Article: article from journal or magazin.
Characterization of two receptors for TRAIL.
Publication types: Journal Article ; Research Support, Non-U.S. Gov't - Publication Status: ppublish
Two receptors for TRAIL, designated TRAIL-R2 and TRAIL-R3, have been identified. Both are members of the tumor necrosis factor receptor family. TRAIL-R2 is structurally similar to the death-domain-containing receptor TRAIL-R1 (DR-4), and is capable of inducing apoptosis. In contrast, TRAIL-R3 does not promote cell death. TRAIL-R3 is highly glycosylated and is membrane bound via a putative phosphatidylinositol anchor. The extended structure of TRAIL-R3 is due to the presence of multiple threonine-, alanine-, proline- and glutamine-rich repeats (TAPE repeats). TRAIL-R2 shows a broad tissue distribution, whereas the expression of TRAIL-R3 is restricted to peripheral blood lymphocytes (PBLs) and skeletal muscle. All three TRAIL receptors bind TRAIL with similar affinity, suggesting a complex regulation of TRAIL-mediated signals.
Amino Acid Sequence, Apoptosis, Apoptosis Regulatory Proteins, Cell Line, Chromosome Mapping, Cloning, Molecular, Humans, Kinetics, Lymphocytes, Membrane Glycoproteins, Molecular Sequence Data, Muscle, Skeletal, Polymerase Chain Reaction, Receptors, TNF-Related Apoptosis-Inducing Ligand, Receptors, Tumor Necrosis Factor, Recombinant Proteins, Sequence Alignment, Sequence Homology, Amino Acid, Sequence Tagged Sites, Signal Transduction, TNF-Related Apoptosis-Inducing Ligand, Transfection, Tumor Necrosis Factor Decoy Receptors, Tumor Necrosis Factor-alpha
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