Fc gamma RII, also known as FcγRII, is an abbreviation used in immunology and molecular biology to denote Fc gamma receptor II. It is a cell surface receptor, primarily found on immune cells, that plays a crucial role in the recognition and binding of immunoglobulin G (IgG) antibodies.
Fc gamma RII belongs to the family of Fc gamma receptors that specifically bind to the Fc region of antibodies. This receptor is a transmembrane glycoprotein, meaning it spans across the cell membrane and possesses sugar molecules on its surface. It consists of two identical subunits, designated as α chains, each comprising an extracellular domain, a transmembrane domain, and a short intracellular tail.
Upon binding to the Fc region of IgG antibodies, Fc gamma RII initiates an intracellular signaling cascade that triggers various immune responses. These responses include phagocytosis, antibody-dependent cellular cytotoxicity (ADCC), and the release of inflammatory molecules. Fc gamma RII is also involved in regulating B cell activation and antibody production.
Different variants of Fc gamma RII exist, such as Fc gamma RIIA, Fc gamma RIIB, and Fc gamma RIIC, with slightly different cell distribution and signaling capabilities. These variants have distinct affinities for different IgG antibody subclasses.
Overall, Fc gamma RII is an essential receptor in the immune system that facilitates the recognition, binding, and activation of immune cells in response to IgG antibody-mediated immune responses.
