A soluble form of the high affinity IgE receptor, Fc-epsilon-RI, circulates in human serum

Soluble IgE receptors are potential in vivo modulators of IgE-mediated immune responses and are thus important for our basic understanding of allergic responses. We here characterize a novel soluble version of the IgE-binding alpha-chain of Fc-epsilon-RI (sFcεRI), the high affinity receptor for IgE....

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Bibliographic Details
Published in:PloS one 2011-04, Vol.6 (4), p.e19098-e19098
Main Authors: Dehlink, Eleonora, Platzer, Barbara, Baker, Alexandra H, Larosa, Jessica, Pardo, Michael, Dwyer, Peter, Yen, Elizabeth H, Szépfalusi, Zsolt, Nurko, Samuel, Fiebiger, Edda
Format: Article
Language:English
Subjects:
Affinity
Allergies
Antigens
Asthma
B cells
Binding sites
Cell culture
Cell surface
Chains
Children & youth
Crosslinking
Dendritic cells
Enzyme-Linked Immunosorbent Assay
Fc receptors
Gastroenterology
Hospitals
Humans
Hypersensitivity
Immune response
Immunoglobulin E
Immunoglobulin E - metabolism
Immunoglobulins
Immunomodulation
Ligands
Medical schools
Medicine
Modulators
Nutrition
Pediatrics
Polymer crosslinking
Protein Binding - genetics
Protein Isoforms - blood
Protein Isoforms - metabolism
Proteins
Receptors
Receptors, IgE - blood
Receptors, IgE - metabolism
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Summary:Soluble IgE receptors are potential in vivo modulators of IgE-mediated immune responses and are thus important for our basic understanding of allergic responses. We here characterize a novel soluble version of the IgE-binding alpha-chain of Fc-epsilon-RI (sFcεRI), the high affinity receptor for IgE. sFcεRI immunoprecipitates as a protein of ∼40 kDa and contains an intact IgE-binding site. In human serum, sFcεRI is found as a soluble free IgE receptor as well as a complex with IgE. Using a newly established ELISA, we show that serum sFcεRI levels correlate with serum IgE in patients with elevated IgE. We also show that serum of individuals with normal IgE levels can be found to contain high levels of sFcεRI. After IgE-antigen-mediated crosslinking of surface FcεRI, we detect sFcεRI in the exosome-depleted, soluble fraction of cell culture supernatants. We further show that sFcεRI can block binding of IgE to FcεRI expressed at the cell surface. In summary, we here describe the alpha-chain of FcεRI as a circulating soluble IgE receptor isoform in human serum.
ISSN:1932-6203
1932-6203
DOI:10.1371/journal.pone.0019098