CD38


Description

The CD38 (CD38 molecule) is a protein-coding gene located on chromosome 4.

CD38 (cluster of differentiation 38), also known as cyclic ADP ribose hydrolase, is a glycoprotein found on the surface of many immune cells (white blood cells), including CD4+, CD8+, B lymphocytes and natural killer cells. CD38 also functions in cell adhesion, signal transduction and calcium signaling. In humans, the CD38 protein is encoded by the CD38 gene which is located on chromosome 4. CD38 is a paralog of CD157, which is also located on chromosome 4 (4p15) in humans. CD38 was first identified in 1980 as a surface marker (cluster of differentiation) of thymus cell lymphocytes. In 1992 it was additionally described as a surface marker on B cells, monocytes, and natural killer cells (NK cells). About the same time, CD38 was discovered to be not simply a marker of cell types, but an activator of B cells and T cells. In 1992 the enzymatic activity of CD38 was discovered, having the capacity to synthesize the calcium-releasing second messengers cyclic ADP-ribose (cADPR) and nicotinic acid adenine dinucleotide phosphate (NAADP). CD38 is most frequently found on plasma B cells, followed by natural killer cells, followed by B cells and T cells, and then followed by a variety of cell types. CD38 can function either as a receptor or as an enzyme.

CD38 synthesizes cyclic ADP-ribose (cADPR), a second messenger for glucose-induced insulin secretion. It also synthesizes nicotinate-adenine dinucleotide phosphate (NAADP), a calcium mobilizer, from 2'-phospho-cADPR and nicotinic acid, as well as from NADP+ and nicotinic acid. CD38 preferentially transforms 2'-phospho-cADPR into NAADP+ at both pH 5.0 and pH 7.4, while preferentially cleaving NADP+ to cADPR and ADPRP rather than into NADDP+. It also exhibits cADPR hydrolase activity.

CD38 is also known as ADPRC 1, ADPRC1, cADPR1.

Associated Diseases


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