| Project/Area Number |
06454224
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| Research Category |
Grant-in-Aid for General Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Research Field |
Immunology
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| Research Institution | Juntendo University School of Medicine |
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Principal Investigator |
RA Chisei Juntendo University School of Medicine, Assoc.Prof., 医学部, 講師 (60230851)
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| Co-Investigator(Kenkyū-buntansha) |
YANAGIHARA Yukiyoshi National Children's Hospital, Dept.of Allergy, Senior Investigator, 小児医療研究センター, 室長 (00166547)
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| Project Period (FY) |
1994 – 1995
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| Project Status |
Completed (Fiscal Year 1995)
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| Budget Amount *help |
¥6,900,000 (Direct Cost: ¥6,900,000)
Fiscal Year 1995: ¥3,100,000 (Direct Cost: ¥3,100,000)
Fiscal Year 1994: ¥3,800,000 (Direct Cost: ¥3,800,000)
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| Keywords | FcepsilonRI / IgE / Mast cell / Allergy / CD40-L / B cell / IL-4 / B細胞 / インターロイキン4 / IgE産生 / クラススウィッチ |
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| Research Abstract |
A recombinant soluble form of the alpha subunit of the human high-affinity receptor for IgE (rsFcepsilonRIalpha), one of the potent IgE-binding molecules, was tested for its ability to regulate IL-4-induced IgE synthesis by human lymphocytes. Addition of rsFcepsilonRIalpha to cultures induced a does-dependent inhibition of the T cell-dependent and independent synthesis of IgE.The suppression of IgE synthesis was observed at the protein and the mRNA levels, and it was IgE class specific. By flow cytometry, specific binding of rsFcepsilonRIalpha was detected on surface IgE-bearing B cells as well as on U266 cells, and it was completely blocked by preincubation with IgE.rsFcepsilonRIalpha bound to the cell surface IgE could be effectively dissociated not only by a large excess of IgE, but also by an anti-rsFcepsilonRIalpha mAb that competes with IgE for the binding to rsFcepsilonRIalpha. This mAb abolished the rsFcepsilonRIalpha-mediated suppression of IgE synthesis. These data suggest that rsFcepsilonRIalpha may have a function in selectively suppressing IgE synthesis through its interaction with the membrane-bound form of IgE.
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