Immunoglobulin E Receptors

Gould, Hannah; Sutton, Brian J.; Beavil, Andrew J.; Edmeades, Rebecca L.; Martin, David

doi:10.1111/j.1365-2222.1991.tb01718.x

Cited by 7 publications

(4 citation statements)

References 24 publications

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“…These observations prompted Gould and colleagues (6,34) to suggest an allosteric mechanism by which binding of IgE or mAb to the lectin domain of the Fc⑀RII would stabilize the coiled coil stalk region and would protect it against proteolysis, whereas other ligands would exert the opposite effect.…”

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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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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“…1) is composed of 4 polypeptides: an α-chain, a β-chain, and a pair of γ chains that form an integral transmembrane complex. Although it is the α-chain that binds IgE, the β-andγ-chains are required for insertion of the α-chain into the membrane and for signal transduction [9,10]. The receptor *Address correspondence to this author at the Immunology Research Institute of New England, 358 Elm Street, Gardner, MA 01440, USA; E-mail: Ldubuske@aol.com is primarily expressed on mast cell and basophil surfaces [11]; it is also found on antigen-presenting cells such as cutaneous Langerhans cells [12], dendritic cells [13], and monocytes [14], as well as on eosinophils [15,16], and platelets [17].…”

Section: Ige Receptorsmentioning

confidence: 99%

IgE, Allergic Diseases, and Omalizumab

DuBuske¹

2006

CPD

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Immunoglobulin E (IgE) plays a central role in the development of allergic diseases. In sensitized individuals, IgE antibodies bind to receptors on mast cell and basophil surfaces, releasing preformed and newly generated mediators that initiate an immunologic cascade and inflammatory symptoms. Omalizumab (Xolair) is a humanized monoclonal antibody designed to bind specifically to IgE. It was approved by the United States Food and Drug Administration in 2003 for the treatment of patients with moderate-to-severe persistent asthma that is inadequately controlled with inhaled corticosteroids (ICS) and who have a positive skin test or in vitro reactivity to a perennial aeroallergen. In clinical trials in such patients, omalizumab reduced the incidence of asthma exacerbations, severe exacerbations, the use of rescue medication, and improved both symptoms and quality of life (QOL).

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“…Epidemiologic studies link total serum IgE concentrations with the incidence of asthma symptoms and bronchial hyperresponsiveness (1,2). An important characteristic of IgE is its ability to bind to mast cells and basophils with high affinity through its Fc portion to the IgE receptor (Fc ε RI) (3,4). Fc ε RI comprises an ␣ chain, a ␤ chain, and two disulphidelinked ␥ chains.…”

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confidence: 99%

“…Fc ε RI comprises an ␣ chain, a ␤ chain, and two disulphidelinked ␥ chains. Alpha chain is involved in IgE binding and re-ceptor internalization, resulting in the allergic mediator release process, whereas ␤ chain plays a role in signal transduction (3,4). Cross-linking of the Fc ε RI, even in the absence of IgE, results in mast-cell triggering (5).…”

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confidence: 99%

Increased Expression of High Affinity IgE (Fc ɛ RI) Receptor- α Chain mRNA and Protein-bearing Eosinophils in Human Allergen-induced Atopic Asthma

Rajakulasingam

Till

Ying

et al. 1998

Am J Respir Crit Care Med

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FcepsilonRI receptors play an important role in allergen-induced mediator release and antigen presentation by mast cells, basophils, and monocyte/macrophages in atopic disorders. The expression of FcepsilonRI by tissue eosinophils in atopic asthma after allergen challenge has not been established. For this reason we attempted to identify mRNA and protein product + FcepsilonRIalpha eosinophils in cytospins made from bronchoalveolar lavage (BAL) from atopic asthmatics (n = 9) and nonatopic normal subjects (n = 4) 24 h after segmental challenge with allergen or diluent. Messenger RNA for FcepsilonRIalpha was determined using in situ hybridization and FcepsilonRIalpha protein expression by immunocytochemistry using a mouse monoclonal antibody 22E7. Colocalization of FcepsilonRIalpha receptors to eosinophils was performed using chromotrope 2R. When compared with a control challenge, segmental challenge with Dermatophagoides pteronyssinus induced significant BAL eosinophilia (p = 0.007). The total number of BAL FcepsilonRIalpha mRNA and protein-positive cells also increased in asthmatics, median values 2 (0.7-7.2) and 11.5 (0.6-65.0) x 10(6) cells (p = 0.02) and 0 (0-0.3 x 10(6)) and 3.1 x 10(6) (0.45 - 162.5 x 10(6)) cells (p = 0.007), respectively, for mRNA and protein. Net increases in FcepsilonRIalpha+ cells correlated with the net increases in BAL eosinophils (r = 0.98, p = 0.0001 for mRNA and r = 0.72, p = 0.02 for protein). Colocalization studies with chromotrope 2R revealed that only 4% of FcepsilonRIalpha+ cells were eosinophils after control challenge and, in contrast, 85 to 95% of FcepsilonRIalpha+ cells were eosinophils after allergen. There were no differences in the numbers of FcepsilonRIalpha+ cells or eosinophils in normal control subjects. Our results demonstrated that local endobronchial allergen provocation in atopic asthmatics results in increased synthesis and expression of FcepsilonRIalpha predominantly on BAL eosinophils.

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Immunoglobulin E Receptors

Cited by 7 publications

References 24 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

IgE, Allergic Diseases, and Omalizumab

Increased Expression of High Affinity IgE (Fc ɛ RI) Receptor- α Chain mRNA and Protein-bearing Eosinophils in Human Allergen-induced Atopic Asthma

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