The production of tumor necrosis factor-.ALPHA. by rat basophilic leukemia cells with triggering IgE receptor.

Ohno, Isao; Tanno, Yasuo; Yamauchi, Kohei; Ida, Shiroh; Takishima, Tamotsu

doi:10.1620/tjem.156.209

Cited by 12 publications

(12 citation statements)

References 4 publications

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“…As can be seen in Fig. 7, TNF-␣ release started as early as 4 h following the incubation with activated T cell membranes, reaching a maximum at 6 h. These TNF-␣ kinetics are similar to those reported for IgEmediated mast cell activation (34). In contrast, the release of active MMP-9 started only after 6 h of incubation, with a prolonged and steady rise to a peak at 22 h of incubation (Fig.…”

Section: Kinetics Of Mmp-9 and Tnf-␣ Releasesupporting

confidence: 83%

Human Mast Cells Release Metalloproteinase-9 on Contact with Activated T Cells: Juxtacrine Regulation by TNF-α

Baram

Vaday

Salamon

et al. 2001

The Journal of Immunology

214

177

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Mast cells, essential effector cells in allergic inflammation, have been found to be activated in T cell-mediated inflammatory processes in accordance with their residence in close physical proximity to T cells. We have recently reported that mast cells release granule-associated mediators and TNF-α upon direct contact with activated T cells. This data suggested an unrecognized activation pathway, where mast cells may be activated during T cell-mediated inflammation. Herein, we show that this cell-cell contact results in the release of matrix metalloproteinase (MMP)-9 and the MMP inhibitor tissue inhibitor of metalloproteinase 1 from HMC-1 human mast cells or from mature peripheral blood-derived human mast cells. The expression and release of these mediators, as well as of β-hexosaminidase and several cytokines, were also induced when mast cells were incubated with cell membranes isolated from activated, but not resting, T cells. Subcellular fractionation revealed that the mature form of MMP-9 cofractionated with histamine and tryptase, indicating its localization within the secretory granules. MMP-9 release was first detected at 6 h and peaked at 22 h of incubation with activated T cell membranes, while TNF-α release peaked after only 6 h. Anti-TNF-α mAb inhibited the T cell membrane-induced MMP-9 release, indicating a possible autocrine regulation of MMP release by mast cell TNF-α. This cascade of events, whereby mast cells are activated by T cells to release cytokines and MMP-9, which are known to be essential for leukocyte extravasation and recruitment to affected sites, points to an important immunoregulatory function of mast cells within the context of T cell-mediated inflammatory processes.

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Section: Kinetics Of Mmp-9 and Tnf-␣ Releasesupporting

confidence: 83%

Human Mast Cells Release Metalloproteinase-9 on Contact with Activated T Cells: Juxtacrine Regulation by TNF-α

Baram

Vaday

Salamon

et al. 2001

The Journal of Immunology

214

177

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“…However, any given mast cell type does not necessarily express all of these cytokines (11). In RBL cells, FcεRI activation has been shown to the induce rapid expression of two immediate-early genes, c-fos and c-jun, and expression and secretion of TNF-␣ (4,39,43). The products of the c-fos and c-jun genes are major components of the transcription factor AP-1 and are likely to play a role in the regulation of downstream genes such as cytokines.…”

Section: Introduction Of a Chimeric Transmembrane Syk Protein Into Rbmentioning

confidence: 99%

Clustering of Syk Is Sufficient To Induce Tyrosine Phosphorylation and Release of Allergic Mediators from Rat Basophilic Leukemia Cells

Rivera

Brugge

1995

Molecular and Cellular Biology

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In mast cells, antigen-mediated aggregation of the high-affinity receptor for immunoglobulin E, FcRI, stimulates tyrosine phosphorylation and activation of multiple signaling pathways leading to the release of several classes of mediators of the allergic response. Early events induced upon cross-linking of FcRI include tyrosine phosphorylation of FcRI subunits and activation of the tyrosine kinase p72 syk (Syk), which binds to tyrosine-phosphorylated FcRI. Clustering of Syk, as a result of its interaction with aggregated FcRI, may play a role in activating one or more of the signaling pathways leading to mediator release. To test this possibility, Syk was introduced into a model mast cell line (rat basophilic leukemia cells) as part of a chimeric transmembrane protein containing the extracellular and transmembrane domains of CD16 and CD7, respectively. Clustering of the Syk chimera, using antibodies against CD16, was found to be sufficient to stimulate early and late events normally induced by clustering of FcRI. Specifically, aggregation of Syk induced degranulation, leukotriene synthesis, and expression of cytokine genes. Induction of mediator release was dependent on the kinase activity of Syk. Consistent with this finding, clustering of Syk also induced the tyrosine phosphorylation of a profile of proteins, including phospholipase C-␥1 and mitogen-activated protein kinase, similar to that induced upon clustering of FcRI. These results strongly suggest that Syk is an early and critical mediator of multiple signaling pathways that emanate from the FcRI receptor and give rise to the allergic response.Antigen-induced aggregation of the high-affinity receptor for immunoglobulin E (IgE), FcεRI, induces mast cells to release several classes of mediators that activate both early and late phases of the allergic response (37, 49). Mediators released upon mast cell activation fall into three classes which are represented by (i) histamines, which are preformed and secreted from granules within minutes of activation; (ii) leukotrienes and prostaglandins, which are newly generated from lipid precursors and are also rapidly released upon activation; and (iii) cytokines, which are newly expressed and released within the first few hours after activation.Activation of the multiple signaling pathways that lead to the synthesis and release of these diverse mediators is preceded by aggregation-induced tyrosine phosphorylation of two subunits of FcεRI (33,40). Subsequent events include (i) the increased tyrosine phosphorylation and activation of a number of signaling molecules, including Syk (7, 23), phospholipase C-␥1 (PLC-␥1) (2,19,41), Vav (36), and mitogen-activated protein (MAP) kinase (46); (ii) activation of protein kinase C (55, 56) and phospholipase A 2 (20); and (iii) elevation of intracellular calcium levels (6). Tyrosine phosphorylation appears to play a critical role in propagating the signal leading to these events since mediator release is blocked by tyrosine kinase inhibitors (27,57).FcεRI is a multisubunit recept...

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“…Similarly, oxygen metabolites, which are released from IgE-activated eosinophils, macrophages, and monocytes, can induce mast-cell secretion through an IgE-independent stimulus (22,23). Furthermore, the chemotactic effect of TNF-a on the recruitment of eosinophils, monocytes, and macrophages is well known, and infiltration of lung tissue by these cells has been observed in asthmatic patients in the late phase of the allergic response (24). The consequences of IgE-mediated target-cell activation are summarized in Fig.…”

mentioning

confidence: 99%

Peptide blocking of IgE/receptor interaction: possibilities and pitfalls

Helm

Spivey

Padlan

1997

Allergy

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The production of tumor necrosis factor-.ALPHA. by rat basophilic leukemia cells with triggering IgE receptor.

Cited by 12 publications

References 4 publications

Human Mast Cells Release Metalloproteinase-9 on Contact with Activated T Cells: Juxtacrine Regulation by TNF-α

Human Mast Cells Release Metalloproteinase-9 on Contact with Activated T Cells: Juxtacrine Regulation by TNF-α

Clustering of Syk Is Sufficient To Induce Tyrosine Phosphorylation and Release of Allergic Mediators from Rat Basophilic Leukemia Cells

Peptide blocking of IgE/receptor interaction: possibilities and pitfalls

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