NDLI: Interaction of Human IgE with Soluble Forms of IgE High Affinity Receptors

Content Provider	Springer Nature Link
Author	Liu, Jim Ruppel, Jane Shire, Steven J.
Copyright Year	1997
Abstract	Purpose. Interaction of human IgE with its high affinity receptor (FcεRI) on mast cells and basophils is an important step for initiating IgE mediated immune responses. To characterize the IgE and FcεRI interaction, we investigated this interaction in terms of stoichiometry and binding affinity in solution. The binding of IgE and IgE FcεRI α chain, the extracellular portion of IgE high affinity receptor (sFcεRIα) was compared with the binding of IgE and IgE immunoadhesin (FcεRIα-IgG). Methods. The interaction was characterized by analytical ultracentrifugation, size exclusion chromatography, light scattering and ELISA. Results. We show that the sFcεRIα is only able to bind to one IgE, while the immunoadhesin can bind to two IgE. The interaction between IgE and FcεRI is very strong. Both forms of soluble receptors have similar intrinsic binding affinity with IgE. Conclusions. Both soluble receptors (FcεRIα-IgG and sFcεRIα) can block the binding of IgE to its high affinity receptors on cell surface. The FcεRIα-IgG is a better IgE binding protein than sFcεRIα at physiological relevant conditions. A humanized anti-IgE monoclonal antibody, rhuMAb E25 that also can block the binding of IgE to its high affinity receptors appears to bind to IgE at slightly different regions or in a different manner as the soluble forms of IgE receptors.
Starting Page	1388
Ending Page	1393
Page Count	6
File Format	PDF
ISSN	07248741
Journal	Pharmaceutical Research
Volume Number	14
Issue Number	10
e-ISSN	1573904X
Language	English
Publisher	Kluwer Academic Publishers-Plenum Publishers
Publisher Date	1997-01-01
Publisher Place	New York
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Pharmacology/Toxicology Pharmacy Biochemistry Medical Law Biomedical Engineering
Content Type	Text
Resource Type	Article
Subject	Organic Chemistry Pharmacology Molecular Medicine Pharmacology (medical) Biotechnology Pharmaceutical Science

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
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