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© 2003 The American Society for Nutritional Sciences J. Nutr. 133:2063S-2067S, June 2003

Supplement: 2nd Amino Acid Workshop

Animal Models Reveal Pathophysiologies of Tyrosinemias1,2

Fumio Endo*,3, Yasuhiko Tanaka*, Kaede Tomoeda*, Akito Tanoue{dagger}, Gozoh Tsujimoto{dagger} and Kimitoshi Nakamura*

* Department of Pediatrics, Kumamoto University School of Medicine, Kumamoto 860-8556, Japan and {dagger} Department of Molecular and Cell Pharmacology, National Research Institute for Child Health and Development, Setagaya-ku, Tokyo 154-8567, Japan

3 To whom correspondence should be addressed. E-mail: fendo{at}gpo.kumamoto-u.ac.jp.

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.

KEY WORDS: • tyrosinemia • apoptosis • animal model mice • hereditary tyrosinemia




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