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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
3
|
| pubmed:dateCreated |
1994-9-30
|
| pubmed:abstractText |
Two mutations are reported in six tyrosinemia type 1 patients from northern Europe. In four patients, a G to A transition at nucleotide position 1009 (G1009-->A) of the fumarylacetoacetase (FAH) coding sequence caused aberrant splicing by introducing an acceptor splice site within exon 12, thereby deleting the first 50 nucleotides of this exon. The following exon-intron boundary was frequently missed, and a cryptic donor splice site within intron 12 caused a partial intron 12 retention of 105 bp. This point mutation alternatively gave a glycine 337 to serine substitution in instances of correct splicing. The mutation is rapidly detected by PvuII digestion of polymerase chain reaction (PCR)-amplified genomic DNA. Another mutation, g+5-->a in the intron 12 donor splice site consensus sequence (IVS12 g+5-->a), was found in five of the patients. This caused alternative splicing with retention of the first 105 nucleotides of intron 12, exon 12 skipping, and a combined deletion of exons 12 and 13. Rapid detection of this mutation is achieved by restriction digestion of PCR-amplified genomic DNA; a mismatch primer combined with the point mutation creates a Tru9I restriction site. One patient who was homozygous for the G1009-->A mutation had a chronic form of tyrosinemia. Three patients were combined heterozygotes for G1009-->A and IVS12 g+5-->a. Their clinical phenotypes varied from acute to chronic, indicating the impact of background genes and/or external factors on the presentation of tyrosinemia type 1.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/DNA Primers,
http://linkedlifedata.com/resource/pubmed/chemical/Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Tyrosine,
http://linkedlifedata.com/resource/pubmed/chemical/fumarylacetoacetase
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Sep
|
| pubmed:issn |
0340-6717
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
94
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
235-9
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:8076937-Amino Acid Metabolism, Inborn Errors,
pubmed-meshheading:8076937-Base Sequence,
pubmed-meshheading:8076937-Child,
pubmed-meshheading:8076937-Child, Preschool,
pubmed-meshheading:8076937-DNA Primers,
pubmed-meshheading:8076937-Electrophoresis, Agar Gel,
pubmed-meshheading:8076937-Exons,
pubmed-meshheading:8076937-Female,
pubmed-meshheading:8076937-Humans,
pubmed-meshheading:8076937-Hydrolases,
pubmed-meshheading:8076937-Infant,
pubmed-meshheading:8076937-Male,
pubmed-meshheading:8076937-Molecular Sequence Data,
pubmed-meshheading:8076937-Point Mutation,
pubmed-meshheading:8076937-Polymerase Chain Reaction,
pubmed-meshheading:8076937-RNA, Messenger,
pubmed-meshheading:8076937-RNA Splicing,
pubmed-meshheading:8076937-Tyrosine
|
| pubmed:year |
1994
|
| pubmed:articleTitle |
Tyrosinemia type 1--complex splicing defects and a missense mutation in the fumarylacetoacetase gene.
|
| pubmed:affiliation |
Institute of Clinical Biochemistry, University of Oslo, Rikshospitalet, Norway.
|
| pubmed:publicationType |
Journal Article
|