Apoptosis induced in normal human hepatocytes by tumor necrosis factor-related apoptosis-inducing ligand (original) (raw)

• Pitti, R.M. et al. Induction of apoptosis by Apo-2 ligand, a new member of the tumor necrosis factor cytokine family. J. Biol. Chem. 271, 12687–12690 (1996).
  Article CAS Google Scholar
• Wiley, S.R. et al. Identification and characterization of a new member of the TNF family that induces apoptosis. Immunity 3, 673–682 (1995).
  Article CAS Google Scholar
• Walczak, H. et al. Tumoricidal activity of tumor necrosis factor-related apoptosis-inducing ligand in vivo. Nature Med. 5, 157 –163 (1999).
  Article CAS Google Scholar
• Ashkenazi, A. et al. Safety and antitumor activity of recombinant soluble Apo2 ligand. J. Clin. Invest. 104, 155– 162 (1999).
  Article CAS Google Scholar
• Li, P. et al. Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade. Cell 91, 479–489 (1997).
  Article CAS Google Scholar
• Germain, M. et al. Cleavage of automodified Poly(ADP-ribose) polymerase during apoptosis. Evidence for involvement of caspase-7. J. Biol. Chem. 274, 28379–28384 ( 1999).
  Article CAS Google Scholar
• D'Amours, D., Germain, M., Orth, K., Dixit, V.M. & Poirier, G.G. Proteolysis of poly(ADP-ribose) polymerase by caspase 3: kinetics of cleavage of mono(ADP-ribosyl)ated and DNA-bound substrates . Radiat. Res. 150, 3–10 (1998).
  Article CAS Google Scholar
• Tang, D. & Kidd, V.J. Cleavage of DFF-45/ICAD by multiple caspases is essential for its function during apoptosis. J. Biol. Chem. 273, 28549–28552 ( 1998).
  Article CAS Google Scholar
• Pan, G. et al. The receptor for the cytotoxic ligand TRAIL. Science 276, 111–3 ( 1997).
  Article CAS Google Scholar
• Walczak, H. et al. TRAIL-R2: a novel apoptosis-mediating receptor for TRAIL. Embo. J. 16, 5386–5397 ( 1997).
  Article CAS Google Scholar
• Pan, G. et al. An antagonist decoy receptor and a death domain-containing receptor for TRAIL. Science 277, 815– 818 (1997).
  Article CAS Google Scholar
• Sheridan, J.P. et al. Control of TRAIL-induced apoptosis by a family of signaling and decoy receptors. Science 277, 818– 821 (1997).
  Article CAS Google Scholar
• Degli-Esposti, M.A. et al. Cloning and characterization of TRAIL-R3, a novel member of the emerging TRAIL receptor family. J. Exp. Med. 186 , 1165–1170 (1997).
  Article CAS Google Scholar
• Pan, G., Ni, J., Yu, G., Wei, Y.F. & Dixit, V.M. TRUNDD, a new member of the TRAIL receptor family that antagonizes TRAIL signalling. FEBS Lett. 424, 41–55 (1998).
  Article CAS Google Scholar
• Fiers, W. Tumor necrosis factor. Characterization at the molecular, cellular and in vivo level. FEBS Lett. 285, 199– 212 (1991).
  Article CAS Google Scholar
• Havell, E.A., Fiers, W. & North, R.J. The antitumor function of tumor necrosis factor (TNF), I. Therapeutic action of TNF against an established murine sarcoma is indirect, immunologically dependent, and limited by severe toxicity. J. Exp. Med. 167, 1067–1085 ( 1988).
  Article CAS Google Scholar
• Tanaka, M., Suda, T., Yatomi, T., Nakamura, N. & Nagata, S. Lethal effect of recombinant human Fas ligand in mice pretreated with Propionibacterium acnes. J. Immunol. 158, 2303–2309 (1997).
  CAS PubMed Google Scholar
• Ogasawara, J. et al. Lethal effect of the anti-Fas antibody in mice. Nature 364, 806–809 ( 1993); erratum 365(6446):568 ( 1993).
  Article CAS Google Scholar
• Strom, S.C. et al. Use of human hepatocytes to study P450 gene induction. Meth. Enzymol. 272, 388–401 (1996).
  Article CAS Google Scholar
• Strom, S.C., Dorko, K., Thompson, M.T., Pisarov, L.A. & Nussler, A.K. Ilots de Langerhans et Hepatocytes (eds. Franco, D., Boudjema, K. & Varet, B.) 195– 205 (Institut National de la Sante et de la Recherche Medicale, Paris, 1998).
  Google Scholar
• Nussler, A.K. et al. Isolation and characterization of a human hepatic epithelial-like cell line (AKN-1) from a normal liver. In Vitro Cell Dev. Biol. Anim. 35, 190–197 ( 1999).
  Article CAS Google Scholar
• Seol, D.W. & Billiar, T.R. A caspase-9 variant missing the catalytic site is an endogenous inhibitor of apoptosis. J. Biol. Chem. 274, 2072–2076 ( 1999).
  Article CAS Google Scholar
• Bohlinger, I. et al. DNA fragmentation in mouse organs during endotoxic shock. Am. J. Pathol. 149, 1381–1393 (1996).
  CAS PubMed PubMed Central Google Scholar
• Kothny-Wilkes, G. et al. Interleukin-1 protects transformed keratinocytes from tumor necrosis factor-related apoptosis-inducing ligand. J. Biol. Chem. 273, 29247–53 ( 1998).
  Article CAS Google Scholar