Abstract |
Hunter disease, an X-linked recessive lysosomal storage disorder, is caused by a deficiency in iduronate sulfatase activity. Sequence analysis of mRNA of fibroblasts of an intermediate phenotype patient showed a single C1327 to T nucleotide transition. This mutation resulted in a substitution of termination codon for normal arginine at position 443 of the peptide sequence. Expression studies with this abnormal cDNA in fibroblasts from the patient revealed a loss of enzymatic activity and instability of the mutated protein. We posturate that this mutation is probably the cause of the intermediate form of Hunter disease.
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Authors | K Sukegawa, S Tomatsu, K Tamai, M Ikeda, T Sasaki, M Masue, S Fukuda, Y Yamada, T Orii |
Journal | Biochemical and biophysical research communications
(Biochem Biophys Res Commun)
Vol. 183
Issue 2
Pg. 809-13
(Mar 16 1992)
ISSN: 0006-291X [Print] United States |
PMID | 1550586
(Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
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Chemical References |
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Topics |
- Base Sequence
- Child
- Fibroblasts
- Gene Expression
- Humans
- Iduronate Sulfatase
(genetics)
- Male
- Molecular Sequence Data
- Mucopolysaccharidosis II
(genetics)
- Mutation
(genetics)
- Pedigree
- Phenotype
- Transfection
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