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. The CD155 ligand CD96 is a member of the Ig superfamily. It's a immunoglobulin-like protein tentatively allocated to the repertoire of human NK receptors. NK cells recognize poliovirus receptor (PVR); anectins and nectin-like protein family member serve to mediate cell-cell adhesion; cell migration; with the presence of an additional receptor; CD96. CD96 promotes NK cell adhesion to target cells expressing PVR; stimulates cytotoxicity of activated NK cells; and mediates acquisition of PVR from target cells.
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. The CD97 is a receptor predominantly expressed in leukocytes and belongs to a new group of seven-span transmembrane molecules, which is also designed EGF-TM7 family. The family members are characterized by an extended extracellular region with several N-terminal epidermal growth factor-like domains two of which contain a calcium binding site. Muture CD 97 has two noncovalently associated subunits and is composed of a large extracellular protein (CD97 alpha) and a seven-membrane spanning protein (CD97 beta). CD97 is considered as a defining feature of G protein-coupled receptors. The effects that lymphocytes and erythrocytes adere to CD97-transfected COS cells suggest that CD97 has the ability to bind cellular ligands. CD97 alpha has three alternatively spliced isforms that are related to the calium binding EGF-like repeats in the microfibril protein fibrillin. Leukocytes strongly positive for CD97 are concentrated at sites of inflammation relative to CD97 expression in normal lymphoid tissues.
CD98 is a single-pass type I I membrane protein which belongs to the SLC3A transporter family. SLC3A2/MDU1 is expressed ubiquitously in all tissues tested with highest levels detected in kidney; placenta and testis and weakest level in thymus. It consists of an 85 kDa glycosylated type II transmembrane heavy chain and a 40-50 kDa non-glycosylated light chain with 12 transmembrane segments. The heavy chain (SLC3A2) pairs with one of several light chains (SLC7A5; 6; 7; 8; 10; or 11) and is required for the cell surface expression and amino acid transport function of the light chains. It is involved in guiding and targeting of LAT1 and LAT2 to the plasma membrane. It also mediates integrin signaling; T cell costimulation; B cell proliferation; and viral fusion with cell membranes.
CD99 Antigen-Like Protein 2 (CD99L2) belongs to the CD99 family. CD99L2 is a single-pass type I membrane protein and expressed in many tissues; with low expression in thymus. CD99L2 plays a role in a late step of leukocyte extravasation helping cells to overcome the endothelial basement membrane. CD99L2 and CD99 are involved in trans-endothelial migration of neutrophils in vitro and in the recruitment of neutrophils into inflamed peritoneum. A similar protein in mouse functions as an adhesion molecule during leukocyte extravasation. Alternate splicing results in multiple transcript variants.
CD99 is a type I transmembrane glycoprotein and the founding member of the CD99 family of molecules. The extracellular domain of CD99 contains no identifiable motifs, its cytoplasmic region, although short, does have signal transduction capability. Cells known to express CD99 include fibroblasts, neutrophils, T cells, double positive thymocytes, CD34+ stem cells, monocytes and endothelial cells. Two types of CD99 isoforms have been classified. Native human CD99 is referred to as the long, or type I isoform. The best studied type II isoform shows an Asp-Gly substitution for the C terminal 27 amino acids. The type I and II isoforms have distinctive signal transduction pathways (FAKsrc for type I PI3K plus srcERK1/2 for type II), and mediate clearly different biological outcomes. Homophilic interaction between CD99 on the neutrophil and CD99 on the endothelial cell regulates the transendothelial migration of neutrophils during inflammation. Human CD99 has 48% aa sequence identity to mouse CD99.
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