Document Detail

IgE receptor on human eosinophils (FcERII). Comparison with B cell CD23 and association with an adhesion molecule.
MedLine Citation:
PMID:  2531185     Owner:  NLM     Status:  MEDLINE    
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.
C Grangette; V Gruart; M A Ouaissi; F Rizvi; G Delespesse; A Capron; M Capron
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Publication Detail:
Type:  Comparative Study; Journal Article    
Journal Detail:
Title:  Journal of immunology (Baltimore, Md. : 1950)     Volume:  143     ISSN:  0022-1767     ISO Abbreviation:  J. Immunol.     Publication Date:  1989 Dec 
Date Detail:
Created Date:  1990-01-05     Completed Date:  1990-01-05     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  2985117R     Medline TA:  J Immunol     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  3580-8     Citation Subset:  AIM; IM    
Centre d'Immunologie et de Biologie Parasitaire, Institut Pasteur Lille, France.
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MeSH Terms
Amino Acid Sequence
Antigens, Differentiation, B-Lymphocyte
B-Lymphocytes / metabolism*
Cell Adhesion Molecules / analysis*
Cell Line
Eosinophils / metabolism*
Immunoglobulin E / metabolism*
Molecular Sequence Data
Oligopeptides / isolation & purification,  physiology
Receptors, Fc / analysis*
Receptors, IgE
Reg. No./Substance:
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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