IgGsynteesi

IgGsynteesi, or immunoglobulin G (IgG) synthesis, refers to the biological process by which the immune system produces antibodies of the IgG class. IgG antibodies are the most abundant and versatile type of antibody found in the blood and extracellular fluid of vertebrates, playing a crucial role in defending against infections and neutralizing toxins.

The synthesis of IgG begins in B lymphocytes, a type of white blood cell. When an antigen—a foreign substance such as a bacterium or virus—enters the body, it is recognized by B cells. This triggers their activation, often with the help of T helper cells. Activated B cells then differentiate into plasma cells, which are specialized for antibody production. Within these plasma cells, the genetic information encoding the variable regions of the antibody is rearranged through a process called somatic hypermutation and class switching, allowing the immune system to generate highly specific antibodies tailored to the invading pathogen.

IgG antibodies consist of four polypeptide chains: two identical heavy chains and two identical light chains. The heavy chains of IgG contain a constant region that determines its class (in this case, IgG) and a variable region that binds specifically to the antigen. The production of IgG is regulated by various cytokines and signaling molecules that influence B cell proliferation, differentiation, and antibody secretion.

IgGsynteesi is essential for long-term immunity, as IgG antibodies can cross the placental barrier, providing passive immunity to the fetus. Additionally, IgG antibodies have a relatively long half-life in the bloodstream, contributing to sustained protection against recurrent infections. Dysregulation in IgG synthesis can lead to immune deficiencies or autoimmune disorders, highlighting its importance in maintaining immune homeostasis.