CD35, also known as complement receptor 1 (CR1), is a 220-300 kDa N-glycosylated member of the RCA (regulators of complement activation) family of proteins. CD35 binds and internalizes particles and immune complexes that are opsonized with MBL or complement components C3b, C3i, C4b, or C1q. CD35 additionally protects the cell from complement-mediated lysis by serving as a cofactor for Factor I and inhibiting the C3 and C5 convertases. The extracellular domain (ECD) of human CD35 contains 30 tandem SCR/SUSHI repeats.
The protein encoded by this gene is the fourth major glycoprotein of the platelet surface and serves as a receptor for thrombospondin in platelets and various cell lines. Since thrombospondins are widely distributed proteins involved in a variety of adhesive processes, this protein may have important functions as a cell adhesion molecule. It binds to collagen, thrombospondin, anionic phospholipids and oxidized LDL. It directly mediates cytoadherence of Plasmodium falciparum parasitized erythrocytes and it binds long chain fatty acids and may function in the transport and/or as a regulator of fatty acid transport. Mutations in this gene cause platelet glycoprotein deficiency. Multiple alternatively spliced transcript variants have been found for this gene.
The cluster of differentiation (CD) system is commonly used as cell markers in Immunophenotyping. Different kinds of cells in the immune system can be identified through the surface CD molecules 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 36 (CD36), also known as FAT, SCARB3, GP88, glycoprotein IV (gpIV) and glycoprotein IIIb (gpIIIb), is a member of the CD system as well as the class B scavenger receptor family of cell surface proteins. CD36 can be found on the surface of many cell types in vertebrate animals and it consists of 472 amino acids and is extensively glycosylated. It is an integral membrane protein primarily serving as receptors for thrombospondin and collagen and by the erythrocytes infected with the human malaria parasite. The role of CD36 as a cell surface receptor has been extended to that of a signal transduction molecule.
The protein encoded by this gene is a non-lineage-restricted, type II transmembrane glycoprotein that synthesizes and hydrolyzes cyclic adenosine 5'-diphosphate-ribose, an intracellular calcium ion mobilizing messenger. The release of soluble protein and the ability of membrane-bound protein to become internalized indicate both extracellular and intracellular functions for the protein. This protein has an N-terminal cytoplasmic tail, a single membrane-spanning domain, and a C-terminal extracellular region with four N-glycosylation sites. Crystal structure analysis demonstrates that the functional molecule is a dimer, with the central portion containing the catalytic site. It is used as a prognostic marker for patients with chronic lymphocytic leukemia. Alternative splicing results in multiple transcript variants.
CD38, also known as ADP-ribosyl cyclase, is a Type II integral membrane protein. The enzyme is able to transform NAD(P)+ into three different products with calcium mobilizing ability, cyclic ADP-ribose, NAADP+, and ADP-ribose . 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.
The cluster of differentiation (CD) system is commonly used as cell markers in Immunophenotyping. Different kinds of cells in the immune system can be identified through the surface CD molecules 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.
CD39,also known as ectonucleoside triphosphate diphosphohydrolase 1 (NTPDase 1), is a multi-pass membrane ectoenzyme that metabolizes adenosine-5'-triphosphate (ATP) to regulate purinergic signaling. Purinergic signaling by extracellular ATP and its metabolites regulate many biological processes, including vascular tone, digestion, neuronal function, and inflammation in both normal and diseased states. CD39 is expressed in endothelial cells in the vasculature to regulate local platelet purinergic signaling via metabolism of ATP to adenosine. Accordingly, CD39 regulates platelet activation aggregation and contributes to the antithrombotic properties of endothelial cells. ATP and its metabolites also finely modulate the activity of T cells and macrophages. Immunomodulation is regulated, in part, by the availability of extracellular ATP and adenosine, suggesting that CD39 may play an immunosuppressive role in the tumor microenvironment.
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