| IgE receptor on human eosinophils (FcERII). Comparison with B cell CD23 and association with an adhesion molecule. | |
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MedLine Citation:
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PMID: 2531185 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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IgE FcR (FcERII) on human eosinophils was characterized and compared with FcERII present on B cells (CD23). Two mAb, BB10 (anti-eosinophil FcERII) and 135 (anti-CD23), bound to the major component of FcERII at 45,000 to 50,000 Mr, both on purified hypodense eosinophils and on a B cell line (WIL-2WT). The specific ligand, human myeloma IgE, was able to bind to the molecules immunoprecipitated by BB10. A cross-reactivity between BB10 and a mAb anti-Leishmania gp63, which is a "fibronectin (Fn)-like" molecule, containing the L-arginine-L-glycyl-L-aspartyl (RGD) cell attachment domain indicated the presence of such a sequence in the common structure present on eosinophil and B cell FcERII. The synthetic tetrapeptide RGDS as well as its inverted sequence (SDGR) reduced the binding of BB10 and anti-Fn mAb to eosinophils and B cells. Flow microfluorometry analysis revealed a variable binding of BB10 and anti-Fn mAb to eosinophils purified from different patients, results compatible with recent findings on the inducibility of FcERIIb. The significant inhibition of IgE-dependent cytotoxicity against parasite targets by preincubation of eosinophils with BB10, anti-Fn and anti-CD23 mAb, with anti-RGDS polyclonal antibodies or with the SDGR peptide suggested the requirement of this cell adhesion sequence for the function of low affinity FcERII. The presence of such a sequence in the C-terminal domain of B cell FcERII raised the possibility of its role in B cell adhesion or B cell growth. |
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Authors:
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C Grangette; V Gruart; M A Ouaissi; F Rizvi; G Delespesse; A Capron; M Capron |
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Publication Detail:
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Type: Comparative Study; Journal Article |
Journal Detail:
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Title: Journal of immunology (Baltimore, Md. : 1950) Volume: 143 ISSN: 0022-1767 ISO Abbreviation: J. Immunol. Publication Date: 1989 Dec |
Date Detail:
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Created Date: 1990-01-05 Completed Date: 1990-01-05 Revised Date: 2006-11-15 |
Medline Journal Info:
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Nlm Unique ID: 2985117R Medline TA: J Immunol Country: UNITED STATES |
Other Details:
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Languages: eng Pagination: 3580-8 Citation Subset: AIM; IM |
Affiliation:
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Centre d'Immunologie et de Biologie Parasitaire, Institut Pasteur Lille, France. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Amino Acid Sequence Antigens, Differentiation, B-Lymphocyte B-Lymphocytes / metabolism* Cell Adhesion Molecules / analysis* Cell Line Eosinophils / metabolism* Humans Immunoglobulin E / metabolism* Molecular Sequence Data Oligopeptides / isolation & purification, physiology Receptors, Fc / analysis* Receptors, IgE |
| Chemical | |
Reg. No./Substance:
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0/Antigens, Differentiation, B-Lymphocyte; 0/Cell Adhesion Molecules; 0/Oligopeptides; 0/Receptors, Fc; 0/Receptors, IgE; 37341-29-0/Immunoglobulin E; 91037-65-9/arginyl-glycyl-aspartyl-serine |
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