Ahouse JJ

Aroeti B

Bakos M-A

Brandtzaeg P

Cambier JC

Coyne RS

Daeron M

Davis W

Edberg JC

Ernst LK

Fridman W

Frutiger S

Gergely J

Harrison PT

Hibbs ML

Hulett MD

Knight KL

Kurosaki T

Kühn L

Lund J

Mallamaci MA

Masuda M

Morgan A

Nissim A

O'Grady JH

Popov S

Randall TD

Robertson MW

Samelson LE

Sears DW

Shen L

Shopes B

Silverstein SC

Simister NE

Stuart S

Underdown BJ

van de Winkel JGJ

Weetall M

 ▪ 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. </jats:p

Fc RECEPTORS AND THEIR INTERACTIONS WITH IMMUNOGLOBULINS

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