Signal Transduction by IgG Receptors Induces Calcium Mobilization, but not Histamine Release, in the Human Basophilic Cell Line KU812F

Kawata, Noriko; Takata, Minoru; Suwaki, Toshimitsu; Tanimoto, Yasushi; Soda, Ryo; Takahashi, Kiyoshi; Kimura, Ikuo

doi:10.1159/000237228

Cited by 10 publications

(8 citation statements)

References 23 publications

(36 reference statements)

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“…We have reported previously that both KU812F cells and human peripheral blood basophils induce intracellular signaling events, such as calcium mobilization, following FcγRII cross‐linking 6 . The data presented here clearly show that tyrosine phosphorylation is necessary for the signaling pathway via FcγRII and tyrosine phosphorylation of Lyn, Syk and PLC‐γ1, at least, is actively involved in this signal transduction.…”

Section: Discussionsupporting

confidence: 59%

“…Intracellular calcium measurements were performed according to the method described previously 6 . Briefly, KU812F cells were resuspended in Hanks’ balanced salt solution (HBSS), without calcium and magnesium, containing 0.01 mol/L EDTA (Sigma, St Louis, MO, USA) and 0.1% bovine serum albumin (BSA; Sigma).…”

Section: Methodsmentioning

confidence: 99%

“…The IgG Fc receptors (FcγR) are broadly expressed on hematopoietic cells and are classified into three major classes: I, II and III 2−4 . We have reported previously that a low‐affinity receptor, namely FcγRII, is expressed on human basophils and cross‐linking of FcγRII induces intracellular calcium mobilization 5,6 .…”

Section: Introductionmentioning

confidence: 99%

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Association of IgG Fc receptor II with tyrosine kinases in the human basophilic leukemia cell line KU812F

Fujii

Tanimoto

Takata

et al. 2003

Allergology International

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A BSTRACTBackground: We previously reported that crosslinking of IgG Fc receptor II (Fc γ RII) induces intracellular calcium mobilization, but not histamine release in human basophils. To clarify functional activities of Fc γ RII on human basophils, we analyzed the Fc γ RIImediated signaling events in the human basophilic leukemia cell line KU812F. Methods: Flow cytometric methods were used to investigate the effect on intracellular calcium mobilization of cross-linking of Fc γ RII. KU812F cells were preincubated with anti-Fc γ RII monoclonal antibody (IV.3). After the addition of various concentrations of the tyrosine kinase inhibitor genistein or buffer alone, cells were stimulated with goat antimouse IgG F(ab ′ ) 2 (GAM) and analyzed with the flow cytometer. Next, in order to test the signaling events after cross-linking of Fc γ RII, we examined tyrosine kinase activity. The timecourse of tyrosine phosphorylation after cross-linking of Fc γ RII and the effect of genistein on this tyrosine phosphorylation were tested by immunoblotting. Immunoprecipitation was also performed to identify the type of tyrosine kinase associated with signal transduction of Fc γ RII. Results: The tyrosine kinase inhibitor genistein inhibited intracellular calcium mobilization caused by cross-linking of Fc γ RII in a dose-dependent manner. Rapid tyrosine phosphorylation after Fc γ RII cross-linking was shown by immunoblot analysis and this phosphorylation was inhibited by genistein. Furthermore, tyrosine phosphorylation of Lyn and Syk was observed upon crosslinking of Fc γ RII. Conclusions: Tyrosine phosphorylation is necessary for the signaling pathway through Fc γ RII and tyrosine phosphorylation of Lyn and Syk, at least, is actively involved in this signal transduction.

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Section: Discussionsupporting

confidence: 59%

Section: Methodsmentioning

confidence: 99%

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Association of IgG Fc receptor II with tyrosine kinases in the human basophilic leukemia cell line KU812F

Fujii

Tanimoto

Takata

et al. 2003

Allergology International

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“…Preparation of aggregated IgG. Aggregated IgG was prepared as described previously (33). Briefly, aggregated IgG was prepared by heating human IgG (Jackson Immuno-Research) at 63°C for 1 hour.…”

Section: Methodsmentioning

confidence: 99%

Activation of human synovial mast cells from rheumatoid arthritis or osteoarthritis patients in response to aggregated IgG through Fcγ receptor I and Fcγ receptor II

Lee¹,

Kashiwakura²,

Matsuda³

et al. 2012

Arthritis & Rheumatism

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Methods. Synovial tissue specimens were obtained from patients with RA or patients with osteoarthritis (OA) who were undergoing joint replacement surgery, and synovial MCs were enzymatically dispersed. Cultured synovium-derived MCs were generated by culturing synovial cells with stem cell factor, and receptor expression was analyzed using fluorescenceactivated cell sorting. Mediators released from MCs were measured using enzyme immunoassays or enzymelinked immunosorbent assays. Results. Primary synovial MCs and cultured synovium-derived

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“…RBL-2H3 cells [14]or human basophils [15]did not bind monomeric IgG but bound aggregated IgG, indicating they had only low-affinity IgG receptors. [Ca 2+ ] i elevation and actin polymerization in a human basophilic cell line KU812F were induced by aggregated IgG stimulation [16], which is thought to be mediated via FcγRIIA.…”

Section: Introductionmentioning

confidence: 99%

IgG-Mediated Signal Transduction in Canine Mastocytoma-Derived Cells

Sato

Teshima²,

Nakamura³

et al. 2002

Int Arch Allergy Immunol

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Background: We have reported canine cutaneous mastocytoma-derived cells named CM-MC sensitized with monomeric IgG released histamine upon anti-IgG stimulation. However, IgG or IgE-mediated signal transduction in the cells remains to be examined. Methods: Monomeric IgG-binding to cells was measured by flow cytometry using FITC-anti-IgG. IgG-mediated protein tyrosine phosphorylation was studied by Western blotting using anti-phosphotyrosine antibody. We monitored the intracellular Ca²⁺ concentration ([Ca²⁺]_i) when IgG-primed cells were activated with anti-canine IgG. Release of Ca²⁺ from intracellular stores was analyzed with thapsigargin in the absence of extracellular Ca²⁺. The Ca²⁺ entry via store-operated Ca²⁺ channel from the external environment was characterized using Ba²⁺, Ni²⁺ and EGTA. Cells sensitized with canine serum abundant in IgG and IgE or heat-inactivated serum were activated by anti-canine IgG or anti-canine IgE. The effect of extracellular Ca²⁺ and reaction time on IgG-mediated histamine release was examined. Staurosporine and ER-27319 were used to clarify the IgG-mediated protein tyrosine phosphorylation. Results: Abundant IgG-binding sites on the cell were detected by FACS analysis. Anti-IgG induced rapid protein tyrosine phosphorylation and [Ca²⁺]_i elevation. When extracellular Ca²⁺ was excluded by EGTA, a mild and transient increase in [Ca²⁺]_i was observed, indicating the release of Ca²⁺ from anti-IgG-sensitive intracellular Ca²⁺ stores. The constant Ba²⁺ entry from external environment proved the Ca²⁺ influx occurred mainly via a store-operated Ca²⁺ channel which was inhibited by Ni²⁺ and EGTA. Canine serum-sensitized cells showed a rapid and sustained increase in [Ca²⁺]_i upon both anti-IgG and anti-IgE stimulation. The [Ca²⁺]_i elevation induced by anti-IgE was decreased in the cells sensitized with heat-inactivated serum. Histamine release from CM-MCs was absolutely dependent on extracellular Ca²⁺, and reached equilibrium within 5 min. Staurosporine inhibited the tyrosine phosphorylation of 38-, 65-, 70-, 80-kD proteins. ER-27319 inhibited the tyrosine phosphorylation of 38- and 70-kD proteins. Staurosporine also inhibited IgG-mediated [Ca²⁺]_i elevation and histamine release in a dose-dependent manner. Conclusions: Canine cutaneous mastocytoma-derived (CM-MC) cells were activated by both IgG- and IgE-mediated mechanisms. IgG-mediated protein tyrosine phosphorylation and Ca²⁺ influx were similar to those mediated by IgE. CM-MC cells are useful for the study of allergic inflammation caused by IgG-dependent mechanisms.

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Signal Transduction by IgG Receptors Induces Calcium Mobilization, but not Histamine Release, in the Human Basophilic Cell Line KU812F

Cited by 10 publications

References 23 publications

Association of IgG Fc receptor II with tyrosine kinases in the human basophilic leukemia cell line KU812F

Association of IgG Fc receptor II with tyrosine kinases in the human basophilic leukemia cell line KU812F

Activation of human synovial mast cells from rheumatoid arthritis or osteoarthritis patients in response to aggregated IgG through Fcγ receptor I and Fcγ receptor II

IgG-Mediated Signal Transduction in Canine Mastocytoma-Derived Cells

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