TY - JOUR
T1 - Novel point mutations in the steroid sulfatase gene in patients with X- linked ichthyosis
T2 - Transfection analysis using the mutated genes
AU - Oyama, Noritaka
AU - Satoh, Masataka
AU - Iwatsuki, Keiji
AU - Kaneko, Fumio
N1 - Copyright:
Copyright 2017 Elsevier B.V., All rights reserved.
PY - 2000
Y1 - 2000
N2 - X-linked ichthyosis is caused by steroid sulfatase deficiency which results from abnormalities in its coding gene. The majority of X-linked ichthyosis patients (≃90%) have complete or partial deletions of the steroid sulfatase gene. In this study, we examined the mutations of the steroid sulfatase gene in two unrelated X-linked ichthyosis patients without complete deletion of the gene. Polymerase chain reaction-single-strand conformation polymorphism and direct sequencing analyses showed that each patient has a different single base pair substitution within exon 8 encoding the C-terminal half of the steroid sulfatase polypeptide. Both mutations resulted in the transversion of functional amino acids: a G→C substitution at nucleotide 1344, causing a predicted change of a glycine to an arginine, and a C→T substitution at nucleotide 1371, causing a change from a glutamine to a stop codon. In vitro steroid sulfatase cDNA expression using site-directed mutagenesis revealed that these mutations are in fact pathogenic and reflect the levels of steroid sulfatase enzyme activities in each of the X-linked ichthyosis patients.
AB - X-linked ichthyosis is caused by steroid sulfatase deficiency which results from abnormalities in its coding gene. The majority of X-linked ichthyosis patients (≃90%) have complete or partial deletions of the steroid sulfatase gene. In this study, we examined the mutations of the steroid sulfatase gene in two unrelated X-linked ichthyosis patients without complete deletion of the gene. Polymerase chain reaction-single-strand conformation polymorphism and direct sequencing analyses showed that each patient has a different single base pair substitution within exon 8 encoding the C-terminal half of the steroid sulfatase polypeptide. Both mutations resulted in the transversion of functional amino acids: a G→C substitution at nucleotide 1344, causing a predicted change of a glycine to an arginine, and a C→T substitution at nucleotide 1371, causing a change from a glutamine to a stop codon. In vitro steroid sulfatase cDNA expression using site-directed mutagenesis revealed that these mutations are in fact pathogenic and reflect the levels of steroid sulfatase enzyme activities in each of the X-linked ichthyosis patients.
KW - Genotype-phenotype correlation
KW - In vitro expression
KW - Polymerase chain reaction-single-strand conformation polymorphism
KW - Site-directed mutagenesis
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U2 - 10.1046/j.1523-1747.2000.00004.x
DO - 10.1046/j.1523-1747.2000.00004.x
M3 - Article
C2 - 10844566
AN - SCOPUS:0034045451
VL - 114
SP - 1195
EP - 1199
JO - Journal of Investigative Dermatology
JF - Journal of Investigative Dermatology
SN - 0022-202X
IS - 6
ER -