Signal transduction pathways involved in soluble fractalkine–induced monocytic cell adhesion

Cambien, Béatrice; Pomeranz, Manuel; Schmid-Antomarchi, Heidy; Millet, Marie-Ange; Breittmayer, Violette A.; Rossi, Bernard; Schmid-Alliana, Annie

doi:10.1182/blood.v97.7.2031

Cited by 82 publications

(85 citation statements)

References 55 publications

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“…Indeed, many groups have reported that s-FKN can mediate both chemotaxis and adhesion of monocytes and THP-1 cells, whereas Pan et al (19) have reported that neither the chemokine-like domain nor the entire extracellular domain of FKN have chemotactic effects on human monocytes and THP1 cells. In our present study, we show that s-FKN, which as we have previously reported, increases adherence of monocytic MonoMac6 cells (28), fails to induce the migration of MonoMac6 cells and monocytes. Imai et al (22), who had initially reported a chemotactic effect of s-FKN, which they qualified as marginal compared with MCP-1, presented evidence in a following report (25), that, in monocytes, FKN functioned as an adhesion molecule, strengthening the interaction between monocytes and endothelial cells, rather than as a chemotactic factor.…”

Section: Discussionsupporting

confidence: 59%

Soluble Fractalkine Prevents Monocyte Chemoattractant Protein-1-Induced Monocyte Migration via Inhibition of Stress-Activated Protein Kinase 2/p38 and Matrix Metalloproteinase Activities

Vitale

Schmid-Alliana

Breuil

et al. 2004

The Journal of Immunology

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In this study, we address the question of the cross-talk between two chemokines that are cosecreted during inflammation, namely monocyte chemoattractant protein-1 (MCP-1) and soluble fractalkine (s-FKN), toward monocyte migration. We found that s-FKN fails to induce MonoMac6 cell migration per se. Interestingly, this chemokine antagonizes transendothelial migration and chemotaxis of MonoMac6 cells and freshly isolated human monocytes induced by MCP-1, indicating a direct effect of s-FKN on monocytic cells. In this study, we found that stress-activated protein kinase (SAPK)1/c-Jun N-terminal kinase 1 and SAPK2/p38 are involved in the control of MCP-1-induced MonoMac6 cell migration. We demonstrated that s-FKN abrogates the MCP-1-induced SAPK2/p38 activation as well as the upstream Pyk2 activity. Furthermore, we observed that s-FKN also inhibits the activity of a major matrix metalloproteinase (MMP), namely MMP-2. Taken collectively, our results indicate that the s-FKN antagonizes the chemoattractant effect of MCP-1 on monocytes, likely by inhibiting crucial signaling pathways, like SAPK2/p38 and MMP-2 activities.

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Section: Discussionsupporting

confidence: 59%

Soluble Fractalkine Prevents Monocyte Chemoattractant Protein-1-Induced Monocyte Migration via Inhibition of Stress-Activated Protein Kinase 2/p38 and Matrix Metalloproteinase Activities

Vitale

Schmid-Alliana

Breuil

et al. 2004

The Journal of Immunology

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“…Upon incubation with CX 3 CL1, the former cells showed increased phosphorylation of PI3K, Erk1/2, Akt and Src and de novo induction of p-p38 (ref. 29), similar to that reported for normal germinal center B cells. 17 Studies with specific inhibitors demonstrated that all of the above kinases were involved in CX 3 CL1-induced chemotaxis, indicating that the PI3K and Src platforms integrated signals from either scaffold.…”

Section: Discussionsupporting

confidence: 87%

“…Five purified leukemic cell suspensions that migrated to CX 3 CL1 were incubated for different times with or without CX 3 CL1 and subjected to western blot or immunoprecipitation analyses using antibodies against unphoshorylated and phosphorylated (p)-p38, Akt, Erk1 and Erk2 and Src. 29 Quantitative analysis of the bands was performed by densitometry. Akt, Erk1, Erk2, and Src, but not p38 were constitutively phosphorylated in all CLL suspensions (Figure 2a).…”

Section: Cl1-driven Signal Transduction In Cll Cellsmentioning

confidence: 99%

A novel role of the CX3CR1/CX3CL1 system in the cross-talk between chronic lymphocytic leukemia cells and tumor microenvironment

et al. 2011

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Several chemokines/chemokine receptors such as CCR7, CXCR4 and CXCR5 attract chronic lymphocytic leukemia (CLL) cells to specific microenvironments. Here we have investigated whether the CX 3 CR1/CX 3 CL1 axis is involved in the interaction of CLL with their microenvironment. CLL cells from 52 patients expressed surface CX 3 CR1 and CX 3 CL1 and released constitutively soluble CX 3 CL1. One third of these were attracted in vitro by soluble CX 3 CL1. CX 3 CL1-induced phosphorylation of PI3K, Erk1/2, p38, Akt and Src was involved in induction of CLL chemotaxis. Leukemic B cells upregulated CXCR4 upon incubation with CX 3 CL1 and this was paralleled by increased chemotaxis to CXCL12. Akt phosphorylation was involved in CX 3 CL1-induced upregulation of CXCR4 on CLL. In proliferation centers from CLL lymph node and bone marrow, CX 3 CL1 was expressed by CLL cells whereas CX 3 CR1 was detected in CLL and stromal cells. Nurselike cells (NLCs) generated from CLL patient blood co-expressed surface CX 3 CR1 and CX 3 CL1, but did not secrete soluble CX 3 CL1. Only half of NLC cell fractions were attracted in vitro by CX 3 CL1. In conclusion, the CX 3 CR1/CX 3 CL1 system may contribute to interactions between CLL cells and tumor microenvironment by increasing CXCL12-mediated attraction of leukemic cells to NLC and promoting directly adhesion of CLL cells to NLC.

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“…Results concerning p38 involvement differ depending on the cell and the conditions studied (32,34). The MAP kinase p38 may also be involved in adhesion through adhesion molecule up-regulation (35) and cytoskeletal remodeling (36).…”

Section: Discussionmentioning

confidence: 99%

Thrombin Induces Mast Cell Adhesion to Fibronectin: Evidence for Involvement of Protease-Activated Receptor-1

Vliagoftis

2002

The Journal of Immunology

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Thrombin activates mast cells to release inflammatory mediators through a mechanism involving protease-activated receptor-1 (PAR-1). We hypothesized that PAR-1 activation would induce mast cell adhesion to fibronectin (FN). Fluorescent adhesion assay was performed in 96-well plates coated with FN (20 μg/ml). Murine bone marrow cultured mast cells (BMCMC) were used after 3–5 wk of culture (>98% mast cells by flow cytometry for c-Kit expression). Thrombin induced β-hexosaminidase, IL-6, and matrix metalloproteinase-9 release from BMCMC. Thrombin and the PAR-1-activating peptide AparafluoroFRCyclohexylACitY-NH2 (cit) induced BMCMC adhesion to FN in a dose-dependent fashion, while the PAR-1-inactive peptide FSLLRY-NH2 had no effect. Thrombin and cit induced also BMCMC adhesion to laminin. Thrombin-mediated adhesion to FN was inhibited by anti-α5 integrin Ab (51.1 ± 6.7%; n = 5). The combination of anti-α5 and anti-α4 Abs induced higher inhibition (65.7 ± 7.1%; n = 5). Unlike what is known for FcεRI-mediated adhesion, PAR-1-mediated adhesion to FN did not increase mediator release. We then explored the signaling pathways involved in PAR-1-mediated mast cell adhesion. Thrombin and cit induced p44/42 and p38 phosphorylation. Pertussis toxin inhibited PAR-1-mediated BMCMC adhesion by 57.3 ± 7.3% (n = 4), indicating that Gi proteins are involved. Wortmannin and calphostin almost completely inhibited PAR-1-mediated mast cell adhesion, indicating that PI-3 kinase and protein kinase C are involved. Adhesion was partially inhibited by the mitogen-activated protein kinase kinase 1/2 inhibitor U0126 (24.5 ± 3.3%; n = 3) and the p38 inhibitor SB203580 (25.1 ± 10.4%; n = 3). The two inhibitors had additive effects. Therefore, thrombin mediates mast cell adhesion through the activation of Gi proteins, phosphoinositol 3-kinase, protein kinase C, and mitogen-activated protein kinase pathways.

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Signal transduction pathways involved in soluble fractalkine–induced monocytic cell adhesion

Cited by 82 publications

References 55 publications

Soluble Fractalkine Prevents Monocyte Chemoattractant Protein-1-Induced Monocyte Migration via Inhibition of Stress-Activated Protein Kinase 2/p38 and Matrix Metalloproteinase Activities

Soluble Fractalkine Prevents Monocyte Chemoattractant Protein-1-Induced Monocyte Migration via Inhibition of Stress-Activated Protein Kinase 2/p38 and Matrix Metalloproteinase Activities

A novel role of the CX3CR1/CX3CL1 system in the cross-talk between chronic lymphocytic leukemia cells and tumor microenvironment

Thrombin Induces Mast Cell Adhesion to Fibronectin: Evidence for Involvement of Protease-Activated Receptor-1

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