Animal models reveal pathophysiologies of tyrosinemias

J Nutr. 2003 Jun;133(6 Suppl 1):2063S-2067S. doi: 10.1093/jn/133.6.2063S.

Abstract

The activity of the enzyme 4-hydroxyphenylpyruvic acid dioxygenase (HPD) is regulated by transcription factors. Mutations in the HPD locus are related to two known distinct diseases: hereditary tyrosinemia type 3 and hawkinsinuria. HPD-deficient mice are a good model with which to examine the biological effects of 4-hydroxyphenylpyruvic acid, which is a keto acid that causes no apparent visceral damage. In contrast, hereditary tyrosinemia type 1, a genetic disease caused by a deficiency of fumarylacetoacetate hydrolase (FAH), induces severe visceral injuries. Mice with FAH deficiency are lethal after birth; thus, efforts to elucidate the mechanisms of the disease process have been impeded. The use of Fah(-/-) Hpd(-/-) double-mutant mice has enabled studies on tyrosinemias, and essential features of visceral injury have been reveale.

Publication types

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

MeSH terms

  • 4-Hydroxyphenylpyruvate Dioxygenase / deficiency
  • 4-Hydroxyphenylpyruvate Dioxygenase / genetics
  • Animals
  • Disease Models, Animal*
  • Gene Expression / drug effects
  • Homogentisic Acid / pharmacology
  • Hydrolases / deficiency
  • Hydrolases / genetics
  • Liver / metabolism
  • Mice
  • Mice, Knockout
  • Mutation
  • Tyrosinemias / enzymology*

Substances

  • 4-Hydroxyphenylpyruvate Dioxygenase
  • Hydrolases
  • fumarylacetoacetase
  • Homogentisic Acid