User:Nnkarma12/sandbox
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Immunoglobulin class switching recombination (CSR), or isotype switching, occurs in B cells and refers to the change in the heavy chain of antibodies caused by cytokines during an adaptive immune response. Immunoglobulins have four interlinked polypeptide chains, two heavy chains and two light chains.[1] The heavy chain determines the antibody class and therefore its effector function. The lower half of the heavy chain is called the Fc region, or variable end. The upper half of the heavy chain and the light chain are the antigen presenting site. This is where the antigen and the immunoglobulin bind in a lock-and-key type interaction, starting an immune response. This immune activation, causes a release of cytokines inducing the production of B cells in the bone marrow. Naive B cells that have never been in contact with a pathogen will produce a particular membrane bound antibody: IgM, or immunoglobulin M. In placental mammals there are five immunoglobulin isotypes known as IgA, IgD, IgE, IgG, and IgM. They are each named with an "Ig" prefix that stands for immunoglobulin, a name sometimes used interchangeably with antibody. As the B cell matures, it will express both IgG and IgM. This co-expression renders the B cell capable of responding to an antigen. The antigen will need to bind to the surface bound antibody in order for the B cell to start releasing antibodies in the blood plasma or the lymphatic system. This, now antibody producing cell, is called a plasma cell. [2]
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