Characterization of two receptors for TRAIL.
Details
State: Public
Version: author
Serval ID
serval:BIB_25D695CC2FFE
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
Characterization of two receptors for TRAIL.
Journal
FEBS letters
ISSN
0014-5793
Publication state
Published
Issued date
1997
Peer-reviewed
Oui
Volume
416
Number
3
Pages
329-34
Language
english
Notes
Publication types: Journal Article ; Research Support, Non-U.S. Gov't - Publication Status: ppublish
Abstract
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.
Keywords
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
Pubmed
Web of science
Open Access
Yes
Create date
24/01/2008 16:18
Last modification date
20/08/2019 14:04
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