The cluster of differentiation (CD) system is commonly used as cell markers in immunophynotyping. Different kinds of cells in the immune system can be identified through the surface CD molecules which associating with the immune function of the cell. There are more than 320 CD unique clusters and subclusters have been identified. Some of the CD molecules serve as receptors or ligands important to the cell through initiating a signal cascade which then alter the behavior of the cell. Some CD proteins do not take part in cell signal process but have other functions such as cell adhesion. Cluster of differentiation 38 (CD38), also known as ADP-ribosyl cyclase, is a glycoprotein found on the surface of many immune cells (white blood cells), including CD4+, CD8+, B and natural killer cells. It shares several characteristics with ADP-ribosyl cyclase 2 CD157. CD38 is a multifunctional ectoenzyme that catalyzes the synthesis and hydrolysis of cyclic ADP-ribose (cADPR) from NAD+ to ADP-ribose. It also functions in cell adhesion, signal transduction and calcium signaling. CD38 has been used as a prognostic marker in leukemia. It can also be used to identify plasma cells.
CD38, also called ADP-ribosyl cyclase, is a Type II integral membrane protein with 301 amino acids in length that belongs to the ADP-ribosyl cyclase family.It synthesizes the second messagers cyclic ADP-ribose and nicotinate-adenine dinucleotide phosphate, the former a second messenger for glucose-induced insulin secretion. And also moonlights as a receptor in cells of the immune system. CD38 is expressed in B and T lymphocytes, osteoclasts, and in cardiac, pancreatic, liver and kidney cells. Through its production of cyclic ADP-ribose, CD38 modulates calcium-mediated signal transduction in many types of cells, including neutrophils and pancreatic beta cells.
CD38, also known as ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1, is a Signal-anchor for type II membrane protein. CD38 is able to transform NAD+ to ADP-D-ribose and nicotinamide. It also can transform NADP+ to nicotinate-adenine dinucleotide phosphate and nicotinamide. CD38 is expressed at high levels in pancreas, liver, kidney, brain, testis, ovary, placenta, malignant lymphoma and neuroblastoma. Synthesizes the second messagers cyclic ADP-ribose and nicotinate-adenine dinucleotide phosphate, the former a second messenger for glucose-induced insulin secretion. Also has cADPr hydrolase activity. Also moonlights as a receptor in cells of the immune system.
CD39, also known as ENTPD1, belongs to the GDA1/CD39 NTPase family. It is expressed primarily on activated lymphoid cells and can also be detected in endothelial tissues. The vascular isoform and the placental isoform II are present in both placenta and umbilical vein, whereas placental isoform I is present in placenta only. CD39 can hydrolyze both nucleoside triphosphates and diphosphates. It is the dominant ecto nucleotidase of vascular and placental trophoblastic tissues and appears to modulate the functional expression of type 2 purinergic (P2) G protein coupled receptors (GPCRs). CD39 transgenic mice exhibit impaired platelet aggregation, prolonged bleeding times, and resistance to systemic thromboembolism. There is a correlation between ATP hydrolysis and triglycerides in patients with chronic heart disease, suggesting a relationship between ATP diphosphohydrolase and thrombogenesis. In the nervous system, CD39 could hydrolyze ATP and other nucleotides to regulate purinergic neurotransmission.
Ectonucleoside triphosphate diphosphohydrolase-1(NTPDase-1)is an integral membrane protein with an extracellular active site. Recombinant mouse NTPDase-1wasexpressed as a protein lacking its N- andC-terminaltransmembrane domains, resulting in the secretion of the soluble ectodomain. NTPDase-1was originally describedas CD39, a B lymphocyte cell surface marker. but it is also present on the surface of natural killer cells, T cells, and some endothelial cells. NTPDase1hydrolyzes the β-andγ phosphate residues of nucleotides, preferring ATP as the substrate. Through its hydrolysis of extracellular nucleotides, NTPDase-1plays arole in the regulation of purinergic signaling. NTPDase-1is involved in the processes of thromboregulation and vascular inflammation. The administration ofsoluble NTPDase-1may have therapeutic applications for the treatment of some vascular and transplantation-associateddiseases.
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