Tumor necrosis factor receptor superfamily member 10A (TNFRSF10A) is also known as TNF-related apoptosis-inducing ligand receptor 1 (TRAIL-R1), Death receptor 4 (DR4), CD261 and APO2, which belongs to TNF superfamily. TNFRSF10A / DR4 is widely expressed and high levels are found in spleen, peripheral blood leukocytes, small intestine and thymus, but also in K-562 erythroleukemia cells, MCF-7 breast carcinoma cells and activated T-cells. APO2 / TNFRSF10A is receptor for the cytotoxic ligand TNFSF10 / TRAIL. This receptor is activated by tumor necrosis factor-related apoptosis inducing ligand (TNFSF1/TRAIL), and thus transduces cell death signal and induces cell apoptosis. TRAIL R1 can promote the activation of NF-kappa-B. TRAIL R1/CD261/TNFRSF1A induces apoptosis of many transformed cell lines but not of normal tissues, even though its death domain-containing receptor, DR4, is expressed on both cell types.
Tumor necrosis factor receptor superfamily, member 10a (TRAIL R1), also known as TRAIL receptor 1 (TRAIL R1) or CD261 antigen, is a member of the TNF-receptor superfamily. This receptor is activated by tumor necrosis factor-related apoptosis inducing ligand (TNFSF10/TRAIL), and thus transduces cell death signal and induces cell apoptosis. Studies with FADD-deficient mice suggested that FADD, a death domain containing adaptor protein, is required for the apoptosis mediated by this protein. TRAIL R1/CD261/TNFRSF10A serves as a receptor for the cytotoxic ligand TNFSF10/TRAIL. The adapter molecule FADD recruits caspase-8 to the activated receptor. The resulting death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation which initiates the subsequent cascade of caspases (aspartate-specific cysteine proteases) mediating apoptosis. TRAIL R1 can promote the activation of NF-kappa-B. TRAIL R1/CD261/TNFRSF10A induces apoptosis of many transformed cell lines but not of normal tissues, even though its death domain-containing receptor, DR4, is expressed on both cell types.
TNFRSF10B is a member of the TNF-receptor superfamily; and contains an intracellular death domain. This receptor can be activated by tumor necrosis factor-related apoptosis inducing ligand (TNFSF10/TRAIL/APO-2L); and transduces apoptosis signal. The adapter molecule FADD recruits caspase-8 to the activated receptor and is required for the apoptosis mediated by TNFRSF10B. TNFRSF10B is expressed in a number of cell types; and to particularly high levels in lymphocytes and spleen. This single-pass transmembrane protein contains two cysteine-rich repeat units in its extracellular region; followed by a transmembrane segment and a cytoplasmic tail containing a typical “death domain”. TNFRSF10B expression is regulated by the tumor suppressor p53. It is also indicated that the activation of NF-kappa-B can be promoted by TNFRSF10B.
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.
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