Bile salt-induced hepatocyte apoptosis involves epidermal growth factor receptor-dependent CD95 tyrosine phosphorylation

Gastroenterology. 2003 Sep;125(3):839-53. doi: 10.1016/s0016-5085(03)01055-2.

Abstract

Background & aims: Hydrophobic bile acids induce CD95-dependent hepatocyte apoptosis.

Methods: The mechanisms of bile acid-induced CD95 activation were studied in 24-hour cultured rat hepatocytes, in situ-perfused rat livers, and livers from bile duct-ligated rats.

Results: Within 1 minute, the proapoptotic bile salts taurolithocholate-3-sulfate and glycochenodeoxycholate induced oxidative stress and EGF receptor (EGF-R) tyrosine phosphorylation followed by rapid c-Jun-N-terminal kinase (JNK) activation. Thereafter, EGF-R associated with CD95 with subsequent CD95 tyrosine phosphorylation, CD95 membrane targeting, and death-inducing signal complex (DISC) formation. All of these responses were also triggered by taurochenodeoxycholate except that DISC formation only occurred in the presence of phosphatidylinositol 3-kinase inhibitors. No activation of EGF-R or CD95 was observed with tauroursodeoxycholate or taurocholate. Taurolithocholate-3-sulfate-induced EGF-R phosphorylation was sensitive to N-acetylcysteine (NAC) and genistein, whereas CD95/EGF-R association was inhibited by NAC, JNK, or protein kinase C inhibition but not by AG1478. However, the latter compound as well as NAC, genistein, inhibition of JNK, or protein kinase C inhibited CD95 tyrosine phosphorylation, membrane trafficking, and DISC formation.

Conclusions: Induction of apoptosis by hydrophobic bile salts involves EGF-R activation and EGF-R-dependent CD95 tyrosine phosphorylation, which triggers CD95 membrane targeting and Fas-associated death domain/caspase-8 recruitment. The latter step is apparently also controlled by phosphatidylinositol 3-kinase.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Apoptosis / drug effects*
  • Bile Acids and Salts / toxicity*
  • Cell Membrane / metabolism
  • ErbB Receptors / physiology*
  • Hepatocytes / drug effects*
  • Hepatocytes / physiology
  • JNK Mitogen-Activated Protein Kinases
  • Male
  • Mitogen-Activated Protein Kinases / metabolism
  • Oxidative Stress
  • Phosphorylation
  • Protein Transport / drug effects
  • Rats
  • Rats, Wistar
  • Tyrosine / metabolism
  • fas Receptor / metabolism*

Substances

  • Bile Acids and Salts
  • fas Receptor
  • Tyrosine
  • ErbB Receptors
  • JNK Mitogen-Activated Protein Kinases
  • Mitogen-Activated Protein Kinases