Identification of a stop mutation in five Finnish patients suffering from hereditary tyrosinemia type I
Abstract
Hereditary tyrosinemia type I is a metabolic disease caused by a deficiency of fumarylacetoacetate hydrolase (FAH, EC 3.7.1.2), the last enzyme in the catabolic pathway of tyrosine. The molecular basis of FAH deficiency was examined in five Finnish patients suffering from this severe metabolic disease. No immunoreactive FAH nor enzymatic activity were found in their liver. Direct sequencing of the 14 exons of the FAH gene showed a G to A transition, which predicts a change from tryptophan to a stop codon (TGG-->TGA) at position 262 (W262X). Four of the five patients examined were homozygous for the mutation. Allele specific oligonucleotide hybridization showed a predominance of the W262X mutation in Finland (9 of 10 alleles) and the absence of this mutant allele in patients from other parts of the world. The loss of a BsaJI restriction site in those patients may be used for diagnosis.
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At least 26 different mutations in FAH have been identified in HT1 patients, including missense, nonsense, and splice consensus site mutations.
“At least 26 different mutations in FAH have been identified in HT1 patients, including missense, nonsense, and splice consensus site mutations (5, 11–17).”
From Point mutations in the murine fumarylacetoacetate hydrolase gene: Animal models for the human genetic disorder hereditary tyrosinemia type 1 (2001) · cites this paper as [14]
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The pathophysiology and treatment of hereditary tyrosinemia type 1
Grompe, M. (2001) · Seminars in Liver Disease · doi:10.1055/s-2001-19035 · Cited by 167 · see citing works
Aponte, J. L., Sega, G. A., Hauser, L. J., Dhar, M. S., Withrow, C. M., Carpenter, D. A., Rinchik, E. M., Culiat, C. T., & Johnson, D. K. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.98.2.641 · Cited by 68 · see citing works
- Authors
- St-Louis, M., Leclerc, B., Laine, J., K.Salo, M., Holmberg, C., & Tanguay, R. M.
- Affiliations
- University of Helsinki (FI)
- Corresponding author
- Tanguay, R. M.
- ORCID
- Tanguay, R. M.
- Venue
- Human Molecular Genetics
- Publisher
- Oxford University Press (OUP)
- Published
- 1994-01-01
- Volume
- 3
- Issue
- 1
- Pages
- 69-72
- ISSN
- 0964-6906 (ISSN-L)
- 1460-2083
- OpenAlex
- W2018412856
- Cited by
- 50
- References
- 0
- Citations by year
- 2024: 1 · 2021: 1 · 2020: 2 · 2019: 2 · 2018: 1 · 2017: 2 · 2014: 1 · 2013: 1 · 2012: 1
- FWCI
- 4.23
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Human Molecular Genetics (publishedVersion)
- PubMed (publishedVersion)
- HighWire Press Open Archive (submittedVersion)
- Funders
- Medical Research Council
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Metabolism and Genetic Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Amino Acid Enzymes and Metabolism
- Health Sciences › Medicine › Rheumatology › Glycogen Storage Diseases and Myoclonus
- Keywords
- tyrosinemia type I, fumarylacetoacetate hydrolase deficiency, stop codon mutation, Finnish patients, homozygous mutation, allele-specific oligonucleotide hybridization, tyrosine catabolism, molecular diagnosis
- MeSH terms
- Amino Acid Metabolism, Inborn Errors, Amino Acid Sequence, Base Sequence, Child, Preschool, Exons, Finland, Humans, Hydrolases, Infant, Liver, Molecular Sequence Data, Tyrosine, Polymerase Chain Reaction, Point Mutation, DNA Primers
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