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Low Affinity IgE Receptors (Fcε RII)

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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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  1. Subdepartment of Immunology, The Johns Hopkins University School of Medicine, 725 North Wolfe Street, 21205, Baltimore, MD

    Daniel H. Conrad

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Conrad, D.H. Low Affinity IgE Receptors (Fcε RII). Clinical Reviews in Allergy 7, 165–192 (1989). https://doi.org/10.1007/BF02914465

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