Role of ICRAC in the Regulation of Secretion

Mathes, Chris; Mendez, Francisco; Fleig, Andrea; Penner, Reinhold

doi:10.1007/978-1-4612-2154-8_27

Cited by 2 publications

(1 citation statement)

References 39 publications

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“…Stimulation of Fc⑀RI is known to open store-operated channels for Ca 2ϩ (23). Two manipulations that should block such an influx of Ca 2ϩ , adding EGTA to the medium or depleting the medium of Ca 2ϩ , largely inhibited the transcription of MCP-1.…”

Section: Discussionmentioning

confidence: 99%

Synthesis and Secretion of Monocyte Chemotactic Protein-1 Stimulated by the High Affinity Receptor for IgE

Eglite

Morin

Metzger

2003

The Journal of Immunology

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In prior studies aggregation of the high affinity receptors for IgE, FcεRI, on a rat mast cell line, RBL-2H3, stimulated transcription of the gene for monocyte chemotactic protein-1 (MCP-1) and secretion of the protein. Unexpectedly, those delayed events appeared much less constrained by kinetic proofreading than had been documented for other receptor-initiated responses. The results of the present experiments are consistent with the proposal that the biosynthesis and secretion of MCP-1 result from a soluble messenger formed in the reaction cascades initiated by the receptor, and that Ca2+ could serve as that messenger. Interestingly, whereas receptor-mediated signals were required for transcription of the gene for MCP-1 and secretion of the chemokine, such signals were not required for the intervening step of translation of its mRNA.

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Section: Discussionmentioning

confidence: 99%

Synthesis and Secretion of Monocyte Chemotactic Protein-1 Stimulated by the High Affinity Receptor for IgE

Eglite

Morin

Metzger

2003

The Journal of Immunology

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Regulation of mediator secretion in human basophils by p38 mitogen-activated protein kinase: phosphorylation is sensitive to the effects of phosphatidylinositol 3-kinase inhibitors and calcium mobilization

Gibbs

Plath

Wolff

et al. 2002

Journal of Leukocyte Biology

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Although human basophils modulate allergic diseases by secreting histamine, leukotriene C4, interleukin (IL)-4, and IL-13, the intermediary signals controlling the release of these mediators are poorly understood. Here, we show that p38 mitogen-activated protein kinase (MAPK) crucially affects basophil activation following stimulation with various secretagogues. Phosphorylation of p38 MAPK occurred within 5 min following anti-immunoglobulin (Ig)E stimulation, but was more rapidly activated in basophils stimulated with formyl-Met-Leu-Phe or A23187. Additionally, activation of p38 MAPK to the above stimuli was dependent on extracellular influx and intracellular mobilization of calcium. SB 203580, a specific p38 MAPK inhibitor, blocked anti-IgE-induced secretion of all basophil mediators and reduced not only p38 MAPK, but also extracellular signal-regulated kinases 1 and 2 activity, whereas the MAPK antagonist, PD 098059, did not affect p38 MAPK. IgE-dependent activation of p38 MAPK and MKK3/6 was affected by LY 294002 and wortmannin, suggesting that these kinases are targets for phosphatidylinositol 3 kinase (PI 3-K). We conclude that p38 MAPK is a pivotal regulator of basophil function downstream of PI 3-K activation and calcium mobilization.

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Role of ICRAC in the Regulation of Secretion

Cited by 2 publications

References 39 publications

Synthesis and Secretion of Monocyte Chemotactic Protein-1 Stimulated by the High Affinity Receptor for IgE

Synthesis and Secretion of Monocyte Chemotactic Protein-1 Stimulated by the High Affinity Receptor for IgE

Regulation of mediator secretion in human basophils by p38 mitogen-activated protein kinase: phosphorylation is sensitive to the effects of phosphatidylinositol 3-kinase inhibitors and calcium mobilization

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