Human lymphocyte Fc receptor for IgE: sequence homology of its cloned cDNA with animal lectins.

Proceedings of the National Academy of Sciences (Impact Factor: 9.81). 03/1987; 84(3):819-23. DOI: 10.1073/pnas.84.3.819
Source: PubMed

ABSTRACT We have purified the human lymphocyte Fc receptor specific for IgE (Fc epsilon receptor) and its soluble form by using the anti-Fc epsilon receptor monoclonal antibody H107. Using an oligonucleotide probe corresponding to the partial amino acid sequence of the soluble Fc epsilon receptor related to IgE binding factor, we cloned, sequenced, and expressed a cDNA for the receptor. The Fc epsilon receptor has 321 amino acid residues with no NH2-terminal signal sequence. The receptor was separated into two domains by a putative 24-amino acid residue transmembrane region located near the NH2-terminal end. The Fc epsilon receptor showed a marked homology with animal lectins including human and rat asialoglycoprotein receptors, chicken hepatic lectin, and rat mannose binding proteins.

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    ABSTRACT: Conclusions and Future Perspectives As indicated herein, the FcεRII, defined rather simply as the “low affinity” receptor for IgE, exists on a variety of cell types. Present evidence from the cloning of the human lymphocyte FcεRII and the α-chain of the FcεRI combined with additional biochemical data indicate that the two receptors are products of different genes and that they interact with different sites on the IgE molecule. The lymphocyte receptor also sheds a FcεRII fragment into the media; in the human, but not murine, system this fragment retains IgE binding activity and has been termed an IgE-BF. The possible immunoregulatory activity of the fragment is an area of active investigation, however, at present the function is unclear. Recent evidence pointing to B cell stimulatory activities of the lymphocyte FcεRII are pointing to new previously unsuspected roles for this molecule. The FcεRII on macrophages, platelets, and eosinophils is not as well structurally characterized; however, functional studies point to a role in parasitic immunity. The exact relationship between the FcεRII on the various cell types, via the use of molecular probes, should be soon available. The classically studied IgE-BF are apparently quite different from the FcεRII fragment in that no apparent sequence homology was present. Biologic activities, both suppression and enhancement of IgE synthesis have been observed. The surprising retroviral homology remains an enigma and future experiments should determine if they are part of a family of related components in other species or if additional, as yet undiscovered, immunoregulatory components are present.
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