Hepatic stress in hereditary tyrosinemia type 1 (HT1) activates the AKT survival pathway in the fah-/- knockout mice model

J Hepatol. 2008 Feb;48(2):308-17. doi: 10.1016/j.jhep.2007.09.014. Epub 2007 Dec 3.

Abstract

Background/aims: The AKT survival pathway is involved in a wide variety of human cancers. We investigated the implication of this pathway in hereditary tyrosinemia type 1 (HT1), a metabolic disease exhibiting hepatocellular carcinoma (HCC), despite treatment with 2-(2-nitro-4-trifluoromethylbenzoyl)-1,3-cyclohexadione (NTBC) which prevents liver damage. HT1 is an autosomal recessive disorder caused by accumulation of toxic metabolites due to a deficiency in fumarylacetoacetate hydrolase (FAH), the last enzyme in the catabolism of tyrosine.

Methods: NTBC withdrawal in the murine fah(-/-) knockout model was used to analyze in vivo the correlation between pathophysiological, biochemical and histological features consistent with hepatocarcinogenesis and activation of the AKT survival pathway.

Results: The HT1 stress initiated by NTBC discontinuation causes a progressive increase of liver and kidney pathophysiology. A stable activation of the AKT survival pathway is observed in the liver but not in kidneys of fah(-/-) mice. Hepatic survival is reinforced by inhibition of mitochondrial-mediated apoptosis through inactivation of Bad and induction of BCl-X(L) and BCl-2.

Conclusions: The chronic stress induced by liver disease in HT1 activates the AKT survival signal and inhibits intrinsic apoptosis to confer cell death resistance in vivo and favor hepatocarcinogenesis.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Carcinoma, Hepatocellular / etiology*
  • Cyclohexanones / pharmacology
  • Disease Models, Animal
  • Hydrolases / deficiency*
  • Liver Neoplasms / etiology*
  • Mice
  • Mice, Knockout
  • Nitrobenzoates / pharmacology
  • Proto-Oncogene Proteins c-akt / physiology*
  • Proto-Oncogene Proteins c-bcl-2 / physiology
  • Signal Transduction*
  • Tyrosinemias / complications
  • Tyrosinemias / metabolism*
  • bcl-X Protein / physiology

Substances

  • Bcl2l1 protein, mouse
  • Cyclohexanones
  • Nitrobenzoates
  • Proto-Oncogene Proteins c-bcl-2
  • bcl-X Protein
  • Proto-Oncogene Proteins c-akt
  • Hydrolases
  • fumarylacetoacetase
  • nitisinone