RT Book, Section A1 Kipps, Thomas J. A2 Kaushansky, Kenneth A2 Prchal, Josef T. A2 Burns, Linda J. A2 Lichtman, Marshall A. A2 Levi, Marcel A2 Linch, David C. SR Print(0) ID 1178749327 T1 Functions of B Lymphocytes and Plasma Cells in Immunoglobulin Production T2 Williams Hematology, 10e YR 2021 FD 2021 PB McGraw-Hill Education PP New York, NY SN 9781260464122 LK hemonc.mhmedical.com/content.aspx?aid=1178749327 RD 2024/11/05 AB SUMMARYMuch of our immune defense against invading organisms is predicated upon the tremendous diversity of immunoglobulin (Ig) molecules. Igs are glycoproteins produced by B lymphocytes and plasma cells. These molecules can be considered receptors because the primary function of the Ig molecule is to bind antigen. A single person can synthesize 10–100 million different Ig molecules, each having a distinct antigen-binding specificity. The great diversity in this so-called humoral immune system allows us to generate antibodies specific for a variety of substances, including synthetic molecules not naturally present in our environment. Despite the diversity in the specificities of antibody molecules, the binding of antibody to antigen initiates a limited series of biologically important effector functions, such as complement activation or adherence of the immune complex to receptors on leukocytes. The eventual outcome is the clearance and degradation of the foreign substance. This chapter describes the structure of Igs and outlines the mechanisms by which B cells produce molecules of such tremendous diversity with defined effector functions.