Hereditary tyrosinemia type 1: novel missense, nonsense and splice consensus mutations in the human fumarylacetoacetate hydrolase gene; variability of the genotype-phenotype relationship
Abstract
The complete fumarylacetoacetate hydrolase (FAH) genotype of probands of thirteen unrelated families with hereditary tyrosinemia type 1 (HT 1) was established. The screening was performed by analysis of exons 2-14 of the FAH gene by using the polymerase chain reaction (PCR) and of the mRNA by reverse transcription/PCR. Nine different mutations were identified, of which six are novel. Three mutations involve consensus sequences for correct splicing, viz. IVS 6-1 (g-t), IVS 7-1 (g-a) and IVS 12 + 5 (g-a). Two missense mutations (C193R and G369V) and three nonsense mutations (R237X, E357X and E364X) were found. One silent mutation N232N was associated with the skipping of exon 8 from the FAH mRNA. Analysis of the effect of the respective mutations on the FAH mRNA showed a strong reduction of FAH mRNA levels in association with the nonsense mutations, and normal levels with the missense mutations. The splice consensus mutations give deletions of complete or small parts of exon sequences from the FAH mRNA. Data suggest a founder effect for several of the mutations, with a frequency for both the IVS 6-1 (g-t) and IVS 12 + 5 (g-a) mutations of approximately 30% in the HT 1 probands. No strict correlation between genotype and phenotype, i.e. the acute, subacute or chronic form of HT 1, was evident.
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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 [16]
Cites
Hereditary tyrosinemia type I: Self-induced correction of the fumarylacetoacetase defect
Kvittingen, E. A., Rootwelt, H., Brandtzaeg, P., Bergan, A., & Berger, R. (1993) · Journal of Clinical Investigation · doi:10.1172/jci116393 · Cited by 102 · cited 1× · see citing works
“It has recently been reported that variable levels of FAH enzyme activity exist in liver tissue from HT 1 patients (Kvittingen et al. 1993).”
BackgroundSelf-citationBerger, R., Van Faassen, H., Taanman, J. W., De Vries, H., & Agsteribbe, E. (1987) · Pediatric Research · doi:10.1203/00006450-198710000-00005 · Cited by 37 · see citing works
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Listening to silence and understanding nonsense: exonic mutations that affect splicing
Cartegni, L., Chew, S. L., & Krainer, A. R. (2002) · Nature Reviews Genetics · doi:10.1038/nrg775 · Cited by 2,209 · 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
- van Amstel, J. K. P., Bergman, A. J. I. W., van Beurden, E. A. C. M., Roijers, J. F. M., Peelen, T., van den Berg, I. E. T., Poll-The, B. T., Kvittingen, E. A., & Berger, R.
- Affiliations
- Wilhelmina Children's Hospital (NL)
- University of Oslo (NO)
- ORCID
- Berger, R.
- Venue
- Human Genetics
- Published
- 1996-01
- Volume
- 97
- Issue
- 1
- Pages
- 51-59
- ISSN
- 0018-7348 (ISSN-L)
- 0340-6717
- 1432-1203
- OpenAlex
- W2094840951
- Cited by
- 60
- References
- 2
- Citations by year
- 2025: 1 · 2023: 1 · 2022: 2 · 2021: 2 · 2019: 1 · 2017: 1 · 2016: 1 · 2015: 1 · 2014: 2 · 2013: 1 · 2012: 2
- FWCI
- 4.81
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Human Genetics (publishedVersion)
- PubMed (publishedVersion)
- Pure Amsterdam UMC (publishedVersion)
- Data Archiving and Networked Services (DANS) (submittedVersion)
- 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
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genomics and Rare Diseases
- Keywords
- tyrosinemia type I, fumarylacetoacetate hydrolase, novel mutations, missense mutations, nonsense mutation, splice site mutation, exon skipping, founder effect, genotype-phenotype correlation, tyrosine metabolism disorders, mRNA levels
- MeSH terms
- Alleles, Amino Acid Metabolism, Inborn Errors, Amino Acid Sequence, Base Sequence, Child, Preschool, Exons, Genotype, Humans, Hydrolases, Infant, Molecular Sequence Data, Mutation, Phenotype, RNA Splicing, RNA, Messenger, Tyrosine, Polymerase Chain Reaction, Consensus Sequence, Point Mutation, Alternative Splicing, DNA Primers
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