Palmitoleate attenuates palmitate-induced Bim and PUMA up-regulation and hepatocyte lipoapoptosis

J Hepatol. 2010 Apr;52(4):586-93. doi: 10.1016/j.jhep.2010.01.003. Epub 2010 Feb 13.

Abstract

Background & aims: Saturated free fatty acids induce hepatocyte lipoapoptosis. This lipotoxicity involves an endoplasmic reticulum stress response, activation of JNK, and altered expression and function of Bcl-2 proteins. The mono-unsaturated free fatty acid palmitoleate is an adipose-derived lipokine which suppresses free fatty acid-mediated lipotoxicity by unclear mechanisms. Herein we examined the mechanisms responsible for cytoprotection.

Methods: We employed isolated human and mouse primary hepatocytes, and the Huh-7 and Hep 3B cell lines for these studies. Cells were incubated in presence and absence of palmitate (16:0), stearate (18:0), and or palmitoleate (16:1, n-7).

Results: Palmitoleate significantly reduced lipoapoptosis by palmitate or stearate in both primary cells and cell lines. Palmitoleate accentuated palmitate-induced steatosis in Huh-7 cells excluding inhibition of steatosis as a mechanism for reduced apoptosis. Palmitoleate inhibited palmitate induction of the endoplasmic reticulum stress response as demonstrated by reductions in CHOP expression, eIF2-alpha phosphorylation, XBP-1 splicing, and JNK activation. Palmitate increased expression of the BH3-only proteins PUMA and Bim, which was attenuated by palmitoleate. Consistent with its inhibition of PUMA and Bim induction, palmitoleate prevented activation of the downstream death mediator Bax.

Conclusions: These data suggest palmitoleate inhibits lipoapoptosis by blocking endoplasmic reticulum stress-associated increases of the BH3-only proteins Bim and PUMA.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Apoptosis / drug effects
  • Apoptosis / physiology
  • Apoptosis Regulatory Proteins / genetics*
  • Apoptosis Regulatory Proteins / metabolism
  • Bcl-2-Like Protein 11
  • Cell Line, Tumor
  • DNA-Binding Proteins / metabolism
  • Drug Interactions
  • Endoplasmic Reticulum / physiology
  • Fatty Acids, Monounsaturated / metabolism*
  • Fatty Acids, Monounsaturated / pharmacology
  • Fatty Liver / pathology
  • Fatty Liver / physiopathology*
  • Hepatocytes / cytology
  • Hepatocytes / drug effects
  • Hepatocytes / physiology*
  • Humans
  • JNK Mitogen-Activated Protein Kinases / metabolism
  • Membrane Proteins / genetics*
  • Membrane Proteins / metabolism
  • Mice
  • Palmitates / metabolism*
  • Palmitates / pharmacology
  • Phosphorylation / drug effects
  • Phosphorylation / physiology
  • Proto-Oncogene Proteins / genetics*
  • Proto-Oncogene Proteins / metabolism
  • RNA, Messenger / metabolism
  • Regulatory Factor X Transcription Factors
  • Stress, Physiological / physiology
  • Transcription Factor CHOP / genetics
  • Transcription Factor CHOP / metabolism
  • Transcription Factors / metabolism
  • Tumor Suppressor Proteins / genetics
  • Tumor Suppressor Proteins / metabolism
  • Up-Regulation / drug effects
  • Up-Regulation / physiology
  • X-Box Binding Protein 1
  • bcl-2-Associated X Protein / metabolism

Substances

  • Apoptosis Regulatory Proteins
  • BAX protein, human
  • BBC3 protein, human
  • BCL2L11 protein, human
  • Bax protein, mouse
  • Bcl-2-Like Protein 11
  • Bcl2l11 protein, mouse
  • DDIT3 protein, human
  • DNA-Binding Proteins
  • Fatty Acids, Monounsaturated
  • Membrane Proteins
  • PUMA protein, mouse
  • Palmitates
  • Proto-Oncogene Proteins
  • RNA, Messenger
  • Regulatory Factor X Transcription Factors
  • Transcription Factors
  • Tumor Suppressor Proteins
  • X-Box Binding Protein 1
  • XBP1 protein, human
  • Xbp1 protein, mouse
  • bcl-2-Associated X Protein
  • Transcription Factor CHOP
  • ELF2 protein, human
  • palmitoleic acid
  • JNK Mitogen-Activated Protein Kinases