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Cross-linking of receptor-bound IgE to aggregates larger than dimers leads to rapid immobilization

Controlled cross-linking of IgE-receptor complexes on the surface of rat basophilic leukemia cells and mast cells has allowed a comparison of the lateral mobility and cell triggering activity of monomers, dimers, and higher oligomers of receptors. Addition of a monoclonal anti-IgE(Fc) antibody to Ig...

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Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1986
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2114094/
https://www.ncbi.nlm.nih.gov/pubmed/2935543
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collection PubMed
description Controlled cross-linking of IgE-receptor complexes on the surface of rat basophilic leukemia cells and mast cells has allowed a comparison of the lateral mobility and cell triggering activity of monomers, dimers, and higher oligomers of receptors. Addition of a monoclonal anti-IgE(Fc) antibody to IgE-sensitized cells in stoichiometric amounts relative to IgE produces IgE-receptor dimers with high efficiency. These dimers are nearly as mobile as IgE-receptor monomers and trigger cellular degranulation poorly, but in the presence of 30% D2O, substantial immobilization of the dimers is seen and degranulation activity doubles. Addition of this monoclonal antibody in larger amounts results in the formation of larger oligomeric receptor clusters which are immobile and effectively trigger the cells. Thus, small receptor clusters that are active in stimulating degranulation are immobilized in a process that is not anticipated by simple hydrodynamic theories. Further experiments involving cross-linking of receptor-bound IgE by multivalent antigen demonstrate that immobilization of receptors occurs rapidly (less than 2 min) upon cross-linking and is fully and rapidly reversible by the addition of excess monovalent hapten. The rapidity and reversibility of the immobilization process are entirely consistent with the possibility that immobilization represents a recognition event between clustered receptors and cytoskeleton- associated components that plays an important role early in the cell triggering mechanism.
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spelling pubmed-21140942008-05-01 Cross-linking of receptor-bound IgE to aggregates larger than dimers leads to rapid immobilization J Cell Biol Articles Controlled cross-linking of IgE-receptor complexes on the surface of rat basophilic leukemia cells and mast cells has allowed a comparison of the lateral mobility and cell triggering activity of monomers, dimers, and higher oligomers of receptors. Addition of a monoclonal anti-IgE(Fc) antibody to IgE-sensitized cells in stoichiometric amounts relative to IgE produces IgE-receptor dimers with high efficiency. These dimers are nearly as mobile as IgE-receptor monomers and trigger cellular degranulation poorly, but in the presence of 30% D2O, substantial immobilization of the dimers is seen and degranulation activity doubles. Addition of this monoclonal antibody in larger amounts results in the formation of larger oligomeric receptor clusters which are immobile and effectively trigger the cells. Thus, small receptor clusters that are active in stimulating degranulation are immobilized in a process that is not anticipated by simple hydrodynamic theories. Further experiments involving cross-linking of receptor-bound IgE by multivalent antigen demonstrate that immobilization of receptors occurs rapidly (less than 2 min) upon cross-linking and is fully and rapidly reversible by the addition of excess monovalent hapten. The rapidity and reversibility of the immobilization process are entirely consistent with the possibility that immobilization represents a recognition event between clustered receptors and cytoskeleton- associated components that plays an important role early in the cell triggering mechanism. The Rockefeller University Press 1986-02-01 /pmc/articles/PMC2114094/ /pubmed/2935543 Text en This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Articles
Cross-linking of receptor-bound IgE to aggregates larger than dimers leads to rapid immobilization
title Cross-linking of receptor-bound IgE to aggregates larger than dimers leads to rapid immobilization
title_full Cross-linking of receptor-bound IgE to aggregates larger than dimers leads to rapid immobilization
title_fullStr Cross-linking of receptor-bound IgE to aggregates larger than dimers leads to rapid immobilization
title_full_unstemmed Cross-linking of receptor-bound IgE to aggregates larger than dimers leads to rapid immobilization
title_short Cross-linking of receptor-bound IgE to aggregates larger than dimers leads to rapid immobilization
title_sort cross-linking of receptor-bound ige to aggregates larger than dimers leads to rapid immobilization
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2114094/
https://www.ncbi.nlm.nih.gov/pubmed/2935543