Abstract
CD38 was identified more than 20 years ago as a cell surface protein expressed on leukocyte subsets [1, 2]. Over the last decade, antibodies to human CD38 have been used to classify tumors from Multiple Myeloma [3, 4] and Chronic Lymphocytic Leukemia patients [5, 6], to identify which HIV+ patients will develop AIDS [7] and to subset a variety of leukocyte populations including hematopoietic progenitors [8, 9], germinal center B cells [10, 11] and regulatory T cells [12, 13]. However, despite the clear utility of using anti-CD38 antibodies as diagnostic and prognostic tools, it was unclear whether CD38 itself played an important functional role on normal lymphocytes. Since CD38 is expressed on the plasma membrane, it was postulated that CD38 was involved in leukocyte signaling or adhesion [14-16]. Although numerous experiments demonstrated that antibody mediated crosslinking of CD38 activated a variety of different signaling pathways in lymphocytes (reviewed in ref. [17, 18]), it was unclear how CD38 initiated signal transduction since the cytoplasmic tail of CD38 does not contain any known signaling motifs [2, 19].
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Lund, F.E., Randall, T.D., Partida-Sánchez, S. (2002). Regulation of Immune Responses by CD38 and cADPR. In: Lee, H.C. (eds) Cyclic ADP-Ribose and NAADP. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-0269-2_11
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