Intermediate form of mucopolysaccharidosis type II (Hunter disease): a C1327 to T substitution in the iduronate sulfatase gene.
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.
Sukegawa
K
K
Department of Pediatrics, Gifu University School of Medicine, Japan.
Tomatsu
S
S
Tamai
K
K
Ikeda
M
M
Sasaki
T
T
Masue
M
M
Fukuda
S
S
Yamada
Y
Y
Orii
T
T
D001483:Base Sequence; D002648:Child; D005347:Fibroblasts; D015870:Gene Expression; D006801:Humans; D007066:Iduronate Sulfatase / Q000235:genetics*; D008297:Male; D008969:Molecular Sequence Data; D016532:Mucopolysaccharidosis II / Q000235:genetics*; D009154:Mutation / Q000235:genetics*; D010375:Pedigree; D010641:Phenotype; D014162:Transfection
D007066:Iduronate Sulfatase