Bax inhibition protects against free fatty acid-induced lysosomal permeabilization

Am J Physiol Gastrointest Liver Physiol. 2006 Jun;290(6):G1339-46. doi: 10.1152/ajpgi.00509.2005. Epub 2006 Feb 16.

Abstract

Lysosomal permeabilization is a key feature of hepatocyte lipotoxicity, yet the mechanisms mediating this critical cellular event are unclear. This study examined the mechanisms involved in free fatty acid (FFA)-induced lysosomal permeabilization and the role of Bax, a Bcl-2 family member, in this event. Exposure of liver cells to palmitate induced Bax activation and translocation to lysosomes. Studies to suppress Bax activation either by pharmacological approaches or small interfering-RNA-mediated inhibition of Bax expression showed that lysosomal permeabilization is Bax dependent. In addition, palmitate treatment resulted in a significant decrease in Bcl-X(L), a Bax antagonist. Moreover, forced Bcl-X(L) expression blocked lysosomal permeabilization. Lysosomal permeabilization by FFA was ceramide and caspase independent. Finally, paradigms that inhibit lysosomal permeabilization also reduced apoptosis. In conclusion, these data strongly support a regulatory role for Bax in FFA-mediated lysosomal permeabilization and subsequent cell death.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Animals
  • Cell Membrane Permeability / drug effects
  • Cell Membrane Permeability / physiology
  • Cells, Cultured
  • Fatty Acids, Nonesterified / pharmacology
  • Hepatocytes / drug effects
  • Hepatocytes / physiology*
  • Lysosomes / drug effects
  • Lysosomes / physiology*
  • Male
  • Mice
  • Mice, Inbred C57BL
  • Palmitic Acid / pharmacology*
  • bcl-2-Associated X Protein / antagonists & inhibitors*
  • bcl-2-Associated X Protein / metabolism*

Substances

  • Bax protein, mouse
  • Fatty Acids, Nonesterified
  • bcl-2-Associated X Protein
  • Palmitic Acid