1932

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 (FcγR) and immunoglobulin E (IgE) receptors (FcϵR) 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 FcγR and FcϵRI proteins, concentrating on the interactions of the extracellular portions of these receptors with immunoglobulins.

Loading

Article metrics loading...

/content/journals/10.1146/annurev.cellbio.12.1.181
1996-11-01
2024-06-21
Loading full text...

Full text loading...

/content/journals/10.1146/annurev.cellbio.12.1.181
Loading
/content/journals/10.1146/annurev.cellbio.12.1.181
Loading

Data & Media loading...

  • Article Type: Review Article
This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error