Beta1,4-Galactosyltransferase-I (B4GALT1), one of seven beta1,4-galactosyltransferases, is an enzyme commonly found in the trans-Golgi complex that adds galactose to oligosaccharides. They have an N-terminal hydrophobic signal sequence that directs the protein to the Golgi apparatus and which then remains uncleaved to function as a transmembrane anchor. By sequence similarity, the beta4GalTs form four groups: beta4GalT1 and beta4GalT2, beta4GalT3 and beta4GalT4, beta4GalT5 and beta4GalT6, and beta4GalT7. B4GALT1 gene directs production of B4GALT1 protein using either of two transcription start sites. The product of the smaller transcript serves the traditional biosynthetic role in the Golgi. This form also complexes with α-lactalbumin, a mammary-specific protein, to form lactose synthase. In addition to a biosynthetic role, the protein translated from the longer transcript appears on the plasma membranes of some cells where it serves as a signalling receptor in cell-matrix interactions such as sperm-egg binding.
Beta-1,4-galactosyltransferase 3 (B4GALT3) belongs to the glycosyltransferase 7 family. It is responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids. It is highest expression in placenta, prostate, testis, ovary, intestine and muscle, and in fetal brain.
β-1,4-galactosyltransferase 4 (B4GALT4) is a single-pass type II membrane protein that belongs to the Glycosyltransferase 7 family. B4GALT4 consist of the following 2 domains: N-Acetyllactosamine Synthase and β-N-Acetylglucosaminyl-Glycolipid β-1,4-Galactosyltransferase. B4GALT4 is highly expressed in the heart, placenta, kidney, and pancreas; it is lowly expressed in the brain, colon, lung, muscle, ovary, testis, and uterus. B4GALT4 function is responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids.
N-Acetyllactosaminide β-1,3-N-Acetylglucosaminyltransferase (B3GNT1) is a member of the β-1,3-N-Acetylglucosaminyltransferase family. B3GNT1 is a single-pass type II membrane protein and widely expressed in many tissues. B3GNT1 can initiate the synthesis or the elongation of the linear poly-N-acetyllactosaminoglycans. B3GNT1 is essential for the synthesis of poly-N-acetyllactosamine, a determinant for the blood group i antigen. It can initiate the synthesis or the elongation of the linear poly-N-acetyllactosaminoglycans.
The protein is the receptor that involved in the costimulatory signal essential for T-lymphocyte proliferation and interleukin-2 production, by binding CD28 or CTLA-4. It may play a critical role in the early events of T-cell activation and costimulation of naive T-cells, such as deciding between immunity and anergy that is made by T-cells within 24 hours after activation. Isoform 2 interferes with the formation of CD86 clusters, and thus acts as a negative regulator of T-cell activation. The protein interacts with MARCH8, human herpesvirus 8 MIR2 protein, adenovirus subgroup B fiber proteins and acts as a receptor for these viruses.It is expressed by activated B-lymphocytes and monocytes and promoted by MARCH8 and results in endocytosis and lysosomal degradation.It contains 1 Ig-like C2-type(immunoglobulin-like) domainand 1 Ig-like V-type (immunoglobulin-like) domain.
Programmed death ligand 2 (PD-L2); also referred to as B7-DC and CD273; is a member of the B7 family of proteins including B7-1; B7-2; B7-H2; B7-H1 (PD-L1); and B7-H3. PD-L2 is a type I membrane protein and structurally consists of an extracellular region containing one V-like and one C-like Ig domain; a transmembrane region; and a short cytoplasmic domain. PD-L2 is expressed on antigen presenting cells; placental endothelium and medullary thymic epithelial cells; and can be induced by LPS in B cells; INF-γ in monocytes; or LPS plus IFN-γ in dendritic cells. The CD28 and B7 protein families are critical regulators of immune responses. PD-L2 and PD-L1 are two ligands for PD-1; member of the CD28/CTLA4 family expressed on activated lymphoid cells; and thus provide signals for regulating T cell activation and immune tolerance. The interaction of B7-DC/PD-1 exhibited a 2-6-fold higher affinity compared with the interaction of B7-H1/PD-1.
CD276, also known as B7-H3, is a member of the B7 superfamily with signature IgV and IgG regions in extracellular domains. It is a type I transmembrane protein and shares 20–27% amino acid identity with other B7 family members. B7-H3 is involved in the activation of T lymphocytes, and regulates murine bone formation. It is also reported that B7-H3 may play an important role in muscle-immune interactions, providing further evidence of the active role of muscle cells in local immunoregulatory processes. B7-H3 is expressed on T-cells, natural killer cells, and antigen presenting cells, as well as some non-immune cells, such as osteoblasts, fibroblasts, fibroblast-like synoviocytes and epithelial cells. High expression of B7-H3 in tumor vasculature also correlates with poor survival in patients, suggesting that it may play a role in tumor cell migration.
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