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        Fc-receptor
                Introduction
                Functions of Fc-receptors
                Classes of Fc-receptors

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    Introduction
    Fc-receptor(s) are structures on the surface of cells and
    can contribute to the protective functions of the immune system.
    The name of Fc-receptors is based on binding and specificty for their
    counter-part or ligand, namely the Fc-portion of an antibody.
    Functionally, Fc-receptors can be involved in antibody-mediated phagocytosis and antibody-dependent cell-mediated cytotoxicity. Structurally, Fc-receptors are classified based on the
    type of antibody recognized

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    Functions of Fc-receptors
    Fc-receptors can be found on cells of the immune system like macrophages, monocytes,
    neutrophils, Natural killer cells and others.
    Cells with Fc-receptors can bind antibodies at the Fc-region 'tail' of an antibody. The binding ability between the Fc-receptors and the Fc-part of antibodies
    allows finding and binding of antibody covered objects. Thus, if the immune system works effectively and protectivey, cells with Fc-receptors like macrophages can bind to sickening bacteria or other microbial pathogens which are covered with antibodies via an interaction between Fc-receptors and antibodies. Once bound to the macrophages by this mechanism, the macrophage can start to ingest 'eat' the microbial pathogen in a process called phagocytosis and kill it. In this scenario the Fc-receptor contributes to protective immunity.
    Another function of Fc-receptors occurrs in a process called antibody-dependent cell-mediated cytotoxicity (ADCC). Under certain circumstances, Fc-receptors on the surface of Natural killer cells allow to kill antibody covered target cells. The consequence of the Fc-receptor antibody interaction is not eating or phagocytosis of the covered target inside the immune cells like the macrophage, but killing the target from the outside by the bystander Natural killer cell.

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    Classes of Fc-receptors
    Fc-receptors are classified according to the type of antibody or immunoglobulin (Ig) recognized:
      Fc-gamma R (FcγR) binds immunoglobulin G (IgG). These receptors can be subdivided according to antibody affinity and molecular structure: FcγRI (CD64, Fc-gamma receptor 1) has a high affinity compared with FcγRII (CD32, Fc-gamma receptor 2) and FcγRIII (CD16, Fc-gamma receptor 3). Also, FcγRI has three extracellular immunoglobulin-like domains compared to 2 domains FcγRII and FcγRIII in mice or man.
      Fc-epsilon receptor (FcεR) binds immunoglobulin E (IgE), and is similarly differentiated by affinity into the high-affinity receptor FcεRI and the low-affinity receptor FcεRII, (CD23) that belongs to the family of animal lectins.
      Poly-Immunoglobulin receptor (pIgR) binds IgM and multimeric IgA. The soluble form of pIgR termed secretory component is covalently bound to di- and oligomeric IgA and enables it to cross the epithelium for secretion.
      Neonatal Fc-receptor (FcRn) is a MHC Class I-like IgG Receptor that is responsible for the placental IgG transfer into the fetus. FcRn binds without specificity all IgG subclasses in a pH dependent manner. Binding to FcRn that is expressed in numerous normal tissues is a prerequisite for a long half-life of IgG antibodies.
     
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    Scientus.org Dictionary (Yet Another Wiki) RC : 1.39
    MIT OpenCourseWare
    This article is licensed under the GNU Free Documentation License [copyleft]. It uses material from the Wikipedia article "Fc-receptor". link