The absence of IgE antibody-mediated augmentation of immune responses in CD23-deficient mice.

Fujiwara, Hiroshi; Kikutani, Hitoshi; Suematsu, Sachiko; Naka, Tetsuji; Yoshida, Kanji; Tanaka, Tetsuji; Suemura, Masaki; Matsumoto, Naoyuki; Kojima, Sayuri

doi:10.1073/pnas.91.15.6835

Proc. Natl. Acad. Sci. U.S.A.

1994

DOI: 10.1073/pnas.91.15.6835

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The absence of IgE antibody-mediated augmentation of immune responses in CD23-deficient mice.

Hiroshi Fujiwara

Hitoshi Kikutani²,

Sachiko Suematsu³

et al.

Abstract: The CD23 antigen, a low-affinity receptor for IgE (FceRfl)

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Cited by 147 publications

(123 citation statements)

References 39 publications

(26 reference statements)

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“…The modulatory effect of CD23 on IgE synthesis has been demonstrated in animals treated with CD23 antibody (14) and in those genetically deficient in CD23 (15)(16)(17).…”

mentioning

confidence: 99%

Binding of Anti-CD23 Monoclonal Antibody to the Leucine Zipper Motif of FcεRII/CD23 on B Cell Membrane Promotes Its Proteolytic Cleavage

Munoz

Brignone

Grenier-Brossette³

et al. 1998

Journal of Biological Chemistry

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In the present study we have compared the binding of two monoclonal antibodies to CD23, EBVCS1 and mAb25, which recognize the stalk and the lectin domain, respectively, on the CD23 molecule. At 4°C, EBVCS1 binds to about 10% of the receptors recognized by mAb25 on the B cell surface. At 37°C, whereas mAb25 reaches its maximal binding within a few seconds, EB-VCS1 requires 60 min to bind to the same extent. Stabilization of the oligomeric structure of CD23 with IgE strongly affects in a dose-dependent fashion the number of binding sites seen by EBVCS1 but not the t 1/2 to reach them, suggesting that EBVCS1 binds to the coiled coil region through an allosteric mechanism. EBVCS1 rapidly down-modulates the membrane CD23 expression with a coincident increase of CD23-soluble fragments in the culture medium, an effect that is inhibited by IgE. In contrast, mAb25, as well as IgE, protects CD23 from proteolytic cleavage and stimulates its endocytosis. These results suggest that EBVCS1 unravels the coiled coil structure of CD23, rendering it more susceptible to proteolytic attack. This supports the oligomeric model proposed previously (Gould, H., Sutton, B., Edmeades, R., and Beavil, A. (1991) Monogr. Allergy 29, 28 -49). The biological significance of these observations is discussed.

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“…The modulatory effect of CD23 on IgE synthesis has been demonstrated in animals treated with CD23 antibody (14) and in those genetically deficient in CD23 (15)(16)(17).…”

mentioning

confidence: 99%

Binding of Anti-CD23 Monoclonal Antibody to the Leucine Zipper Motif of FcεRII/CD23 on B Cell Membrane Promotes Its Proteolytic Cleavage

Munoz

Brignone

Grenier-Brossette³

et al. 1998

Journal of Biological Chemistry

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“…In both humans and mice, CD23-bound IgE is thought to enhance B cell Ag presentation to T cells when CD23-bound IgE is cross-linked by Ag and endocytosed (8,9). The significance of this pathway is demonstrated by the ability of CD23-activated BCRm + B cells to present Ag to naive T cells (10).…”

mentioning

confidence: 99%

CD23-Bound IgE Augments and Dominates Recall Responses through Human Naive B Cells

Griffith

Liang

Onguru

et al. 2011

The Journal of Immunology

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Human peripheral blood BCRμ+ B cells express high levels of CD23 and circulate preloaded with IgE. The Ag specificity of CD23-bound IgE presumably differs from the BCR and likely reflects the Ag-specific mix of free serum IgE. CD23-bound IgE is thought to enhance B cell Ag presentation to T cells raising the question of how a B cell might respond when presented with a broad mix of Ags and CD23-bound IgE specificities. We recently reported that an increase in CD23+ B cells is associated with the development of resistance to schistosomiasis, highlighting the potential importance of CD23-bound IgE in mediating immunity. We sought to determine the relationship between BCR and CD23-bound IgE-mediated B cell activation in the context of schistosomiasis. We found that crude schistosome Ags downregulate basal B cell activation levels in individuals hyperexposed to infectious worms. Schistosome-specific IgE from resistant, occupationally exposed Kenyans recovered responses of B cells to schistosome Ag. Furthermore, cross-linking of CD23 overrode intracellular signals mediated via the BCR, illustrating its critical and dominating role in B cell activation. These results suggest that CD23-bound IgE augments and dominates recall responses through naive B cells.

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“…CD23 is constitutively and inducibly expressed in variety of cell types, including B cells, eosinophils, monocytes, and Langerhans cells (16,18,25,26). More interestingly, CD23 has various functions, such as mediating B cell growth, enhancing IgE-mediated Ag presentation (27,28), and regulating IgE homeostasis (29)(30)(31)(32).…”

mentioning

confidence: 99%

CD23-Dependent Transcytosis of IgE and Immune Complex across the Polarized Human Respiratory Epithelial Cells

Palaniyandi

Tomei

et al. 2011

The Journal of Immunology

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IgE-mediated allergic inflammation occurs when allergens cross-link IgE on the surface of immune cells, thereby triggering the release of inflammatory mediators as well as enhancing Ag presentations. IgE is frequently present in airway secretions, and its level can be enhanced in human patients with allergic rhinitis and bronchial asthma. However, it remains completely unknown how IgE appears in the airway secretions. In this study, we show that CD23 (FcεRII) is constitutively expressed in established or primary human airway epithelial cells, and its expression is significantly upregulated when airway epithelial cells were subjected to IL-4 stimulation. In a transcytosis assay, human IgE or IgE-derived immune complex (IC) was transported across a polarized Calu-3 monolayer. Exposure of the Calu-3 monolayer to IL-4 stimulation also enhanced the transcytosis of either human IgE or the IC. A CD23-specific Ab or soluble CD23 significantly reduced the efficiency of IgE or IC transcytosis, suggesting a specific receptor-mediated transport by CD23. Transcytosis of both IgE and the IC was further verified in primary human airway epithelial cell monolayers. Furthermore, the transcytosed Ag–IgE complexes were competent in inducing degranulation of the cultured human mast cells. Because airway epithelial cells are the first cell layer to come into contact with inhaled allergens, our study implies CD23-mediated IgE transcytosis in human airway epithelial cells may play a critical role in initiating and contributing to the perpetuation of airway allergic inflammation.

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The absence of IgE antibody-mediated augmentation of immune responses in CD23-deficient mice.

Abstract: The CD23 antigen, a low-affinity receptor for IgE (FceRfl)

Cited by 147 publications

References 39 publications

Binding of Anti-CD23 Monoclonal Antibody to the Leucine Zipper Motif of FcεRII/CD23 on B Cell Membrane Promotes Its Proteolytic Cleavage

Binding of Anti-CD23 Monoclonal Antibody to the Leucine Zipper Motif of FcεRII/CD23 on B Cell Membrane Promotes Its Proteolytic Cleavage

CD23-Bound IgE Augments and Dominates Recall Responses through Human Naive B Cells

CD23-Dependent Transcytosis of IgE and Immune Complex across the Polarized Human Respiratory Epithelial Cells

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