Short-term delay of Fas-stimulated apoptosis by GM-CSF as a result of temporary suppression of FADD recruitment in neutrophils: evidence implicating phosphatidylinositol 3-kinase and MEK1-ERK1/2 pathways downstream of classical protein kinase C

Kotone-Miyahara, Yasuko; Yamashita, Kouhei; Lee, Kyung-Kwon; Yonehara, Shin; Uchiyama, Takashi; Sasada, Masataka; Takahashi, Atsushi

doi:10.1189/jlb.0104048

Cited by 28 publications

(25 citation statements)

References 70 publications

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“…The histogram in Fig. 3A confirms the observation of others (Iwai et al 1994, Liles et al 1996, Kotone-Miyahara et al 2004) that neutrophils express Fas. As shown in Fig.…”

Section: Igf1 Does Not Affect Fas Expression and Caspase-8 Activationsupporting

confidence: 88%

“…This concentration of CH11 has been shown to stimulate Fasmediated apoptosis in neutrophils. It activates caspase-8 ( Kotone-Miyahara et al 2004, Iwase et al 2006 and it evokes the recruitment of FADD to Fas (Kotone-Miyahara et al 2004). Indeed, stimulation of the extrinsic pathway by CH11 further increased the percentage of apoptotic neutrophils to 39 .…”

Section: Inhibition Of Spontaneous and Fas-mediated Apoptosismentioning

confidence: 99%

“…Some of these factors are able to modulate each other's effects. For instance, it has been shown that CSF2 is able to delay Fas-mediated apoptosis by suppression of Fasassociated protein with dead domain (FADD) recruitment (Kotone-Miyahara et al 2004) and that activation of TNFRSF9 abrogates the anti-apoptotic effects of CSF2 in neutrophils (Heinisch et al 2000). It has also been shown that TNF down-regulates TNFRSF9 expression on neutrophils, indicating that the extrinsic route for apoptosis can be inhibited by cytokines (Heinisch et al 2000).…”

Section: Introductionmentioning

confidence: 99%

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Insulin-like growth factor-1 delays Fas-mediated apoptosis in human neutrophils through the phosphatidylinositol-3 kinase pathway

Himpe

Degaillier²,

Coppens³

et al. 2008

Journal of Endocrinology

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Apoptosis of human neutrophils is a crucial mechanism for the resolution of inflammation. We previously showed that insulinlike growth factor-1 (IGF1) delays spontaneous neutrophil apoptosis without influencing the secretion of cytokines by these cells. In the present study, we further addressed the role of IGF1 in regulating neutrophil survival in the presence of other factors present during inflammation, and the mechanism involved in delaying apoptosis. We show that IGF1 delays neutrophil apoptosis triggered by the agonistic anti-Fas antibody CH11 and that the effect of IGF1 is comparable in magnitude to that of the acknowledged anti-apoptotic cytokines interferon-g (IFNG) and granulocyte-macrophage colony-stimulating factor (GM-CSF; now known as CSF2). Furthermore, IGF1 exerted additional effects on cell survival in the presence of these cytokines. IGF1 did not affect Fas expression or activation by anti-Fas of caspase-8, but inhibited the depolarization of the mitochondrial membrane. Inhibitor studies indicate that the phosphatidylinositol-3 kinase (PI3K) pathway, but not the MEK-ERK pathway, mediates the effects of IGF1. However, in contrast to CSF2, IGF1 did not induce phosphorylation and translocation to the membrane of AKT, the canonical downstream target of PI3K. We therefore speculate that other downstream targets of PI3K are involved in the delay of neutrophil apoptosis by IGF1, possibly through stabilization of the mitochondrial membrane.

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“…The histogram in Fig. 3A confirms the observation of others (Iwai et al 1994, Liles et al 1996, Kotone-Miyahara et al 2004) that neutrophils express Fas. As shown in Fig.…”

Section: Igf1 Does Not Affect Fas Expression and Caspase-8 Activationsupporting

confidence: 88%

Section: Inhibition Of Spontaneous and Fas-mediated Apoptosismentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Insulin-like growth factor-1 delays Fas-mediated apoptosis in human neutrophils through the phosphatidylinositol-3 kinase pathway

Himpe

Degaillier²,

Coppens³

et al. 2008

Journal of Endocrinology

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show abstract

“…The fact that the apoptotic response is restored in the presence of PD98058 is an indication that the protective function of ERK occurs downstream of MEK1. In neutrophils, the activation of MEK1-ERK axis by granulocyte macrophage colonystimulating factor confers protective function against Fas-induced apoptosis by impairing the recruitment of FADD to Fas (47). Given that the apoptotic functions of DR3 are tightly associated with the recruitment of FADD (22,25), a likely possibility is that E-selectin-mediated activation of ERK protects against apoptosis by impairing the recruitment of FADD to DR3.…”

Section: Discussionmentioning

confidence: 99%

Death Receptor-3, a New E-Selectin Counter-Receptor that Confers Migration and Survival Advantages to Colon Carcinoma Cells by Triggering p38 and ERK MAPK Activation

et al. 2006

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E-selectin-mediated adhesion of colon cancer cells to endothelial cells is a key event in metastasis. However, the signaling mechanisms that confer metastatic advantages to cancer cells adhering to E-selectin are ill defined. By using affinity column chromatography and pull-down assays on purified membrane extracts of HT29 and LoVo cells coupled to mass spectrometry analysis, we obtained the first evidence indicating that E-selectin binds to death receptor-3 (DR3) expressed by the cancer cells. Thereafter, we accumulated several results, suggesting that DR3 is an E-selectin receptor on colon cancer cells and that its activation by E-selectin triggers the activation of p38 and extracellular signalregulated kinase (ERK) mitogen-activated protein kinase (MAPK) and confers migration and survival advantages. First, by Western blotting, we found that the E-selectin-binding protein, identified as DR3, is recognized by two anti-DR3 antibodies. Second, the neutralization of DR3 with an antibody and its knockdown by small interfering RNA decrease the adhesion of colon cancer cells to E-selectin and E-selectinexpressing human umbilical vein endothelial cells. Third, inhibiting DR3 and knocking down its expression impair transendothelial migration of HT29 cells and block the activation of p38 and ERK by E-selectin. Fourth, high molecular weight isoforms of DR3 are expressed in samples of primary human colon carcinoma but not in samples from normal colon tissue. Intriguingly, DR3 is a death receptor but its activation by E-selectin does not induce apoptosis in colon cancer cells, except when ERK is inhibited. Our findings identify novel signaling and functional roles of DR3 activated in response to E-selectin and highlight the potential link between DR3 and metastasis. (Cancer Res 2006; 66(18): 9117-24)

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“…To signal, the receptor dimerizes with another ab complex, and the b-chains interact to induce proliferation (20) through Jak2/ STAT5 and the MAPK pathway. In an inflammatory environment, GM-CSF signaling counterbalances IFN-g's antiproliferative effects on T cells by antagonizing STAT1 (21,22), in addition to promoting the mobilization of monocytes, the maturation of DCs, and the survival and activation of macrophages and granulocytes (23,24). SOCS3's regulation of GM-CSFR signaling was made evident through how SOCS3 2/2 animals developed erythrocytosis and in how the transgenic expression of SOCS3 inhibited erythropoiesis.…”

Section: Combining Cytokines To Target Distinct Immune Cellular Subsetsmentioning

confidence: 99%

GM-CSF–Based Fusion Cytokines as Ligands for Immune Modulation

Williams

Galipeau

2011

The Journal of Immunology

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Chromosomal translocations that combine distinct functional domains of unrelated proteins are an experiment in nature. They demonstrate how endogenous regulatory checkpoints can be overridden by altered cell biochemistry, informing a means to engineering an aberrant signal that the cell is incapable of counterregulating. Thus, our laboratory and others have synthesized fusions of GM-CSF with peptides, ILs, and chemokines, which we have termed fusokines, with the aim of inducing an enhanced immune response against cancer, aiming to overcome the maladapted biological processes causing disease. In doing so, we found that these fusokines did not behave as merely the sum of their natural unfused counterparts, but as entirely novel ligands co-opting their cognate receptor to communicate a unique message to responsive cellular targets. In this review, we discuss how fusion proteins combining different bioactive ligands can alter immune responses and briefly discuss the regulatory pathways that they circumvent.

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Short-term delay of Fas-stimulated apoptosis by GM-CSF as a result of temporary suppression of FADD recruitment in neutrophils: evidence implicating phosphatidylinositol 3-kinase and MEK1-ERK1/2 pathways downstream of classical protein kinase C

Cited by 28 publications

References 70 publications

Insulin-like growth factor-1 delays Fas-mediated apoptosis in human neutrophils through the phosphatidylinositol-3 kinase pathway

Insulin-like growth factor-1 delays Fas-mediated apoptosis in human neutrophils through the phosphatidylinositol-3 kinase pathway

Death Receptor-3, a New E-Selectin Counter-Receptor that Confers Migration and Survival Advantages to Colon Carcinoma Cells by Triggering p38 and ERK MAPK Activation

GM-CSF–Based Fusion Cytokines as Ligands for Immune Modulation

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