In immunology, an Fc receptor is a protein found on the surface of certain cells – including, among others, B lymphocytes, follicular dendritic cells, natural killer cells, macrophages, neutrophils, eosinophils, basophils, human platelets, and mast cells – that contribute to the protective functions of the immune system.

Nov 10, 2021 · Fc receptors (FcRs) are a group of glycoproteins that belong to the immunoglobulin superfamily and are classified, like Fc alpha receptors (FcαRs), Fc gamma receptors (FcγRs) and Fc epsilon ...

Human and mouse Fc receptors for IgG (FcγRs) can be distinguished by their affinity for the antibody Fc-fragment and by the signalling pathways they induce.

Antibodies are major molecular effectors of adaptive immune responses. Most, if not all, biological activities of antibodies, however, depend on the functional properties of cells that express receptors for the Fc portion of antibodies (FcR). Most ...

Jan 10, 2025 · Fc receptors are fundamental in orchestrating immune responses, acting as conduits for communication between antibodies and immune cells. Their ability to bind antibodies allows them to translate the presence of antigens into actionable cellular processes.

Fc receptors (FcRs) belong to the ITAM-associated receptor family. FcRs control the humoral and innate immunity which are essential for appropriate responses to infections and prevention of chronic inflammation or auto-immune diseases.

Aug 1, 2002 · The receptors for the Fc of immunoglobulins, Fc receptors (FcRs), link the humoral and cellular branches of the immune system, and they have important functions in the activation and down ...

Fc receptors (FcRs) are a series of cell-surface proteins that specifically recognize the Fc region of an antibody. They are the only class of receptors responsible for the functions of immunoglobulins and plays a role in regulating immune activity.

Fc receptors are integral membrane glycoproteins recognising the fragment crystallisable (FC) region of various immunoglobulin classes and subclasses. There is a specific Fc receptor for each immunoglobulin; IgA binds to FcαR, IgG to FcγR, IgD to FcδR, IgE to FcεR and IgM to FcμR.

The extracellular parts of most human Fc receptors are composed of varying amounts (1–5) of immunoglobulin domains. The two exceptions are the lectin family member FceRII and the major histocompatibility complex (MHC) class I protein family