Tumor Necrosis Factor Receptor Superfamily Member 10C (TNFRSF10C) is a glycosyl-phosphatidylinositol-linked membrane protein which binds TRAIL with high affinity. TNFRSF10C has the TRAIL-binding extracellular cysteine-rich domains; lacks the intracellular signaling domain. As a result; binding of TRAIL to TRAIL R3 doesn’t transduce an apoptosis signal. The expression of TRAIL R3 gene has been shown to protect cells bearing TRAIL R1 and/or TRAIL R2 from TRAIL-induced apoptosis.
Human TRAIL R4 is a type 1, TNF R family membrane protein, which is a receptor for TRAIL (APO2 ligand). TRAIL R4 contains an extracellular TRAIL-binding domain, a transmembrane domain, and a truncated cytoplasmic death domain. In the new TNF superfamily nomenclature, TRAIL R4 is referred to as TNFRSF10D. TRAIL R4 is unique among the TRAIL receptors in that its cytoplasmic domain contains a truncated consensus death domain motif. Binding of TRAIL R4 does not result in an apoptotic signal. Overexpression of TRAIL R4 can protect cells bearing TRAIL R1 and/or TRAIL R2 from TRAIL mediated apoptosis. The human soluble TRAIL R4/Fc chimera neutralizes the ability of TRAIL to induce apoptosis.
Tumor necrosis factor receptor superfamily member 10D (TNFRSF10D), also known as TNF-related apoptosis-inducing ligand receptor 4 (TRAIL R4), CD264, and Decoy receptor 2, is a member of the TNF-receptor superfamily. This receptor contains an extracellular TRAIL-binding domain, a transmembrane domain, and a truncated cytoplamic death domain. This receptor does not induce apoptosis, and has been shown to play an inhibitory role in TRAIL-induced cell apoptosis. TRAIL R4/CD264/TNFRSF10D is widely expressed, in particular in fetal kidney, lung and liver, and in adult testis and liver. TRAIL R4/CD264/TNFRSF10D is also expressed in peripheral blood leukocytes, colon and small intestine, ovary, prostate, thymus, spleen, pancreas, kidney, lung, placenta and heart. The signaling capacity of TRAIL R4 is similar to that of TRAIL R1 and TRAIL R2 with respect to NF-κB activation, but differs in its inability to induce apoptosis. TRAIL R4 retains a C-terminal element containing one third of a consensus death domain motif. Transient overexpression of TRAIL R4 in cells normally sensitive to TRAIL-mediated killing confers complete protection, suggesting that one function of TRAIL R4 may be inhibition of TRAIL cytotoxicity.
Transaldolase (TALDO1) belongs to the transaldolase family of Type 1 subfamily. TALDO1 is expressed selectively in oligodendrocytes of the brain. TALDO1 is a key enzyme of the nonoxidative pentose phosphate pathway providing ribose-5-phosphate for nucleic acid synthesis and NADPH for lipid biosynthesis. This pathway can also maintain glutathione at a reduced state and thus protect sulfhydryl groups and cellular integrity from oxygen radicals. TALDO1 deficiency results in telangiectases of the skin, hepatosplenomegaly and enlarged clitoris.
Transferrin is a glycoprotein with an approximate molecular weight of 76.5 kDa. This glycoprotein is thought to have been created as a result of an ancient gene duplication event that led to generation of homologous C and N-terminal domains each of which binds one ion of ferric iron. The function of Transferrin is to transport iron from the intestine, reticuloendothelial system, and liver parenchymal cells to all proliferating cells in the body. This protein may also have a physiologic role as granulocyte / pollen-binding protein (GPBP) involved in the removal of certain organic matter and allergens from serum. Transferrins are iron binding transport proteins which bind Fe3+ ion in association with the binding of an anion, usually bicarbonate. It is responsible for the transport of iron from sites of absorption and heme degradation to those of storage and utilization. Serum transferrin may also have a further role in stimulating cell proliferation. When a transferrin loaded with iron encounters with a transferring receptor on cell surface, transferring binds to it and, as a consequence, is transported into the cell in a visicle by receptor-mediated endocytosis. The PH is reduced by hydrogen iron pumps. The lower pH causes transferrin to release its iron ions. The receptor is then transported through the endocytic cycle back to the cell surface, ready for another round of iron uptake. Each transferrin molecule has the ability to carry two iron ions in the ferric form.
Serotransferrin belongs to transferrin family, and contains 2 transferrin-like domains. The protein is a secreted protein, and expressed by the liver and secreted in plasma. Transferrins are iron binding transport proteins which can bind two Fe3+ ions in association with the binding of an anion. It is responsible for the transport of iron from sites of absorption and heme degradation to those of storage and utilization. Serum transferrin may also have a further role in stimulating cell proliferation.
Transferrin receptor protein 1 (TFRC) belongs to the peptidase M28 family that is synthesized as a 172 amino acid (aa). TFRC regulated by cellular iron levels through binding of the iron regulatory proteins, IRP1 and IRP2, to iron-responsive elements in the 3'-UTR. It binds one transferrin or HFE molecule per subunit and binds the HLA class II histocompatibility antigen, DR1. It Interacts with SH3BP3 and STEAP3, facilitates TFRC endocytosis in erythroid precursor cells. Cellular uptake of iron occurs via receptor-mediated endocytosis of ligand-occupied transferrin receptor into specialized endosomes. Endosomal acidification leads to iron release. The apotransferrin-receptor complex is then recycled to the cell surface with a return to neutral pH and the concomitant loss of affinity of apotransferrin for its receptor. Transferrin receptor is necessary for development of erythrocytes and the nervous system. A second ligand, the heditary hemochromatosis protein HFE, competes for binding with transferrin for an overlapping C-terminal binding site. It positively regulates T and B cell proliferation through iron uptake.
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