scholarly journals Lymphocytes with Immunoglobulin E Fc Receptors in Patients with Atopic Disorders

1979 ◽  
Vol 64 (3) ◽  
pp. 714-720 ◽  
Author(s):  
H. L. Spiegelberg ◽  
R. D. O'Connor ◽  
R. A. Simon ◽  
D. A. Mathison
Keyword(s):  
Immunoglobulin E ◽  
Fc Receptors

scholarly journals Lateral electromigration and diffusion of Fc epsilon receptors on rat basophilic leukemia cells: effects of IgE binding.

1984 ◽  
Vol 99 (3) ◽  
pp. 778-787 ◽  
Author(s):  
M A McCloskey ◽  
Z Y Liu ◽  
M M Poo
Keyword(s):  
Cell Surface ◽  
Immunoglobulin E ◽  
Fc Receptors ◽  
Lateral Diffusion ◽  
Surface Proteins ◽  
Ige Binding ◽  
The Difference ◽  
D Values ◽  
Rbl Cells ◽  
Basophilic Leukemia

We have used in situ electromigration and post-field relaxation (Poo, M.-m., 1981, Annu. Rev. Biophys. Bioeng., 10:245-276) to assess the effect of immunoglobulin E (IgE) binding on the lateral mobility of IgE-Fc receptors in the plasmalemma of rat basophilic leukemia (RBL) cells. Bound IgE sharply increased the receptor's electrokinetic mobility, whereas removal of cell surface neuraminic acids cut it to near zero. In contrast, we found only a small difference between the lateral diffusion coefficients (D) of vacant and IgE-occupied Fc receptors (D: 4 vs. 3 X 10(-10) cm2/s at 24 degrees C). This is true for monomeric rat IgE; with mouse IgE, the difference in apparent diffusion rates was slightly greater (D: 4.5 vs. 2.3 X 10(-10) cm2/s at 24 degrees C). This range of D values is close to that found in previous photobleaching studies of the IgE-Fc epsilon receptor complex in RBL cells and rat mast cells. Moreover, enzymatic depletion of cell coat components did not measurably alter the diffusion rate of IgE-occupied receptors. Thus, binding of fluorescent macromolecular probes to cell surface proteins need not severely impede lateral diffusion of the probed species. If the glycocalyx of RBL cells does limit lateral diffusion of the Fc epsilon receptor, it must act primarily on the receptor itself, rather than on receptor-bound IgE.

Immunoglobulin E (IGE)-Binding FC Receptors

2016 ◽  
Author(s):  
Douglas M. Templeton ◽  
Michael Schwenk ◽  
Reinhild Klein ◽  
John H. Duffus
Keyword(s):  
Immunoglobulin E ◽  
Fc Receptors ◽  
Ige Binding

scholarly journals IgE Antibodies: From Structure to Function and Clinical Translation

Antibodies ◽  
2019 ◽  
Vol 8 (1) ◽  
pp. 19 ◽  
Author(s):  
Brian Sutton ◽  
Anna Davies ◽  
Heather Bax ◽  
Sophia Karagiannis
Keyword(s):  
Conformational Changes ◽  
Immunoglobulin E ◽  
Fc Receptors ◽  
Solid Tumours ◽  
Clinical Translation ◽  
Therapeutic Modality ◽  
Ige Antibodies ◽  
Effector Functions ◽  
Anti Cancer

Immunoglobulin E (IgE) antibodies are well known for their role in mediating allergic reactions, and their powerful effector functions activated through binding to Fc receptors FcεRI and FcεRII/CD23. Structural studies of IgE-Fc alone, and when bound to these receptors, surprisingly revealed not only an acutely bent Fc conformation, but also subtle allosteric communication between the two distant receptor-binding sites. The ability of IgE-Fc to undergo more extreme conformational changes emerged from structures of complexes with anti-IgE antibodies, including omalizumab, in clinical use for allergic disease; flexibility is clearly critical for IgE function, but may also be exploited by allosteric interference to inhibit IgE activity for therapeutic benefit. In contrast, the power of IgE may be harnessed to target cancer. Efforts to improve the effector functions of therapeutic antibodies for cancer have almost exclusively focussed on IgG1 and IgG4 subclasses, but IgE offers an extremely high affinity for FcεRI receptors on immune effector cells known to infiltrate solid tumours. Furthermore, while tumour-resident inhibitory Fc receptors can modulate the effector functions of IgG antibodies, no inhibitory IgE Fc receptors are known to exist. The development of tumour antigen-specific IgE antibodies may therefore provide an improved immune functional profile and enhanced anti-cancer efficacy. We describe proof-of-concept studies of IgE immunotherapies against solid tumours, including a range of in vitro and in vivo evaluations of efficacy and mechanisms of action, as well as ex vivo and in vivo safety studies. The first anti-cancer IgE antibody, MOv18, the clinical translation of which we discuss herein, has now reached clinical testing, offering great potential to direct this novel therapeutic modality against many other tumour-specific antigens. This review highlights how our understanding of IgE structure and function underpins these exciting clinical developments.

Expression and Function of Fc Receptors in the Thymus

1995 ◽  
Vol 15 (3-4) ◽  
pp. 215-233 ◽  
Author(s):  
Georges Leclercq ◽  
Jean Plum
Keyword(s):  
Fc Receptors ◽  
And Function

Serum immunoglobulin E reactivity to cross-reacting panallergen components in north-eastern Poland patients pollen sensitized

2020 ◽  
Vol 41 (3) ◽  
pp. 183-191
Author(s):  
Krzysztof Kowal ◽  
Agnieszka Pampuch ◽  
Ewa Sacharzewska ◽  
Ewa Swiebocka ◽  
Zenon Siergiejko ◽  
...  
Keyword(s):  
Allergic Rhinitis ◽  
Allergen Immunotherapy ◽  
Immunoglobulin E ◽  
Pollen Allergy ◽  
Serum Ige ◽  
Ige Reactivity ◽  
Allergen Components ◽  
North Eastern ◽  
Allergen Sources ◽  
Seasonal Pollen

Background: The presence of immunoglobulin E (IgE), which cross-reacts with allergen components, such as profilins, polcalcins, and cross-reacting carbohydrate determinants (CCD), creates a problem when selecting patients for allergen immunotherapy by using conventional methods. The aim of this study was to evaluate the prevalence of sensitization to profilins, polcalcins, and CCDs in patients with seasonal pollen allergic rhinitis. Methods: The study was performed on a group of 112 patients with seasonal pollen allergic rhinitis, ages 14 to 55 years, with sensitization to at least one seasonal allergen (IgE > 0.7 kUA/L). The presence of IgE sensitization to recombinant (r) Bet v 2, rPhl p 12, rBet v 4, rPhl p 7, and CCDs, in addition to rBet v 1, rPhl p 1, rPhl p 5, was evaluated by using a multiparameter immunoblot. Results: Among the studied patients, 64.3, 80.4, and 41.1% were sensitized to birch, timothy grass, and mugwort pollen, respectively. Sensitization to profilins rBet v 2/Phl p 12 was demonstrated in 28.6%, to polcalcins Bet v 4/Phl p 7 in 8.9%, and to CCDs in 25%. In 29.3%, serum IgE reactivity to any of the cross-reactive components could be demonstrated. Serum IgE reactivity to rBet v 2 was always accompanied by IgE reactivity to rPhl p 12, and IgE reactivity to rBet v 4 was always accompanied by IgE reactivity to rPhl p 7. Among the patients with pollinosis co-sensitized to at least two allergen sources according to extract-based diagnosis, possible false-positive results due to sensitization to cross-reactive components were detected in 17.9%. Conclusion: Evaluation of sensitization to cross-reacting components may be useful in evaluation of patients with pollen allergy who are being assessed for allergen immunotherapy to optimize the constitution of their immunotherapy vaccines.

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