Tumor Necrosis Factor (TNF) Receptor Superfamily Member TACI Is a High Affinity Receptor for TNF Family Members APRIL and BLyS
| Autor: | Yuxiang Gan, Jeff Carrell, Paul A. Moore, Donna Dimke, Steve Ruben, David W. Lafleur, Youmei Wu, Ping Feng, Palanisamy Kanakaraj, Thi Sau Migone, Kevin P. Baker, Ping Wei, Stephen Ullrich, Bernardetta Nardelli, Yun Hee Cho, Kara Taylor, Andy Garcia, Dana Bressette, Thomas Kaufman, Elisa Gollatz, Henrik S. Olsen |
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| Rok vydání: | 2000 |
| Předmět: |
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Complementary Time Factors Recombinant Fusion Proteins Transmembrane Activator and CAML Interactor Protein Ligands Transfection Polymerase Chain Reaction Biochemistry Receptors Tumor Necrosis Factor Cell Line Humans RNA Messenger Receptor BAFF receptor B-cell activating factor Molecular Biology Gene Library B-Lymphocytes Dose-Response Relationship Drug Reverse Transcriptase Polymerase Chain Reaction Tumor Necrosis Factor-alpha Chemistry Transmembrane activator and CAML interactor Cell Membrane Neuropeptides HEK 293 cells Membrane Proteins Nuclear Proteins Cell Biology Flow Cytometry Fusion protein Molecular biology Kinetics Cancer research Tumor necrosis factor alpha Signal transduction B-Cell Activation Factor Receptor Protein Binding Signal Transduction |
| Zdroj: | Journal of Biological Chemistry. 275:35478-35485 |
| ISSN: | 0021-9258 |
| Popis: | An expression cloning approach was employed to identify the receptor for B-lymphocyte stimulator (BLyS) and identified the tumor necrosis factor receptor superfamily member TACI as a BLyS-binding protein. Expression of TACI in HEK293T cells confers on the cells the ability to bind BLyS with subnanomolar affinity. Furthermore, a TACI-Fc fusion protein recognizes both the cleaved, soluble form of BLyS as well as the membrane BLyS present on the cell surface of a recombinant cell line. TACI mRNA is found predominantly in B-cells and correlates with BLyS binding in a panel of B-cell lines. We also demonstrate that TACI interacts with nanomolar affinity with the BLyS-related tumor necrosis factor homologue APRIL for which no clear in vivo role has been described. BLyS and APRIL are capable of signaling through TACI to mediate NF-kappaB responses in HEK293 cells. We conclude that TACI is a receptor for BLyS and APRIL and discuss the implications for B-cell biology. |
| Databáze: | OpenAIRE |
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