Interaction of the cell-binding domain of fibronectin with VLA-5 integrin induces monokine production in cultured human monocytes

Takizawa, Takashi; Nishinarita, Susumu; Kitamura, Noboru; Kang, Hoil; Tomita, Yasuyuki; Mitamura, Ko; Yamagami, Keiji; Horie, Takashi

doi:10.1111/j.1365-2249.1995.tb08367.x

Cited by 18 publications

(13 citation statements)

References 58 publications

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“…rsCD40L Induced IL-8 Gene Expression in U937 Cells-The interaction of monocytes with fibronectin leads to inflammatory cytokines expression (30,32), cellular responses that could also be induced in these cells by sCD40L-triggered signaling. To assess the expression of biological mediators, we analyzed IL-8 gene expression in U937 cells stimulated with 100 ng of rsCD40L for 15 min to 4 h. In U937 cells, rsCD40L induced a weak but significant IL-8 gene expression (Fig.…”

Section: Resultsmentioning

confidence: 99%

CD40 Ligand Binds to α5β1 Integrin and Triggers Cell Signaling

Léveillé

Bouillon

Wen

et al. 2007

Journal of Biological Chemistry

110

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It was originally thought that the critical role of the CD40 ligand (CD40L) in normal and inflammatory immune responses was mainly mediated through its interaction with the classic receptor, CD40. However, data from CD40L ؊/؊ and CD40؊/؊ mice suggest that the CD40L-induced inflammatory immune response involves at least one other receptor. This hypothesis is supported by the fact that CD40L stabilizes arterial thrombi through an ␣IIb␤3-dependent mechanism. Here we provide evidence that soluble CD40L (sCD40L) binds to cells of the undifferentiated human monocytic U937 cell line in a CD40-and ␣IIb␤3-independent manner. Binding of sCD40L to U937 cells was inhibited by anti-CD40L monoclonal antibody 5C8, anti-␣5␤1 monoclonal antibody P1D6, and soluble ␣5␤1. The direct binding of sCD40L to purified ␣5␤1 was confirmed in a solid phase binding assay. Binding of sCD40L to ␣5␤1 was modulated by the form of ␣5␤1 expressed on the cell surface as the activation of ␣5␤1 by Mn 2؉ or dithiothreitol resulted in the loss of sCD40L binding. Moreover, sCD40L induced the translocation of ␣5␤1 to the Triton X-100-insoluble fraction of U937 cells, the rapid activation of the MAPK pathways ERK1/2, and interleukin-8 gene expression. The binding of sCD40L to CD40 on BJAB cells, an ␣5␤1-negative B cell line, and the resulting activation of ERK1/2 was not inhibited by soluble ␣5␤1, suggesting that sCD40L can bind concomitantly to both receptors. These results document the existence of novel CD40L-dependent pathways of physiological relevance for cells expressing multiple receptors (CD40, ␣5␤1, and ␣IIb␤3) for CD40L. (2). The expression of CD154 is inducible, and its expression on T cells is triggered primarily by T cell receptor signaling and is regulated by CD28-dependent and independent pathways (3) CD40L is stored in platelets and a subpopulation of T cells and rapidly translocates to the cell membrane following T cell and platelet activation (4, 5). A soluble form of biologically active CD40L trimer (sCD40L) is present in the supernatant of activated T cells (6) and platelets (7) and results from the proteolytic cleavage of the homotrimeric CD40L by a metalloproteinase (7).It was originally thought that CD40L had only one receptor, CD40, which is a type I transmembrane protein that is a member of the TNF receptor superfamily. CD40 is expressed on the surface of many immune and non-immune cells, including B lymphocytes, monocytes/macrophages, and dendritic cells, as well as platelets, epithelial, and endothelial cells (8). Most biological functions of CD40L have been attributed to its direct interaction with CD40. However, studies using CD40L Ϫ/Ϫ and CD40 Ϫ/Ϫ mice have suggested that CD40L may also bind to one or more other receptors (9). In support of this hypothesis, it has been elegantly demonstrated that sCD40L interacts with ␣IIb␤3 (GPIIb/IIIa), an integrin expressed on platelets (10), triggering outside-in signaling and inducing platelet activation and spreading (11). CD40L Ϫ/Ϫ mice exhibit increased bleeding time (12) and reduce...

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Section: Resultsmentioning

confidence: 99%

CD40 Ligand Binds to α5β1 Integrin and Triggers Cell Signaling

Léveillé

Bouillon

Wen

et al. 2007

Journal of Biological Chemistry

110

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“…However, the physiological role of plasma FN is still unknown. We have previously investigated the effect of the soluble form of FN on the production of IL‐1 α , IL‐1 β , IL‐6 and TNF‐ α by cultured human monocytes from normal individuals [10]. FN markedly stimulated the secretion of IL‐1 α , IL‐1 β , IL‐6 and TNF‐ α .…”

Section: Discussionmentioning

confidence: 99%

“…In cultured human monocytes, FN‐coated substrate enhanced both monocyte adhesion and cytokine production. We have previously shown that FN in culture medium activates monocytes through the VLA‐5 receptor, inducing the production of proinflammatory cytokines such as IL‐1, IL‐6 and tumour necrosis factor‐alpha (TNF‐ α ) by these activated cultured human monocytes [10]. Many studies have shown that these same exogenous cytokines are also able to stimulate cultured human monocytes [1–3].…”

Section: Introductionmentioning

confidence: 99%

Cultured human monocytes secrete fibronectin in response to activation by proinflammatory cytokines

Kitamura

Nishinarita

Takizawa

et al. 2000

Clinical and Experimental Immunology

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SUMMARYWe studied the effects of the cytokines IL-1a , IL-6, tumour necrosis factor-alpha (TNF-a ), IL-4, IL-10, IL-13 and transforming growth factor-beta (TGF-b ) on fibronectin (FN) production by cultured-human monocytes. IL-1a , IL-6 and TNF-a all increased FN production, an indicator of monocyte activation. These cytokines increased FN production in a dose-dependent fashion, with a 4-h treatment being sufficient to measure FN production by radioimmunoassay. Conversely, IL-4, IL-10 and IL-13 strongly inhibited cytokine-induced FN production, while TGF-b only partially inhibited FN production. The combination of suboptimal doses of cytokines (IL-1a 1 IL-6, IL-1a 1 TNF-a , IL-6 1 TNF-a ), which could not singly induce substantial amounts of FN, were able to induce FN production by cultured monocytes. Northern blot analysis with a cDNA specific for FN confirmed the expression of FN mRNA in cultured monocytes stimulated with a single cytokine or a combination of cytokines. Our data demonstrate that monocytes may not always require high concentrations of cytokines for activation in vitro, and that the synergistic or additive action of low levels of cytokines on monocyte activation may be sufficient to promote immune or inflammatory reactions. Our data also suggest that certain T cell cytokines may regulate monocyte activation.

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“…Furthermore, exosomes from several independent mouse tumor cell lines trigger MDSC suppressive function in an HSP72/TLR2 dependent manner 63 . At the level of macrophages, exosome-associated fibronectin induces IL-1β production 64 and microvesicles released by late stage mouse melanoma cells were found to exert a dose-dependent suppression of MHC Class II expression in these cells 65 . Recently, it has been proposed that miRNAs from tumor exosomes may also play a role in mobilizing myeloid cells to pre-metastatic niches 3 .…”

Section: How the Tumor Shapes Infiltrating Myeloid Cell Populationsmentioning

confidence: 99%

Instruction of myeloid cells by the tumor microenvironment: Open questions on the dynamics and plasticity of different tumor-associated myeloid cell populations

et al. 2012

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The versatility and plasticity of myeloid cell polarization/differentiation has turned out to be crucial in health and disease, and has become the subject of intense investigation during the last years. On one hand, myeloid cells provide a critical contribution to tissue homeostasis and repair. On the other hand, myeloid cells not only play an important role as first line defense against pathogens but also they are involved in a broad array of inflammation-related diseases such as cancer. Recent studies show that macrophages can exist in different activation states within the same tumor, underlining their plasticity and heterogeneity. In this review, we will discuss recent evidence on how the tumor microenvironment, as it evolves, shapes the recruitment, function, polarization and differentiation of the myeloid cell compartment, leading to the selection of myeloid cells with immunosuppressive and angiogenic functions that facilitate tumor progression and dissemination.

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Interaction of the cell-binding domain of fibronectin with VLA-5 integrin induces monokine production in cultured human monocytes

Cited by 18 publications

References 58 publications

CD40 Ligand Binds to α5β1 Integrin and Triggers Cell Signaling

CD40 Ligand Binds to α5β1 Integrin and Triggers Cell Signaling

Cultured human monocytes secrete fibronectin in response to activation by proinflammatory cytokines

Instruction of myeloid cells by the tumor microenvironment: Open questions on the dynamics and plasticity of different tumor-associated myeloid cell populations

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