BAFF receptor
BAFF receptor (B-cell activating factor receptor, BAFF-R), also known as tumor necrosis factor receptor superfamily member 13C (TNFRSF13C), is a membrane protein of the TNF receptor superfamily which recognizes BAFF.[1] In humans it is encoded by the TNFRSF13C gene.[2]
Function
B-cell activating factor (BAFF) enhances B-cell survival in vitro and is a regulator of the peripheral B-cell population. The protein encoded by this gene is a receptor for BAFF and is a type III transmembrane protein containing a single extracellular phenylalanine-rich domain. It is thought that this receptor is the principal receptor required for BAFF-mediated mature B-cell survival.[2]
Clinical significance
Overexpression of BAFF in mice results in mature B-cell hyperplasia and symptoms of systemic lupus erythematosus (SLE). Also, some SLE patients have increased levels of BAFF in serum. Therefore, it has been proposed that abnormally high levels of BAFF may contribute to the pathogenesis of autoimmune diseases by enhancing the survival of autoreactive B cells.[2]
See also
References
- ↑ Thompson JS, Bixler SA, Qian F, Vora K, Scott ML, Cachero TG, Hession C, Schneider P, Sizing ID, Mullen C, Strauch K, Zafari M, Benjamin CD, Tschopp J, Browning JL, Ambrose C (Sep 2001). "BAFF-R, a newly identified TNF receptor that specifically interacts with BAFF". Science 293 (5537): 2108–11. doi:10.1126/science.1061965. PMID 11509692.
- 1 2 3 "Entrez Gene: TNFRSF13C tumor necrosis factor receptor superfamily, member 13C".
Further reading
- Laâbi Y, Egle A, Strasser A (Dec 2001). "TNF cytokine family: more BAFF-ling complexities". Current Biology 11 (24): R1013–6. doi:10.1016/S0960-9822(01)00613-3. PMID 11747837.
- Defrance T, Casamayor-Pallejà M, Krammer PH (2003). "The life and death of a B cell". Advances in Cancer Research 86: 195–225. doi:10.1016/S0065-230X(02)86006-7. PMID 12374279.
- Ambrose CM (2003). "BAFF-R". Journal of Biological Regulators and Homeostatic Agents 16 (3): 211–3. PMID 12456020.
- Bossen C, Schneider P (Oct 2006). "BAFF, APRIL and their receptors: structure, function and signaling". Seminars in Immunology 18 (5): 263–75. doi:10.1016/j.smim.2006.04.006. PMID 16914324.
- Treml LS, Crowley JE, Cancro MP (Oct 2006). "BLyS receptor signatures resolve homeostatically independent compartments among naïve and antigen-experienced B cells". Seminars in Immunology 18 (5): 297–304. doi:10.1016/j.smim.2006.07.001. PMID 16919470.
- Kalled SL (Oct 2006). "Impact of the BAFF/BR3 axis on B cell survival, germinal center maintenance and antibody production". Seminars in Immunology 18 (5): 290–6. doi:10.1016/j.smim.2006.06.002. PMID 16931038.
- Mackay F, Leung H (Oct 2006). "The role of the BAFF/APRIL system on T cell function". Seminars in Immunology 18 (5): 284–9. doi:10.1016/j.smim.2006.04.005. PMID 16931039.
- Schneider P, MacKay F, Steiner V, Hofmann K, Bodmer JL, Holler N, Ambrose C, Lawton P, Bixler S, Acha-Orbea H, Valmori D, Romero P, Werner-Favre C, Zubler RH, Browning JL, Tschopp J (Jun 1999). "BAFF, a novel ligand of the tumor necrosis factor family, stimulates B cell growth". The Journal of Experimental Medicine 189 (11): 1747–56. doi:10.1084/jem.189.11.1747. PMC 2193079. PMID 10359578.
- Hartley JL, Temple GF, Brasch MA (Nov 2000). "DNA cloning using in vitro site-specific recombination". Genome Research 10 (11): 1788–95. doi:10.1101/gr.143000. PMC 310948. PMID 11076863.
- Yan M, Brady JR, Chan B, Lee WP, Hsu B, Harless S, Cancro M, Grewal IS, Dixit VM (Oct 2001). "Identification of a novel receptor for B lymphocyte stimulator that is mutated in a mouse strain with severe B cell deficiency". Current Biology 11 (19): 1547–52. doi:10.1016/S0960-9822(01)00481-X. PMID 11591325.
- Rolink AG, Melchers F (Apr 2002). "BAFFled B cells survive and thrive: roles of BAFF in B-cell development". Current Opinion in Immunology 14 (2): 266–75. doi:10.1016/S0952-7915(02)00332-1. PMID 11869903.
- Xu LG, Shu HB (Dec 2002). "TNFR-associated factor-3 is associated with BAFF-R and negatively regulates BAFF-R-mediated NF-kappa B activation and IL-10 production". Journal of Immunology 169 (12): 6883–9. doi:10.4049/jimmunol.169.12.6883. PMID 12471121.
- Kim HM, Yu KS, Lee ME, Shin DR, Kim YS, Paik SG, Yoo OJ, Lee H, Lee JO (May 2003). "Crystal structure of the BAFF-BAFF-R complex and its implications for receptor activation". Nature Structural Biology 10 (5): 342–8. doi:10.1038/nsb925. PMID 12715002.
- Liu Y, Hong X, Kappler J, Jiang L, Zhang R, Xu L, Pan CH, Martin WE, Murphy RC, Shu HB, Dai S, Zhang G (May 2003). "Ligand-receptor binding revealed by the TNF family member TALL-1". Nature 423 (6935): 49–56. doi:10.1038/nature01543. PMID 12721620.
- Gordon NC, Pan B, Hymowitz SG, Yin J, Kelley RF, Cochran AG, Yan M, Dixit VM, Fairbrother WJ, Starovasnik MA (May 2003). "BAFF/BLyS receptor 3 comprises a minimal TNF receptor-like module that encodes a highly focused ligand-binding site". Biochemistry 42 (20): 5977–83. doi:10.1021/bi034017g. PMID 12755599.
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| | 1oqe: Crystal structure of sTALL-1 with BAFF-R |
| 1osx: Solution Structure of the Extracellular Domain of BLyS Receptor 3 (BR3) |
| 1p0t: Crystal Structure of the BAFF-BAFF-R complex (part II) |
| 2hfg: Crystal structure of hBR3 bound to CB3s-Fab |
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This article incorporates text from the United States National Library of Medicine, which is in the public domain.
