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Beschreibung

ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1 (UniProt: P28907, also known as EC:3.2.2.6, 2'-phospho-ADP-ribosyl cyclase, 2'-phospho-ADP-ribosyl cyclase/2'-phospho-cyclic-ADP-ribose transferase, 2'-phospho-cyclic-ADP-ribose transferase, ADP-ribosyl cyclase 1, ADPRC 1, Cyclic ADP-ribose hydrolase 1, cADPr hydrolase 1, T10, CD38) is encoded by the CD38 gene (Gene ID: 952) in human. CD38, a member of the ADP-ribosyl cyclase family, is a single-pass type II membrane glycoprotein that contains a short cytoplasmic domain (aa 1-21), a transmembrane domain (aa 22-42), and a long extracellular domain (aa 43-300). It is expressed in high levels in pancreas, liver, kidney, brain, and in malignant lymphoma and neuroblastoma. It plays a role in cell adhesion, migration, and signal transduction. It is preferentially expressed at both early and late stages of the B and T-cell maturation and is detected on erythroid and myeloid progenitors in bone marrow, where the level of surface expression was shown to decrease during differentiation of blast-forming unit E to colony-forming unit E. CD38 is a bifunctional enzyme with both ADP-ribosyl cyclase and cADPR hydrolase activities. Its catalytic activity resides in the extracellular domain that can both generate and degrade cyclic-ADP ribose and can catalyze the base-exchange reaction between NADP+ and nicotinic acid to produce Nicotinic acid adenine dinucleotide phosphate (NAADP+). CD38 also moonlights as a receptor in cells of the immune system where it serves as a lymphocyte receptor and is a considered to be a prognostic marker for survival with B-cell chronic lymphoblastic leukemia.