Identification of a receptor for BLyS demonstrates a crucial role in humoral immunity (original) (raw)

• Gruss, H. J. & Dower, S. K. Tumor necrosis factor ligand superfamily: involvement in the pathology of malignant lymphomas. Blood 85, 3378–3404 (1995).
  CAS PubMed Google Scholar
• Smith, C. A., Farrah, T. & Goodwin, R. G. The TNF receptor superfamily of cellular and viral proteins: activation, costimulation, and death. Cell 76, 959–962 (1994).
  CAS PubMed Google Scholar
• Ashkenazi, A. & Dixit, V. M. Death receptors: signling and modulation. Science 281, 1305–1308 (1998).
  CAS PubMed Google Scholar
• Moore, P.A. et al. BLyS: member of the tumor necrosis factor family and B lymphocyte stimulator. Science 285, 260–263 (1999).
  CAS PubMed Google Scholar
• Shu, H. B., Hu, W. H. & Johnson, H. TALL-1 is a novel member of the TNF family that is down-regulated by mitogens. J. Leukocyte Biol. 65, 680–683 (1999).
  CAS PubMed Google Scholar
• Mukhopadhyay, A., Ni, J., Zhai, Y., Yu, G. L. & Aggarwal, B. B. Identification and characterization of a novel cytokine, THANK, a TNF homologue that activates apoptosis, nuclear factor-kappaB, and c-Jun NH2-terminal kinase. J. Biol. Chem. 274, 15978–15981 (1999).
  CAS PubMed Google Scholar
• Schneider, P. et al. BAFF, a novel ligand of the tumor necrosis factor family, stimulates B cell growth. J. Exp. Med. 189, 1747–1756 (1999).
  CAS PubMed PubMed Central Google Scholar
• Mackay, F. et al. Mice transgenic for BAFF develop lymphocytic disorders along with autoimmune manifestations. J. Exp. Med. 190, 1697–1710 (1999).
  CAS PubMed PubMed Central Google Scholar
• Kahre, S. D. et al. Severe B cell hyperplasia and autoimmune disease in TALL-1 transgenic mice. Proc. Natl Acad. Sci. USA 97, 3370–3375 (2000).
  Google Scholar
• Flanagan, J. G. & Leder, P. The kit ligand: a cell surface molecule altered in steel mutant fibroblasts. Cell 63, 185–194 (1990).
  CAS PubMed Google Scholar
• von Bulow, G. U. & Bram, R. J. NF-AT activation induced by a CAML-interacting member of the tumor necrosis factor receptor superfamily. Science 278, 138–141 (1997).
  CAS PubMed Google Scholar
• Pennica, D. et al. Human tumour necrosis factor: precursor structure, expression and homology to lymphotoxin. Nature 312, 724–729 (1984).
  CAS PubMed Google Scholar
• Mauri, D. et al. LIGHT, a new member of the TNF superfamily, and lymphotoxin alpha are ligands for Herpesvirus Entry Mediator. Immunity 8, 21–30 (1998).
  CAS PubMed Google Scholar
• Ashkenazi, A. et al. Protection against endotoxic shock by a tumor necrosis factor receptor immunoadhesin. Proc. Natl Acad. Sci. USA 88, 10535–10539 (1991).
  CAS PubMed PubMed Central Google Scholar
• Pitti, R. M. et al. Induction of apoptosis by Apo-2 Ligand, a new member of the tumor necrosis factor receptor family. J. Biol. Chem. 271, 12697–12690 (1996).
  Google Scholar
• Marsters, S. A. et al. Identification of a ligand for the death-domain-containing receptor Apo3. Curr. Biol. 8, 525–528 (1998).
  CAS PubMed Google Scholar
• Wong, B. R. et al. TRANCE is a novel ligand of the TNFR family that activates c-Jun-N-terminal kinase in T cells. J. Biol. Chem. 272, 25190–25194 (1997).
  CAS PubMed Google Scholar
• Tan, K. et al. Characterization of a novel TNF-like ligand and recently described TNF ligand and TNF receptor superfamily genes and their constitutive and inducible expression in hematopoietic and non-hematopoietic cells. Gene 204, 35–46 (1997).
  CAS PubMed Google Scholar
• Gurney, A. et al. Identification of a new member of the tumor necrosis factor family and its receptor, a human ortholog of mouse GITR. Curr. Biol. 9, 215–221 (1999).
  CAS PubMed Google Scholar
• Marsters, S. et al. HVEM, a member of the TNF receptor family, interacts with members of the TRAF family and activates the transcription factors NF-kB and AP-1. J. Biol. Chem. 272, 14029–14032 (1997).
  CAS PubMed Google Scholar
• Chinnaiyan, A. M. et al. Signal transduction by DR3, a death domain-containing receptor related to TNFR-1 and CD95. Science 274, 990–992 (1996).
  CAS PubMed Google Scholar
• Marsters, S. et al. Apo3, a new member of the tumor necrosis factor receptor family, contains a death domain and activates apoptosis and NF-κB. Curr. Biol. 6, 1669–1676 (1996).
  CAS PubMed Google Scholar
• Pan, G. et al. Identification and functional characterization of DR6, a novel death domain-containing TNF receptor. FEBS Lett. 431, 351–356 (1998).
  CAS PubMed Google Scholar
• Gray, D. Recruitment of virgin B cells into an immune response is restricted to activation outside lymphoid follicles. Immunology 65, 73–79 (1988).
  CAS PubMed Google Scholar
• MacLennan, I. C. Germinal centers. Annu. Rev. Immunol. 12, 117–139 (1994).
  CAS PubMed Google Scholar
• Matsumoto, M. et al. Affinity maturation without germinal centres in lymphotoxin-alpha-deficient mice. Nature 382, 462–466 (1996).
  CAS PubMed Google Scholar
• Kato, J. et al. Affinity maturation in Lyn kinase-deficient mice with defective germinal center formation. J. Immunol. 160, 4788–4795 (1998).
  CAS PubMed Google Scholar
• Futterer, A., Mink, K., Luz, A., Kosco-Vilbois, M. H. & Pfeffer, K. The lymphotoxin beta receptor controls organogenesis and affinity maturation in peripheral lymphoid tissues. Immunity 9, 59–70 (1998).
  CAS PubMed Google Scholar
• Foy, T. M., Aruffo, A., Bajorath, J., Buhlmann, J. E. & Noelle, R. J. Immune regulation by CD40 and its ligand GP39. Annu. Rev. Immunol. 14, 591–617 (1996).
  CAS PubMed Google Scholar
• Han, S. et al. Cellular interaction in germinal centers. Roles of CD40 ligand and B7-2 in established germinal centers. J. Immunol. 155, 556–567 (1995).
  CAS PubMed Google Scholar
• Lenschow, D. J., Walunas, T. L. & Bluestone, J. A. CD28/B7 system of T cell costimulation. Annu. Rev. Immunol. 14, 233–258 (1996).
  CAS PubMed Google Scholar
• Lane, P. et al. B cell function in mice transgenic for mCTLA4-H gamma 1: lack of germinal centers correlated with poor affinity maturation and class switching despite normal priming of CD4+ T cells. J. Exp. Med. 179, 819–830 (1994).
  CAS PubMed Google Scholar
• Durie, F. H., Foy, T. M., Masters, S. R., Laman, J. D. & Noelle, R. J. The role of CD40 in the regulation of humoral and cell-mediated immunity. Immunol. Today 15, 406–411 (1994).
  CAS PubMed Google Scholar
• Hathcock, K. S. et al. Identification of an alternative CTLA-4 ligand costimulatory for T cell activation [see comments]. Science 262, 905–907 (1993).
  CAS PubMed Google Scholar
• Linsley, P. S. et al. Immunosuppression in vivo by a soluble form of the CTLA-4 T cell activation molecule. Science 257, 792–795 (1992).
  CAS PubMed Google Scholar
• Renshaw, B.R. et al. Humoral immune responses in CD40 ligand-deficient mice. J. Exp. Med. 180, 1889–1900 (1994).
  CAS PubMed Google Scholar
• Xu, J. et al. Mice deficient for the CD40 ligand. Immunity 1, 423–431 (1994).
  CAS PubMed Google Scholar
• Kawabe, T. et al. The immune responses in CD40-deficient mice: impaired immunoglobulin class switching and germinal center formation. Immunity 1, 167–178 (1994).
  CAS PubMed Google Scholar
• Foy, T.M. et al. gp39-CD40 interactions are essential for germinal center formation and the development of B cell memory. J. Exp. Med. 180, 157–163 (1994).
  CAS PubMed Google Scholar
• Callard, R. E., Armitage, R. J., Fanslow, W. C. & Spriggs, M.K. CD40 ligand and its role in X-linked hyper-IgM syndrome. Immunol. Today 14, 559–564 (1993).
  CAS PubMed Google Scholar
• Allen, R. C. et al. CD40 ligand gene defects responsible for X-linked hyper-IgM syndrome. Science 259, 990–993 (1993).
  CAS PubMed Google Scholar
• Aruffo, A. et al. The CD40 ligand, gp39, is defective in activated T cells from patients with X-linked hyper-IgM syndrome. Cell 72, 291–300 (1993).
  CAS PubMed Google Scholar