CD38 was first identified in 1980 by E. L. Reinherz, S. Schlossman, and colleagues during their pioneering analysis of the human lymphocyte surface using monoclonal antibodies . Initially, it served as a marker for the study of thymocytes and activated T cells. Over time, its expression was also observed on other cell types, including B cells and monocytes .
Structurally, CD38 is composed of a single polypeptide chain with an extracellular domain, a transmembrane region, and a short cytoplasmic tail. The extracellular domain contains the active site responsible for its enzymatic functions.
CD38 has several important functions:
CD38 has gained significant attention in the field of oncology, particularly in the treatment of multiple myeloma (MM). Multiple myeloma is a hematological cancer characterized by the proliferation of malignant plasma cells in the bone marrow . CD38 is highly and uniformly expressed on multiple myeloma cells, making it an attractive target for immunotherapeutic approaches .
Several CD38-targeting monoclonal antibodies have been developed, including daratumumab and isatuximab . These antibodies have shown promising results in clinical trials, demonstrating significant anti-tumor activity and manageable toxicity profiles. CD38-targeted therapies are now an integral part of the treatment regimen for multiple myeloma patients .
Recombinant CD38 refers to the artificially produced form of the protein, typically generated using recombinant DNA technology. This involves inserting the gene encoding CD38 into a suitable expression system, such as bacteria or mammalian cells, to produce the protein in large quantities. Recombinant CD38 is used in various research applications, including the study of its enzymatic activity, receptor functions, and potential therapeutic uses.