Bile acids stimulate cFLIP phosphorylation enhancing TRAIL-mediated apoptosis

J Biol Chem. 2003 Jan 3;278(1):454-61. doi: 10.1074/jbc.M209387200. Epub 2002 Oct 28.

Abstract

Bile acids induce hepatocyte injury by enhancing death receptor-mediated apoptosis. In this study, bile acid effects on TRAIL-mediated apoptosis were examined to gain insight into bile acid potentiation of death receptor signaling. TRAIL-induced apoptosis of HuH-7 cells, stably transfected with a bile acid transporter, was enhanced by bile acids. Caspase 8 and 10 activation, bid cleavage, cytosolic cytochrome c, and caspase 3 activation by TRAIL were all increased by the bile acid glycochenodeoxycholate (GCDCA). GCDCA (100 microm) did not alter expression of TRAIL-R1/DR4, TRAIL-R2/DR5, procaspase 8, cFLIP-L, cFLIP-s, Bax, Bcl-xL, or Bax. However, both caspase 8 and caspase 10 recruitment and processing within the TRAIL death-inducing signaling complex (DISC) were greater in GCDCA-treated cells whereas recruitment of cFLIP long and short was reduced. GCDCA stimulated phosphorylation of both cFLIP isoforms, which was associated with decreased binding to GST-FADD. The protein kinase C antagonist chelerythrine prevented bile acid-stimulated cFLIP-L and -s phosphorylation, restored cFLIP binding to GST-FADD, and attenuated bile acid potentiation of TRAIL-induced apoptosis. These results provide new insights into the mechanisms of bile acid cytotoxicity and the proapoptotic effects of cFLIP phosphorylation in TRAIL signaling.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adaptor Proteins, Signal Transducing*
  • Apoptosis / physiology*
  • Apoptosis Regulatory Proteins
  • Biological Transport / physiology
  • CASP8 and FADD-Like Apoptosis Regulating Protein
  • Carrier Proteins / genetics
  • Carrier Proteins / metabolism*
  • Caspase 10
  • Caspase 8
  • Caspase 9
  • Caspase Inhibitors
  • Caspases / metabolism
  • Cell Fractionation
  • Enzyme Activation
  • Enzyme Inhibitors / metabolism*
  • Fas-Associated Death Domain Protein
  • Glycochenodeoxycholic Acid / metabolism*
  • Humans
  • Hydroxysteroid Dehydrogenases*
  • Intracellular Signaling Peptides and Proteins*
  • Membrane Glycoproteins / genetics
  • Membrane Glycoproteins / metabolism*
  • Microscopy, Fluorescence
  • Phosphorylation
  • Protein Binding
  • Protein Isoforms
  • Protein Kinase C / metabolism
  • Proto-Oncogene Proteins / metabolism
  • Proto-Oncogene Proteins c-bcl-2 / metabolism
  • Recombinant Fusion Proteins / metabolism
  • Signal Transduction / physiology
  • TNF-Related Apoptosis-Inducing Ligand
  • Tumor Cells, Cultured
  • Tumor Necrosis Factor-alpha / genetics
  • Tumor Necrosis Factor-alpha / metabolism*
  • bcl-2-Associated X Protein

Substances

  • Adaptor Proteins, Signal Transducing
  • Apoptosis Regulatory Proteins
  • BAX protein, human
  • CASP8 and FADD-Like Apoptosis Regulating Protein
  • CFLAR protein, human
  • Carrier Proteins
  • Caspase Inhibitors
  • Enzyme Inhibitors
  • FADD protein, human
  • Fas-Associated Death Domain Protein
  • Intracellular Signaling Peptides and Proteins
  • Membrane Glycoproteins
  • Protein Isoforms
  • Proto-Oncogene Proteins
  • Proto-Oncogene Proteins c-bcl-2
  • Recombinant Fusion Proteins
  • TNF-Related Apoptosis-Inducing Ligand
  • TNFSF10 protein, human
  • Tumor Necrosis Factor-alpha
  • bcl-2-Associated X Protein
  • bile acid binding proteins
  • Glycochenodeoxycholic Acid
  • Hydroxysteroid Dehydrogenases
  • AKR1C2 protein, human
  • Protein Kinase C
  • CASP8 protein, human
  • CASP9 protein, human
  • Caspase 10
  • Caspase 8
  • Caspase 9
  • Caspases
  • CASP10 protein, human