Impact Of Tak1 On Fmlf and Gm-csf Signaling In Human Neutropsupporting

confidence: 58%

Activation of TAK1 by Chemotactic and Growth Factors, and Its Impact on Human Neutrophil Signaling and Functional Responses

Sylvain-Prévost

Ear

Simard

et al. 2015

The Journal of Immunology

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The MAP3 kinase, TAK1, is known to act upstream of IKK and MAPK cascades in several cell types, and is typically activated in response to cytokines (e.g., TNF, IL-1) and TLR ligands. In this article, we report that in human neutrophils, TAK1 can also be activated by different classes of inflammatory stimuli, namely, chemoattractants and growth factors. After stimulation with such agents, TAK1 becomes rapidly and transiently activated. Blocking TAK1 kinase activity with a highly selective inhibitor (5z-7-oxozeaenol) attenuated the inducible phosphorylation of ERK occurring in response to these stimuli but had little or no effect on that of p38 MAPK or PI3K. Inhibition of TAK1 also impaired MEKK3 (but not MEKK1) activation by fMLF. Moreover, both TAK1 and the MEK/ERK module were found to influence inflammatory cytokine expression and release in fMLF- and GM-CSF–activated neutrophils, whereas the PI3K pathway influenced this response independently of TAK1. Besides cytokine production, other responses were found to be under TAK1 control in neutrophils stimulated with chemoattractants and/or GM-CSF, namely, delayed apoptosis and leukotriene biosynthesis. Our data further emphasize the central role of TAK1 in controlling signaling cascades and functional responses in primary neutrophils, making it a promising target for therapeutic intervention in view of the foremost role of neutrophils in several chronic inflammatory conditions.

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“…TNFα has many known signal transduction pathways such as NF-kB activation [14], MAPK activation [15], and the induction of cell death [16]. Moreover, TNFα induces apoptosis through the production of reactive oxygen species [17] and by activating caspase [18].…”

Section: Introductionmentioning

confidence: 99%

Silver nanoparticles reduce the apoptosis induced by tumor necrosis factor-α

Fehaid

Taniguchi

2018

Science and Technology of Advanced Materials

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Silver nanoparticles (AgNPs) are widely known to have anti-inflammatory properties, but the exact mechanism underlying this anti-inflammatory effect is not clearly understood. Tumor necrosis factor-α (TNFα) is a major pro-inflammatory cytokine that is expressed in the early stage of cell inflammation and induces apoptosis by several known pathways. Our study aimed to investigate the effect of AgNPs on the response of lung epithelial cells to TNFα and the molecular mechanism of this response. Lung epithelial cell line NCI-H292 cells were exposed to AgNPs (5 µg/mL) and/or TNFα (20 ng/mL) for 24 h, then cellular uptake was analyzed using flow cytometry. Our results showed that AgNPs were taken up by cells in a dose-dependent manner and that the cellular uptake ratio of AgNPs was significantly increased in the presence of TNFα. Apoptosis assays indicated that exposure to AgNPs significantly decreased the apoptotic effect of TNFα. Confocal microscopy was used to localize the tumor necrosis factor receptor 1 (TNFR1) and revealed that TNFR1 localized on the surface of cells exposed to TNFα. In contrast, TNFR1 localized inside cells exposed to both AgNPs and TNFα, with very few receptors scattered on the cell membrane. The results indicated that AgNPs reduced the cell surface TNFR1 expression level. The results suggested that the reduction of surface TNFR1 reduced cellular response to TNFα, resulting in an anti-apoptotic effect.

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Activation of mitogen-activated protein kinase cascades during priming of human neutrophils by TNF-α and GM-CSF

Cited by 152 publications

References 62 publications

CEACAM1 (CD66a) mediates delay of spontaneous and Fas ligand-induced apoptosis in granulocytes

CEACAM1 (CD66a) mediates delay of spontaneous and Fas ligand-induced apoptosis in granulocytes

Activation of TAK1 by Chemotactic and Growth Factors, and Its Impact on Human Neutrophil Signaling and Functional Responses

Silver nanoparticles reduce the apoptosis induced by tumor necrosis factor-α

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