Table of Contents Author Guidelines Submit a Manuscript
Mediators of Inflammation
Volume 2010, Article ID 182958, 11 pages
http://dx.doi.org/10.1155/2010/182958
Review Article

TNF Superfamily: A Growing Saga of Kidney Injury Modulators

1IIS- Fundación Jiménez Díaz, 28040 Madrid, Spain
2Nefrologia e Transplantação Renal, Hospital de Santa Maria, CHLN, EPE, 1600 Lisbon, Portugal
3Servicio de Nefrologia, Fundacion para la Investigacion Biomedica del Hospital Universitario La Paz, RedinREN, Instituto de Salud Carlos III, Fondos FEDER, 28046 Madrid, Spain
4Universidad Autónoma de Madrid, Madrid, Spain
5Fundación Renal íñigo Álvarez de Toledo, Madrid, Spain
6Unidad de Diálisis, Fundación Jiménez Díaz, Av Reyes Católicos 2, 28040 Madrid, Spain

Received 24 May 2010; Revised 31 August 2010; Accepted 6 September 2010

Academic Editor: F. D'Acquisto

Copyright © 2010 Maria D. Sanchez-Niño et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Linked References

  1. B. B. Aggarwal, W. J. Kohr, and P. E. Hass, “Human tumor necrosis factor: production, purification, and characterization,” The Journal of Biological Chemistry, vol. 260, no. 4, pp. 2345–2354, 1985. View at Google Scholar · View at Scopus
  2. D. Pennica, G. E. Nedwin, and J. S. Hayflick, “Human tumour necrosis factor: precursor structure, expression and homology to lymphotoxin,” Nature, vol. 312, no. 5996, pp. 724–729, 1984. View at Google Scholar · View at Scopus
  3. H.-J. Gruss and S. K. Dower, “Tumor necrosis factor ligand superfamily: involvement in the pathology of malignant lymphomas,” Blood, vol. 85, no. 12, pp. 3378–3404, 1995. View at Google Scholar · View at Scopus
  4. J.-L. Bodmer, P. Schneider, and J. Tschopp, “The molecular architecture of the TNF superfamily,” Trends in Biochemical Sciences, vol. 27, no. 1, pp. 19–26, 2002. View at Publisher · View at Google Scholar · View at Scopus
  5. B. B. Aggarwal, “Signalling pathways of the TNF superfamily: a double-edged sword,” Nature Reviews Immunology, vol. 3, no. 9, pp. 745–756, 2003. View at Publisher · View at Google Scholar · View at Scopus
  6. M. Lotz, M. Setareh, J. von Kempis, and H. Schwarz, “The nerve growth factor/tumor necrosis factor receptor family,” Journal of Leukocyte Biology, vol. 60, no. 1, pp. 1–7, 1996. View at Google Scholar · View at Scopus
  7. R. J. Armitage, “Tumor necrosis factor receptor superfamily members and their ligands,” Current Opinion in Immunology, vol. 6, no. 3, pp. 407–413, 1994. View at Publisher · View at Google Scholar · View at Scopus
  8. D. Cosman, “A family of ligands for the TNF receptor superfamily,” Stem Cells, vol. 12, no. 5, pp. 440–455, 1994. View at Google Scholar · View at Scopus
  9. T. Hehlgans and K. Pfeffer, “The intriguing biology of the tumour necrosis factor/tumour necrosis factor receptor superfamily: players, rules and the games,” Immunology, vol. 115, no. 1, pp. 1–20, 2005. View at Publisher · View at Google Scholar · View at Scopus
  10. D. Foster, J. Parrish-Novak, B. Fox, and W. Xu, “Cytokine-receptor pairing: accelerating discovery of cytokine function,” Nature Reviews Drug Discovery, vol. 3, no. 2, pp. 160–170, 2004. View at Google Scholar · View at Scopus
  11. M. G. Tansey and D. E. Szymkowski, “The TNF superfamily in 2009: new pathways, new indications, and new drugs,” Drug Discovery Today, vol. 14, no. 23-24, pp. 1082–1088, 2009. View at Publisher · View at Google Scholar
  12. A. B. Sanz, M. D. Sanchez-Niño, A. M. Ramos et al., “NF-κB in renal inflammation,” Journal of the American Society of Nephrology, vol. 21, no. 8, pp. 1254–1262, 2010. View at Publisher · View at Google Scholar
  13. S. Mas, R. Martínez-Pinna, J. L. Martín-Ventura et al., “Local non-esterified fatty acids correlate with inflammation in atheroma plaques of patients with type 2 diabetes,” Diabetes, vol. 59, no. 6, pp. 1292–1301, 2010. View at Publisher · View at Google Scholar
  14. A. Ortiz and J. Egido, “Is there a role for specific anti-TNF strategies in glomerular diseases?” Nephrology Dialysis Transplantation, vol. 10, no. 3, pp. 309–311, 1995. View at Google Scholar · View at Scopus
  15. T. Ernandez and T. N. Mayadas, “Immunoregulatory role of TNFα in inflammatory kidney diseases,” Kidney International, vol. 76, no. 3, pp. 262–276, 2009. View at Publisher · View at Google Scholar · View at Scopus
  16. D. J. MacEwan, “TNF receptor subtype signalling: differences and cellular consequences,” Cellular Signalling, vol. 14, no. 6, pp. 477–492, 2002. View at Publisher · View at Google Scholar · View at Scopus
  17. I. Gresser, D. Woodrow, and J. Moss, “Toxic effects of recombinant tumor necrosis factor in suckling mice: comparisons with interferon α/β,” American Journal of Pathology, vol. 128, no. 1, pp. 13–18, 1987. View at Google Scholar · View at Scopus
  18. A. Ortiz, C. Lorz, S. González-Cuadrado, R. Garcia Del Moral, F. O'Valle, and J. Egido, “Cytokines and Fas regulate apoptosis in murine renal interstitial fibroblasts,” Journal of the American Society of Nephrology, vol. 8, no. 12, pp. 1845–1854, 1997. View at Google Scholar · View at Scopus
  19. R. Misseri, D. R. Meldrum, C. A. Dinarello et al., “TNF-α mediates obstruction-induced renal tubular cell apoptosis and proapoptotic signaling,” American Journal of Physiology, vol. 288, no. 2, pp. F406–F411, 2005. View at Publisher · View at Google Scholar · View at Scopus
  20. K. K. Donnahoo, B. D. Shames, A. H. Harken, and D. R. Meldrum, “The role of tumor necrosis factor in renal ischemia-reperfusion injury,” Journal of Urology, vol. 162, no. 1, pp. 196–203, 1999. View at Publisher · View at Google Scholar · View at Scopus
  21. J. F. Navarro and C. Mora-Fernández, “The role of TNF-α in diabetic nephropathy: pathogenic and therapeutic implications,” Cytokine and Growth Factor Reviews, vol. 17, no. 6, pp. 441–450, 2006. View at Publisher · View at Google Scholar · View at Scopus
  22. S. B. Khan, H. T. Cook, G. Bhangal, J. Smith, F. W. K. Tam, and C. D. Pusey, “Antibody blockade of TNF-α reduces inflammation and scarring in experimental crescentic glomerulonephritis,” Kidney International, vol. 67, no. 5, pp. 1812–1820, 2005. View at Publisher · View at Google Scholar · View at Scopus
  23. J. Egido, M. Gomez-Chiarri, A. Ortiz et al., “Role of tumor necrosis factor-α in the pathogenesis of glomerular diseases,” Kidney International, Supplement, no. 39, pp. S-59–S-64, 1993. View at Google Scholar · View at Scopus
  24. G. Ramesh and W. Brian Reeves, “TNF-α mediates chemokine and cytokine expression and renal injury in cisplatin nephrotoxicity,” The Journal of Clinical Investigation, vol. 110, no. 6, pp. 835–842, 2002. View at Publisher · View at Google Scholar · View at Scopus
  25. M. A. R. C. Daemen, M. W. C. M. van de Ven, E. Heineman, and W. A. Buurman, “Involvement of endogenous interleukin-10 and tumor necrosis factor-α in renal, ischemia-reperfusion injury,” Transplantation, vol. 67, no. 6, pp. 792–800, 1999. View at Google Scholar · View at Scopus
  26. R. S. Al-Lamki, J. Wang, P. Vandenabeele et al., “TNFR1- and TNFR2-mediated signaling pathways in human kidney are cell type-specific and differentially contribute to renal injury,” The FASEB Journal, vol. 19, no. 12, pp. 1637–1645, 2005. View at Publisher · View at Google Scholar · View at Scopus
  27. K. Tsuruya, T. Ninomiya, M. Tokumoto et al., “Direct involvement of the receptor-mediated apoptotic pathways in cisplatin-induced renal tubular cell death,” Kidney International, vol. 63, no. 1, pp. 72–82, 2003. View at Publisher · View at Google Scholar · View at Scopus
  28. G. Ramesh and W. B. Reeves, “TNFR2-mediated apoptosis and necrosis in cisplatin-induced acute renal failure,” American Journal of Physiology, vol. 285, no. 4, pp. F610–F618, 2003. View at Google Scholar · View at Scopus
  29. G. Guo, J. Morrissey, R. McCracken, T. Tolley, and S. Klahr, “Role of TNFR1 and TNFR2 receptors in tubulointerstitial fibrosis of obstructive nephropathy,” American Journal of Physiology, vol. 277, no. 5, pp. F766–F772, 1999. View at Google Scholar · View at Scopus
  30. T. Zhou, C. K. Edwards III, P. Yang, Z. Wang, H. Bluethmann, and J. D. Mountz, “Greatly accelerated lymphadenopathy and autoimmune disease in lpr mice lacking tumor necrosis factor receptor I,” The Journal of Immunology, vol. 156, no. 8, pp. 2661–2665, 1996. View at Google Scholar · View at Scopus
  31. V. Vielhauer, G. Stavrakis, and T. N. Mayadas, “Renal cell-expressed TNF receptor 2, not receptor 1, is essential for the development of glomerulonephritis,” The Journal of Clinical Investigation, vol. 115, no. 5, pp. 1199–1209, 2005. View at Publisher · View at Google Scholar · View at Scopus
  32. V. Haridas, B. G. Darnay, K. Natarajan, R. Heller, and B. B. Aggarwal, “Overexpression of the p80 TNF receptor leads to TNF-dependent apoptosis, nuclear factor-κB activation, and c-Jun kinase activation,” The Journal of Immunology, vol. 160, no. 7, pp. 3152–3162, 1998. View at Google Scholar · View at Scopus
  33. M. Aringer, F. Houssiau, C. Gordon et al., “Adverse events and efficacy of TNF-α blockade with infliximab in patients with systemic lupus erythematosus: long-term follow-up of 13 patients,” Rheumatology, vol. 48, no. 11, pp. 1451–1454, 2009. View at Google Scholar
  34. M. Aringer and J. S. Smolen, “Efficacy and safety of TNF-blocker therapy in systemic lupus erythematosus,” Expert Opinion on Drug Safety, vol. 7, no. 4, pp. 411–419, 2008. View at Publisher · View at Google Scholar · View at Scopus
  35. A. Booth, L. Harper, T. Hammad et al., “Prospective study of TNFα blockade with infliximab in anti-neutrophil cytoplasmic antibody-associated systemic vasculitis,” Journal of the American Society of Nephrology, vol. 15, no. 3, pp. 717–721, 2004. View at Publisher · View at Google Scholar · View at Scopus
  36. P. Lamprecht, J. Voswinkel, T. Lilienthal et al., “Effectiveness of TNF-α blockade with infliximab in refractory Wegener's granulomatosis,” Rheumatology, vol. 41, no. 11, pp. 1303–1307, 2002. View at Google Scholar · View at Scopus
  37. M. D. Morgan, M. T. Drayson, C. O.S. Savage, and L. Harper, “Addition of infliximab to standard therapy for ANCA-associated Vasculitis,” Nephron—Clinical Practice, vol. 117, no. 2, pp. c89–c97, 2010. View at Publisher · View at Google Scholar
  38. S. Laurino, A. Chaudhry, A. Booth, G. Conte, and D. Jayne, “Prospective study of TNFα blockade with adalimumab in ANCA-associated systemic vasculitis with renal involvement,” Nephrology Dialysis Transplantation, vol. 25, no. 10, pp. 3307–3314, 2010. View at Publisher · View at Google Scholar
  39. M. Feldmann and C. D. Pusey, “Is there a role for TNF-α in anti-neutrophil cytoplasmic antibody-associated vasculitis? Lessons from other chronic inflammatory diseases,” Journal of the American Society of Nephrology, vol. 17, no. 5, pp. 1243–1252, 2006. View at Publisher · View at Google Scholar · View at Scopus
  40. D. Huugen, J. W. Cohen Tervaert, and P. Heeringa, “TNF-α bioactivity-inhibiting therapy in ANCA-associated vasculitis: clinical and experimental considerations,” Clinical Journal of the American Society of Nephrology, vol. 1, no. 5, pp. 1100–1107, 2006. View at Publisher · View at Google Scholar · View at Scopus
  41. P. J. Charles, R. J. T. Smeenk, J. De Jong, M. Feldmann, and R. N. Maini, “Assessment of antibodies to double-stranded DNA induced in rheumatoid arthritis patients following treatment with infliximab, a monoclonal antibody to tumor necrosis factor α: findings in open-label and randomized placebo-controlled trials,” Arthritis and Rheumatism, vol. 43, no. 11, pp. 2383–2390, 2000. View at Publisher · View at Google Scholar · View at Scopus
  42. M. De Bandt, J. Sibilia, X. Le Loët et al., “Systemic lupus erythematosus induced by anti-tumour necrosis factor alpha therapy: a French national survey,” Arthritis Research & Therapy, vol. 7, no. 3, pp. R545–551, 2005. View at Google Scholar · View at Scopus
  43. N. F. Crum, E. R. Lederman, and M. R. Wallace, “Infections associated with tumor necrosis factor-α antagonists,” Medicine, vol. 84, no. 5, pp. 291–302, 2005. View at Publisher · View at Google Scholar · View at Scopus
  44. O. Y. Saliu, C. Sofer, D. S. Stein, S. K. Schwander, and R. S. Wallis, “Tumor-necrosis-factor blockers: differential effects on mycobacterial immunity,” Journal of Infectious Diseases, vol. 194, no. 4, pp. 486–492, 2006. View at Publisher · View at Google Scholar · View at Scopus
  45. S. Nagata and P. Golstein, “The Fas death factor,” Science, vol. 267, no. 5203, pp. 1449–1456, 1995. View at Google Scholar · View at Scopus
  46. C. M. Trambas and G. M. Griffiths, “Delivering the kiss of death,” Nature Immunology, vol. 4, no. 5, pp. 399–403, 2003. View at Publisher · View at Google Scholar · View at Scopus
  47. M. Schulte, K. Reiss, M. Lettau et al., “ADAM10 regulates FasL cell surface expression and modulates FasL-induced cytotoxicity and activation-induced cell death,” Cell Death and Differentiation, vol. 14, no. 5, pp. 1040–1049, 2007. View at Publisher · View at Google Scholar · View at Scopus
  48. A. Ashkenazi and V. M. Dixit, “Apoptosis control by death and decoy receptors,” Current Opinion in Cell Biology, vol. 11, no. 2, pp. 255–260, 1999. View at Publisher · View at Google Scholar · View at Scopus
  49. T. Suda, H. Hashimoto, M. Tanaka, T. Ochi, and S. Nagata, “Membrane Fas ligand kills human peripheral blood T lymphocytes, and soluble fas ligand blocks the killing,” Journal of Experimental Medicine, vol. 186, no. 12, pp. 2045–2050, 1997. View at Publisher · View at Google Scholar · View at Scopus
  50. P. Schneider, N. Holler, J.-L. Bodmer et al., “Conversion of membrane-bound Fas(CD95) ligand to its soluble form is associated with downregulation of its proapoptotic activity and loss of liver toxicity,” Journal of Experimental Medicine, vol. 187, no. 8, pp. 1205–1213, 1998. View at Publisher · View at Google Scholar · View at Scopus
  51. A. Strasser, P. J. Jost, and S. Nagata, “The Many Roles of FAS Receptor Signaling in the Immune System,” Immunity, vol. 30, no. 2, pp. 180–192, 2009. View at Publisher · View at Google Scholar · View at Scopus
  52. M. E. Peter, R. C. Budd, J. Desbarats et al., “The CD95 receptor: apoptosis revisited,” Cell, vol. 129, no. 3, pp. 447–450, 2007. View at Publisher · View at Google Scholar · View at Scopus
  53. K. Miwa, M. Asano, R. Horai, Y. Iwakura, S. Nagata, and T. Suda, “Caspase 1-independent IL-1β release and inflammation induced by the apoptosis inducer Fas ligand,” Nature Medicine, vol. 4, no. 11, pp. 1287–1292, 1998. View at Publisher · View at Google Scholar · View at Scopus
  54. A. Ortiz, C. Lorz, and J. Egido, “The Fas ligand/Fas system in renal injury,” Nephrology Dialysis Transplantation, vol. 14, no. 8, pp. 1831–1834, 1999. View at Publisher · View at Google Scholar · View at Scopus
  55. M. J. Ross, S. Martinka, V. D. D'Agati, and L. A. Bruggeman, “NF-κB regulates Fas-mediated apoptosis in HIV-associated nephropathy,” Journal of the American Society of Nephrology, vol. 16, no. 8, pp. 2403–2411, 2005. View at Publisher · View at Google Scholar · View at Scopus
  56. T. Eichler, Q. Ma, C. Kelly et al., “Single and combination toxic metal exposures induce apoptosis in cultured murine podocytes exclusively via the extrinsic caspase 8 pathway,” Toxicological Sciences, vol. 90, no. 2, pp. 392–399, 2006. View at Publisher · View at Google Scholar · View at Scopus
  57. C. Wang, H. Peng, H. Tang et al., “Serum IgA1 from IgA nephropathy patients induces apoptosis in podocytes through direct and indirect pathways,” Clinical and Investigative Medicine, vol. 30, no. 6, pp. E240–E249, 2007. View at Google Scholar · View at Scopus
  58. C. Du, J. Jiang, Q. Guan et al., “Renal tubular epithelial cell self-injury through Fas/Fas ligand interaction promotes renal allograft injury,” American Journal of Transplantation, vol. 4, no. 10, pp. 1583–1594, 2004. View at Publisher · View at Google Scholar · View at Scopus
  59. C. Lorz, A. Ortiz, P. Justo et al., “Proapoptotic Fas ligand is expressed by normal kidney tubular epithelium and injured glomeruli,” Journal of the American Society of Nephrology, vol. 11, no. 7, pp. 1266–1277, 2000. View at Google Scholar · View at Scopus
  60. C. Lorz, P. Justo, A. Sanz, D. Subirá, J. Egido, and A. Ortiz, “Paracetamol-induced renal tubular injury: a role for ER stress,” Journal of the American Society of Nephrology, vol. 15, no. 2, pp. 380–389, 2004. View at Publisher · View at Google Scholar · View at Scopus
  61. P. Justo, C. Lorz, A. Sanz, J. Egido, and A. Ortiz, “Intracellular Mechanisms of Cyclosporin A-Induced Tubular Cell Apoptosis,” Journal of the American Society of Nephrology, vol. 14, no. 12, pp. 3072–3080, 2003. View at Publisher · View at Google Scholar · View at Scopus
  62. A. Ortiz, C. Lorz, and J. Egido, “New kids in the block: the role of FasL and Fas in kidney damage,” Journal of Nephrology, vol. 12, no. 3, pp. 150–158, 1999. View at Google Scholar · View at Scopus
  63. T. Tsukinoki, H. Sugiyama, R. Sunami et al., “Mesangial cell Fas ligand: upregulation in human lupus nephritis and NF-κB-mediated expression in cultured human mesangial cells,” Clinical and Experimental Nephrology, vol. 8, no. 3, pp. 196–205, 2004. View at Publisher · View at Google Scholar · View at Scopus
  64. K. H. Tan and W. Hunziker, “Compartmentalization of Fas and Fas ligand may prevent auto- or paracrine apoptosis in epithelial cells,” Experimental Cell Research, vol. 284, no. 2, pp. 283–290, 2003. View at Publisher · View at Google Scholar · View at Scopus
  65. J. G. Boonstra, F. J. van der Woude, P. C. Wever, J. C. Laterveer, M. R. Daha, and C. van Kooten, “Expression and function of Fas (CD95) on human renal tubular epithelial cells,” Journal of the American Society of Nephrology, vol. 8, no. 10, pp. 1517–1524, 1997. View at Google Scholar · View at Scopus
  66. S. González-Cuadrado, M.-J. López-Armada, C. Gómez-Guerrero et al., “Anti-Fas antibodies induce cytolysis and apoptosis in cultured human mesangial cells,” Kidney International, vol. 49, no. 4, pp. 1064–1070, 1996. View at Google Scholar · View at Scopus
  67. S. Gonzalez-Cuadrado, C. Lorz, R. García Del Moral et al., “Agonistic anti-Fas antibodies induce glomerular cell apoptosis in mice in vivo,” Kidney International, vol. 51, no. 6, pp. 1739–1746, 1997. View at Google Scholar · View at Scopus
  68. S. Khan, A. Koepke, G. Jarad et al., “Apoptosis and JNK activation are differentially regulated by Fas expression level in renal tubular epithelial cells,” Kidney International, vol. 60, no. 1, pp. 65–76, 2001. View at Publisher · View at Google Scholar · View at Scopus
  69. J. R. Schelling, N. Nkemere, J. B. Kopp, and R. P. Cleveland, “Fas-dependent fratricidal apoptosis is a mechanism of tubular epithelial cell deletion in chronic renal failure,” Laboratory Investigation, vol. 78, no. 7, pp. 813–824, 1998. View at Google Scholar · View at Scopus
  70. L. A. O Reilly, L. Tai, L. Lee et al., “Membrane-bound Fas ligand only is essential for Fas-induced apoptosis,” Nature, vol. 461, no. 7264, pp. 659–663, 2009. View at Publisher · View at Google Scholar · View at Scopus
  71. G. Jarad, B. Wang, S. Khan et al., “Fas activation induces renal tubular epithelial cell ß8 integrin expression and function in the absence of apoptosis,” The Journal of Biological Chemistry, vol. 277, no. 49, pp. 47826–47833, 2002. View at Publisher · View at Google Scholar · View at Scopus
  72. S. Nogae, M. Miyazaki, N. Kobayashi et al., “Induction of apoptosis in ischemia-reperfusion model of mouse kidney: possible involvement of Fas,” Journal of the American Society of Nephrology, vol. 9, no. 4, pp. 620–631, 1998. View at Google Scholar · View at Scopus
  73. A. Ortiz-Arduan, “Regulation of Fas and Fas ligand expression in cultured murine renal cells and in the kidney during endotoxemia,” American Journal of Physiology, vol. 271, no. 6, pp. F1193–F1201, 1996. View at Google Scholar · View at Scopus
  74. T. Matsuno, H. Sasaki, K. Nakagawa et al., “Expression of Fas/Fas ligand and apoptosis induction during renal allograft rejection,” Transplantation Proceedings, vol. 30, no. 7, pp. 2947–2949, 1998. View at Publisher · View at Google Scholar · View at Scopus
  75. J. R. Schelling and R. P. Cleveland, “Involvement of Fas-dependent apoptosis in renal tubular epithelial cell deletion in chronic renal failure,” Kidney International, vol. 56, no. 4, pp. 1313–1316, 1999. View at Publisher · View at Google Scholar · View at Scopus
  76. Y.-J. Hoi, E. Baranowska-Daca, V. Nguyen et al., “Mechanism of chronic obstructive uropathy: increased expression of apoptosis-promoting molecules,” Kidney International, vol. 58, no. 4, pp. 1481–1491, 2000. View at Publisher · View at Google Scholar · View at Scopus
  77. W. Wang, A. Tzanidis, M. Divjak, N. M. Thomson, and A. N. Stein-Oakley, “Altered signaling and regulatory mechanisms of apoptosis in focal and segmental glomerulosclerosis,” Journal of the American Society of Nephrology, vol. 12, no. 7, pp. 1422–1433, 2001. View at Google Scholar · View at Scopus
  78. E. Erkan, C. D. Garcia, L. T. Patterson et al., “Induction of renal tubular cell apoptosis in focal segmental glomerulosclerosis: roles of proteinuria and Fas-dependent pathways,” Journal of the American Society of Nephrology, vol. 16, no. 2, pp. 398–407, 2005. View at Publisher · View at Google Scholar · View at Scopus
  79. P. W. Sanders and P.-X. Wang, “Activation of the Fas/Fas ligand pathway in hypertensive renal disease in Dahl/Rapp rats,” BMC Nephrology, vol. 3, article 1, pp. 1–9, 2002. View at Publisher · View at Google Scholar · View at Scopus
  80. W.-Z. Ying, P.-X. Wang, and P. W. Sanders, “Induction of apoptosis during development of hypertensive nephrosclerosis,” Kidney International, vol. 58, no. 5, pp. 2007–2017, 2000. View at Publisher · View at Google Scholar · View at Scopus
  81. J. G. Kelly, R. N. Carpenter, and J. A. Tague, “Object classification and acoustic imaging with active sonar,” Journal of the Acoustical Society of America, vol. 91, no. 4, pp. 2073–2081, 1992. View at Google Scholar · View at Scopus
  82. P. Hamar, E. Song, G. Kökeny, A. Chen, N. Ouyang, and J. Lieberman, “Small interfering RNA targeting Fas protects mice against renal ischemia-reperfusion injury,” Proceedings of the National Academy of Sciences of the United States of America, vol. 101, no. 41, pp. 14883–14888, 2004. View at Publisher · View at Google Scholar · View at Scopus
  83. C. Du, S. Wang, H. Diao, Q. Guan, R. Zhong, and A. M. Jevnikar, “Increasing resistance of tubular epithelial cells to apoptosis by shRNA therapy ameliorates renal ischemia-reperfusion injury,” American Journal of Transplantation, vol. 6, no. 10, pp. 2256–2267, 2006. View at Publisher · View at Google Scholar · View at Scopus
  84. P. Hamar, M. Wang, M. Godó et al., “Lupus nephritis reoccurs following transplantation in the lupus prone mouse,” Lupus, vol. 19, no. 2, pp. 175–181, 2010. View at Publisher · View at Google Scholar
  85. T. Wada, A. Schwarting, K. Kinoshita et al., “Fas on renal parenchymal cells does not promote autoimmune nephritis in MRL mice,” Kidney International, vol. 55, no. 3, pp. 841–851, 1999. View at Publisher · View at Google Scholar · View at Scopus
  86. M. Fleck, E. R. Kern, T. Zhou et al., “Apoptosis mediated by Fas but not tumor necrosis factor receptor 1 prevents chronic disease in mice infected with murine cytomegalovirus,” The Journal of Clinical Investigation, vol. 102, no. 7, pp. 1431–1443, 1998. View at Google Scholar · View at Scopus
  87. H.-G. Zhang, M. Fleck, E. R. Kern et al., “Antigen presenting cells expressing Fas ligand down-modulate chronic inflammatory disease in Fas ligand-deficient mice,” The Journal of Clinical Investigation, vol. 105, no. 6, pp. 813–821, 2000. View at Google Scholar · View at Scopus
  88. K. M. Swenson, K. E. Bibo, T. Wang et al., “Fas ligand gene transfer to renal allografts in rats: effects on allograft survival,” Transplantation, vol. 65, no. 2, pp. 155–160, 1998. View at Google Scholar · View at Scopus
  89. D. Kayser, G. Einecke, K. S. Famulski et al., “Donor Fas is not necessary for T-cell-mediated rejection of mouse kidney allografts,” American Journal of Transplantation, vol. 8, no. 10, pp. 2049–2055, 2008. View at Publisher · View at Google Scholar · View at Scopus
  90. S. R. Wiley, K. Schooley, P. J. Smolak et al., “Identification and characterization of a new member of the TNF family that induces apoptosis,” Immunity, vol. 3, no. 6, pp. 673–682, 1995. View at Publisher · View at Google Scholar · View at Scopus
  91. R. M. Pitti, S. A. Marsters, S. Ruppert, C. J. Donahue, A. Moore, and A. Ashkenazi, “Induction of apoptosis by Apo-2 ligand, a new member of the tumor necrosis factor cytokine family,” The Journal of Biological Chemistry, vol. 271, no. 22, pp. 12687–12690, 1996. View at Publisher · View at Google Scholar · View at Scopus
  92. D. C. Spierings, E. G. de Vries, E. Vellenga et al., “Tissue distribution of the death ligand TRAIL and its receptors,” Journal of Histochemistry and Cytochemistry, vol. 52, no. 6, pp. 821–831, 2004. View at Publisher · View at Google Scholar · View at Scopus
  93. S.-J. Zheng, P. Wang, G. Tsabary, and Y. H. Chen, “Critical roles of TRAIL in hepatic cell death and hepatic inflammation,” The Journal of Clinical Investigation, vol. 113, no. 1, pp. 58–64, 2004. View at Publisher · View at Google Scholar · View at Scopus
  94. A. Krieg, T. Krieg, M. Wenzel et al., “TRAIL-β and TRAIL-γ two novel splice variants of the human TNF-related apoptosis-inducing ligand (TRAIL) without apoptotic potential,” British Journal of Cancer, vol. 88, no. 6, pp. 918–927, 2003. View at Publisher · View at Google Scholar · View at Scopus
  95. M. Kamachi, T. Aramaki, S. Tanimura et al., “Activation of protein phosphatase causes alternative splicing of tumor necrosis factor-related apoptosis-inducing ligand (TRAIL): potential effect on immune surveillance,” Biochemical and Biophysical Research Communications, vol. 360, no. 1, pp. 280–285, 2007. View at Publisher · View at Google Scholar · View at Scopus
  96. M. MacFarlane, M. Ahmad, S. M. Srinivasula, T. Fernandes-Alnemri, G. M. Cohen, and E. S. Alnemri, “Identification and molecular cloning of two novel receptors for the cytotoxic ligand TRAIL,” The Journal of Biological Chemistry, vol. 272, no. 41, pp. 25417–25420, 1997. View at Publisher · View at Google Scholar · View at Scopus
  97. X. D. Zhang, A. V. Franco, T. Nguyen, C. P. Gray, and P. Hersey, “Differential localization and regulation of death and decoy receptors for TNF-related apoptosis-inducing ligand (TRAIL) in human melanoma cells,” The Journal of Immunology, vol. 164, no. 8, pp. 3961–3970, 2000. View at Google Scholar · View at Scopus
  98. E. Rimondi, P. Secchiero, A. Quaroni, C. Zerbinati, S. Capitani, and G. Zauli, “Involvement of TRAIL/TRAIL-receptors in human intestinal cell differentiation,” Journal of Cellular Physiology, vol. 206, no. 3, pp. 647–654, 2006. View at Publisher · View at Google Scholar · View at Scopus
  99. J. G. Emery, P. McDonnell, M. B. Burke et al., “Osteoprotegerin is a receptor for the cytotoxic ligand TRAIL,” The Journal of Biological Chemistry, vol. 273, no. 23, pp. 14363–14367, 1998. View at Publisher · View at Google Scholar · View at Scopus
  100. W. S. Simonet, D. L. Lacey, C. R. Dunstan et al., “Osteoprotegerin: a novel secreted protein involved in the regulation of bone density,” Cell, vol. 89, no. 2, pp. 309–319, 1997. View at Google Scholar · View at Scopus
  101. A. Truneh, S. Sharma, C. Silverman et al., “Temperature-sensitive differential affinity of TRAIL for its receptors: DR5 is the highest affinity receptor,” The Journal of Biological Chemistry, vol. 275, no. 30, pp. 23319–23325, 2000. View at Publisher · View at Google Scholar · View at Scopus
  102. I. Holen, P. I. Croucher, F. C. Hamdy, and C. L. Eaton, “Osteoprotegerin (OPG) is a survival factor for human prostate cancer cells,” Cancer Research, vol. 62, no. 6, pp. 1619–1623, 2002. View at Google Scholar · View at Scopus
  103. L. B. Pritzker, M. Scatena, and C. M. Giachelli, “The role of osteoprotegerin and tumor necrosis factor-related apoptosis-inducing ligand in human microvascular endothelial cell survival,” Molecular Biology of the Cell, vol. 15, no. 6, pp. 2834–2841, 2004. View at Publisher · View at Google Scholar · View at Scopus
  104. T. Miyashita, A. Kawakami, T. Nakashima et al., “Osteoprotegerin (OPG) acts as an endogenous decoy receptor in tumour necrosis factor-related apoptosis-inducing ligand (TRAIL)-mediated apoptosis of fibroblast-like synovial cells,” Clinical and Experimental Immunology, vol. 137, no. 2, pp. 430–436, 2004. View at Publisher · View at Google Scholar · View at Scopus
  105. C. M. Shipman and P. I. Croucher, “Osteoprotegerin is a soluble decoy receptor for tumor necrosis factor-related apoptosis-inducing ligand/Apo2 ligand and can function as a paracrine survival factor for human myeloma cells,” Cancer Research, vol. 63, no. 5, pp. 912–916, 2003. View at Google Scholar · View at Scopus
  106. H. Walczak, R. E. Miller, K. Ariail et al., “Tumoricidal activity of tumor necrosis factor-related apoptosis-inducing ligand in vivo,” Nature Medicine, vol. 5, no. 2, pp. 157–163, 1999. View at Publisher · View at Google Scholar · View at Scopus
  107. X.-X. Wu, O. Ogawa, and Y. Kakehi, “TRAIL and chemotherapeutic drugs in cancer therapy,” Vitamins and Hormones, vol. 67, pp. 365–383, 2004. View at Publisher · View at Google Scholar · View at Scopus
  108. P. Marini, “Drug evaluation: lexatumumab, an intravenous human agonistic mAb targeting TRAIL receptor 2,” Current Opinion in Molecular Therapeutics, vol. 8, no. 6, pp. 539–546, 2006. View at Google Scholar · View at Scopus
  109. R. Di Pietro and G. Zauli, “Emerging non-apoptotic functions of tumor necrosis factor-related apoptosis-inducing ligand (TRAIL)/Apo2L,” Journal of Cellular Physiology, vol. 201, no. 3, pp. 331–340, 2004. View at Publisher · View at Google Scholar · View at Scopus
  110. Z.-L. Chu, T. A. McKinsey, L. Liu, J. J. Gentry, M. H. Malim, and D. W. Ballard, “Suppression of tumor necrosis factor-induced cell death by inhibitor of apoptosis c-IAP2 is under NF-κB control,” Proceedings of the National Academy of Sciences of the United States of America, vol. 94, no. 19, pp. 10057–10062, 1997. View at Publisher · View at Google Scholar · View at Scopus
  111. P. Secchiero, E. Melloni, M. Heikinheimo et al., “TRAIL regulates normal erythroid maturation through an ERK-dependent pathway,” Blood, vol. 103, no. 2, pp. 517–522, 2004. View at Publisher · View at Google Scholar · View at Scopus
  112. P. Secchiero, C. Zerbinati, E. Rimondi et al., “TRAIL promotes the survival, migration and proliferation of vascular smooth muscle cells,” Cellular and Molecular Life Sciences, vol. 61, no. 15, pp. 1965–1974, 2004. View at Google Scholar · View at Scopus
  113. C. Lorz, A. Benito-Martin, A. Boucherot et al., “The death ligand TRAIL in diabetic nephropathy,” Journal of the American Society of Nephrology, vol. 19, no. 5, pp. 904–914, 2008. View at Publisher · View at Google Scholar · View at Scopus
  114. E. Cretney, K. Takeda, H. Yagita, M. Glaccum, J. J. Peschon, and M. J. Smyth, “Increased susceptibility to tumor initiation and metastasis in TNF-related apoptosis-inducing ligand-deficient mice,” The Journal of Immunology, vol. 168, no. 3, pp. 1356–1361, 2002. View at Google Scholar · View at Scopus
  115. D. Kumar, S. Robertson, and K. D. Burns, “Evidence of apoptosis in human diabetic kidney,” Molecular and Cellular Biochemistry, vol. 259, no. 1-2, pp. 67–70, 2004. View at Publisher · View at Google Scholar · View at Scopus
  116. M. D. Sanchez-Niño, A. B. Sanz, P. Ihalmo et al., “The MIF receptor CD74 in diabetic podocyte injury,” Journal of the American Society of Nephrology, vol. 20, no. 2, pp. 353–362, 2009. View at Publisher · View at Google Scholar · View at Scopus
  117. S.-E. Lamhamedi-Cherradi, S.-J. Zheng, K. A. Maguschak, J. Peschon, and Y. H. Chen, “Defective thymocyte apoptosis and accelerated autoimmune diseases in TRAIL-/- mice,” Nature Immunology, vol. 4, no. 3, pp. 255–260, 2003. View at Publisher · View at Google Scholar · View at Scopus
  118. S.-E. Lamhamedi-Cherradi, S. Zheng, R. M. Tisch, and Y. H. Chen, “Critical roles of tumor necrosis factor-related apoptosis-inducing ligand in type 1 diabetes,” Diabetes, vol. 52, no. 9, pp. 2274–2278, 2003. View at Publisher · View at Google Scholar · View at Scopus
  119. Q.-S. Mi, D. Ly, S.-E. Lamhamedi-Cherradi et al., “Blockade of tumor necrosis factor-related apoptosis-inducing ligand exacerbates type 1 diabetes in NOD mice,” Diabetes, vol. 52, no. 8, pp. 1967–1975, 2003. View at Publisher · View at Google Scholar · View at Scopus
  120. C. Bossen, K. Ingold, A. Tardivel et al., “Interactions of tumor necrosis factor (TNF) and TNF receptor family members in the mouse and human,” The Journal of Biological Chemistry, vol. 281, no. 20, pp. 13964–13971, 2006. View at Publisher · View at Google Scholar · View at Scopus
  121. M. Nakayama, K. Ishidoh, Y. Kojima et al., “Fibroblast growth factor-inducible 14 mediates multiple pathways of TWEAK-induced cell death,” The Journal of Immunology, vol. 170, no. 1, pp. 341–348, 2003. View at Google Scholar · View at Scopus
  122. S. R. Wiley and J. A. Winkles, “TWEAK, a member of the TNF superfamily, is a multifunctional cytokine that binds the TweakR/Fn14 receptor,” Cytokine and Growth Factor Reviews, vol. 14, no. 3-4, pp. 241–249, 2003. View at Publisher · View at Google Scholar · View at Scopus
  123. R. L. Meighan-Mantha, D. K. W. Hsu, Y. Guo et al., “The mitogen-inducible Fn14 gene encodes a type I transmembrane protein that modulates fibroblast adhesion and migration,” The Journal of Biological Chemistry, vol. 274, no. 46, pp. 33166–33176, 1999. View at Publisher · View at Google Scholar · View at Scopus
  124. S. A. Marsters, J. P. Sheridan, R. M. Pitti, J. Brush, A. Goddard, and A. Ashkenazi, “Identification of a ligand for the death-domain-containing receptor Apo3,” Current Biology, vol. 8, no. 9, pp. 525–528, 1998. View at Google Scholar · View at Scopus
  125. A. Kaptein, M. Jansen, G. Dilaver et al., “Studies on the interaction between TWEAK and the death receptor WSL-1/TRAMP (DR3),” FEBS Letters, vol. 485, no. 2-3, pp. 135–141, 2000. View at Google Scholar · View at Scopus
  126. M. Nakayama, K. Ishidoh, N. Kayagaki et al., “Multiple pathways of TWEAK-induced cell death,” The Journal of Immunology, vol. 168, no. 2, pp. 734–743, 2002. View at Google Scholar · View at Scopus
  127. L. C. Bover, M. Cardó-Vila, A. Kuniyasu et al., “A previously unrecognized protein-protein interaction between TWEAK and CD163: potential biological implications,” The Journal of Immunology, vol. 178, no. 12, pp. 8183–8194, 2007. View at Google Scholar
  128. A. Ortiz, A. B. Sanz, B. M. García et al., “Considering TWEAK as a target for therapy in renal and vascular injury,” Cytokine and Growth Factor Reviews, vol. 20, no. 3, pp. 251–258, 2009. View at Publisher · View at Google Scholar · View at Scopus
  129. H.-X. Gao, S. R. Campbell, L. C. Burkly et al., “TNF-like weak inducer of apoptosis (TWEAK) induces inflammatory and proliferative effects in human kidney cells,” Cytokine, vol. 46, no. 1, pp. 24–35, 2009. View at Publisher · View at Google Scholar · View at Scopus
  130. S. Campbell, L. C. Burkly, H.-X. Gao et al., “Proinflammatory effects of Tweak/Fn14 interactions in glomerular mesangial cells,” The Journal of Immunology, vol. 176, no. 3, pp. 1889–1898, 2006. View at Google Scholar · View at Scopus
  131. A. B. Sanz, M. D. Sanchez-Niño, M. C. Izquierdo et al., “Tweak induces proliferation in renal tubular epithelium: a role in uninephrectomy induced renal hyperplasia,” Journal of Cellular and Molecular Medicine, vol. 13, no. 9, pp. 3329–3342, 2009. View at Publisher · View at Google Scholar
  132. P. Justo, A. B. Sanz, M. D. Sanchez-Niño et al., “Cytokine cooperation in renal tubular cell injury: the role of TWEAK,” Kidney International, vol. 70, no. 10, pp. 1750–1758, 2006. View at Publisher · View at Google Scholar · View at Scopus
  133. A. B. Sanz, P. Justo, M. D. Sanchez-Nino et al., “The cytokine TWEAK modulates renal tubulointerstitial inflammation,” Journal of the American Society of Nephrology, vol. 19, no. 4, pp. 695–703, 2008. View at Publisher · View at Google Scholar · View at Scopus
  134. A. B. Sanz, M. D. Sanchez-Niño, M. C. Izquierdo et al., “TWEAK activates the non-canonical NFκB pathway in murine renal tubular cells: modulation of CCL21,” PLoS ONE, vol. 5, no. 1, Article ID e8955, pp. 1–13, 2010. View at Publisher · View at Google Scholar
  135. A. B. Sanz, B. Santamaría, M. Ruiz-Ortega, J. Egido, and A. Ortiz, “Mechanisms of renal apoptosis in health and disease,” Journal of the American Society of Nephrology, vol. 19, no. 9, pp. 1634–1642, 2008. View at Publisher · View at Google Scholar · View at Scopus
  136. A. Molano, P. Lakhani, A. Aran, L. C. Burkly, J. S. Michaelson, and C. Putterman, “TWEAK stimulation of kidney resident cells in the pathogenesis of graft versus host induced lupus nephritis,” Immunology Letters, vol. 125, no. 2, pp. 119–128, 2009. View at Publisher · View at Google Scholar · View at Scopus
  137. J. Sun, W. J. Langer, K. Devish, and P. H. Lane, “Compensatory kidney growth in estrogen receptor-α null mice,” American Journal of Physiology, vol. 290, no. 2, pp. F319–F323, 2006. View at Publisher · View at Google Scholar · View at Scopus