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 14 (CD14) is a member of the CD system. It takes its name from its inclusion in the CD molecule surface marker proteins. CD14 exists in two forms: a form anchored into the membrane or a soluble form. CD14 was found expressed in macrophages, neutrophil granulocyte and dendritic cells. The major function is to serve as a co-receptor (along with TLR4 and MD-2) for the bacterial lipopolysaccharide (LPS) and other pathogen-associated molecular patterns.
SLAM-induced signal-transduction events in T-lymphocytes are different from those in B-cells. Two modes ofSLAM signaling are likely to exist: one in which the inhibitor SH2D1A acts as a negative regulator and another inwhich protein-tyrosine phosphatase 2C (PTPN11)-dependent signal transduction operates.
CD155, commonly known as PVR (poliovirus receptor) and Necl-5 (nectin-like molecule-5), is a type I transmembrane single-span glycoprotein, and belongs to the nectins and nectin-like (Necl) subfamily. CD155 was originally identified based on its ability to mediate the cell attachment and entry of poliovirus (PV), an etiologic agent of the central nervous system disease poliomyelitis. The normal cellular function is in the establishment of intercellular adherens junctions between epithelial cells. CD155 may assist in an efficient humoral immune response generated within the intestinal immune system. It has been demonstrated that CD155 can be recognized and bond by DNAM-1 and CD96 which promote the adhesion, migration and NK-cell killing, and thus efficiently prime cell-mediated tumor-specific immunity.
The protein encoded by this gene is a transmembrane glycoprotein belonging to the immunoglobulin superfamily. The external domain mediates cell attachment to the extracellular matrix molecule vitronectin, while its intracellular domain interacts with the dynein light chain Tctex-1/DYNLT1. The gene is specific to the primate lineage, and serves as a cellular receptor for poliovirus in the first step of poliovirus replication. Multiple transcript variants encoding different isoforms have been found for this gene.
The glycan determinant CD15 is a distinguishing marker for human myeloid cells and mediates neutrophil adhesion to dendritic cells.
FcgRIV, also known as CD16-2, is an intermediate-affinity activating receptor for IgG2a and IgG2b. CD16-2 is the mouse homolog of human FcgRIIIA. CD16-2 is a low-affinity IgE receptor for all allotypes and the ligation of FcgRIV by antigen-IgE immune complexes promotes macrophage-mediated phagocytosis and is involved in lung inflammation.
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