BAFF is a TNF cytokine member (a type II membrane protein) that acts in both a membrane-bound form and soluble cytokine form. The extracellular domain of BAFF shows high homology with APRIL. The soluble form is derived by a cleavage in a furin consensus site. In human neutrophils treated with G-CSF, BAFF is processed intracellularly by a furin-type convertase. BAFF acts mainly as a soluble trimer and binds to three receptors, with decreasing affinity in the following order: BAFFR > TACI > BCMA. Mice deficient in BAFF or its receptor BAFFR exhibit an obstruction in B cell development after the transitional T1 stage and lack a marginal zone (MZ) and conventional B2 B cells. BAFFR-deficient mice and humans (patients with common variable immunodeficiency, CVID) develop severe B cell lymphopenia due to the arrest of B cell development at the transitional B cell stage. Extreme BAFF production triggers severe autoimmune disorders in mice similar to systemic lupus erythematosus and Sjögren’s syndrome. BAFF has been associated with different human diseases such as pancreatic ductal adenocarcinoma (PDAC), autoimmune pancreatitis, systemic lupus erythematosus, rheumatoid arthritis, Sjögren's syndrome, lymphoid cancers, HIV infection, and B cell malignancies such as non-Hodgkin's lymphoma (NHL).
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