Journal article
Fc receptors and their interactions with immunoglobulins
ANNUAL REVIEW OF CELL AND DEVELOPMENTAL BIOLOGY, Vol.12, pp.181-220
1996
DOI: 10.1146/annurev.cellbio.12.1.181
Abstract
Receptors for the Fc domain of immunoglobulins play an important role in immune defense. There are two well-defined functional classes of mammalian receptors. One class of receptors transports immunoglobulins across epithelial tissues to their main sites of action. This class includes the neonatal Fc receptor (FcRn), which transports immunoglobulin G (IgG), and the polymeric immunoglobulin receptor (pIgR), which transports immunoglobulin A (IgA) and immunoglobulin M (IgM). Another class of receptors present on the surfaces of effector cells triggers various biological responses upon binding antibody-antigen complexes. Of these, the IgG receptors (Fc gamma R) and immunoglobulin E (IgE) receptors (Fc epsilon R) are the best characterized. The biological responses elicited include antibody-dependent, cell-mediated cytotoxicity, phagocytosis, release of inflammatory mediators, and regulation of lymphocyte proliferation and differentiation. We summarize the current knowledge of the structures and functions of FcRn, pIgR, and the Fc gamma R and Fc epsilon RI proteins, concentrating on the interactions of the extracellular portions of these receptors with immunoglobulins.
Details
- Title: Subtitle
- Fc receptors and their interactions with immunoglobulins
- Creators
- M Raghavan - California Institute of TechnologyP J Bjorkman - California Institute of Technology
- Resource Type
- Journal article
- Publication Details
- ANNUAL REVIEW OF CELL AND DEVELOPMENTAL BIOLOGY, Vol.12, pp.181-220
- DOI
- 10.1146/annurev.cellbio.12.1.181
- ISSN
- 1530-8995
- Language
- English
- Date published
- 1996
- Academic Unit
- Roy J. Carver Department of Biomedical Engineering
- Record Identifier
- 9984232114502771
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