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PubMed1987

Linkage of the steroid sulfatase gene to the sex-reversed mutation in the mouse.

Dosage studies and the inheritance pattern of the gene for steroid sulfatase (Sts) in the mouse have previously provided indirect evidence for a functional Y-linked allele which recombines obligatorily with its X-linked allele in male meiosis. In this study, we have investigated the linkage relationship of Sts and the sex-reversed mutation (Sxr), a gene which is known to reside in the pairing region of the Y chromosome. The results clearly demonstrate that Sxr and Sts are linked in a region of obligatory recombination and Sts maps proximal to Sxr with most recombinants occurring proximal to the two genes.

Alleles↗
PubMed1987

Linkage of the murine steroid sulfatase locus, Sts, to sex reversed, Sxr: a genetic and molecular analysis.

We present genetic and molecular data demonstrating linkage of the gene for steroid sulfatase (Sts) to the mutation sex reversed (Sxr) definitively showing the existance of a functional allele for Sts mapping to the pseudoautosomal region of the mouse Y chromosome. Thus, in mouse, functional Sts genes are present in the pseudoautosomal region of both the X and Y chromosomes. This is in contrast to man where Sts has been mapped to the short arm of the X just centromeric to the pseudoautosomal region. Only a single recombinant separating Sts and Sxr was found out of 103 male meioses analyzed; double recombinants were not found between sex (Tdy), Sts and Sxr. If the rate of recombination in the pseudoautosomal region in male mice is equivalent to that in man and thus 7-10X higher than normal, then our data suggest that the distance between Sts and Sxr (or the telomere of the Y) is approximately 100-200 kb in length. Our data is in contrast to a recent report of a recombination frequency separating Sts and Sxr of as high as 6.2-9.8%.

Animals↗
PubMed1990

A long range restriction map of the distal human X chromosome short arm around the steroid sulfatase locus.

The distal short arm of the human X chromosome is of interest because it contains genes which escape X chromosome inactivation and because it is subject to frequent deletions in human patients. The steroid sulfatase gene has been particularly well studied as an example of a gene which escapes X inactivation and which is included in a number of these deletion events. For these reasons a physical map of the region around the STS gene would be of interest. We have constructed a rare cutting enzyme map of this area and have determined the position of several nearby markers with respect to STS. We have also oriented the 5' and 3' ends of the STS gene on this map and have determined the centromeric and telomeric portions of the region. Finally, we have shown that this map can be used to locate deletion breakpoints in STS deficient patients.

Arylsulfatases↗
PubMed1984

Ichthyosis vulgaris with hypogenitalism and hypogonadism: evidence for different genotypes by lipoprotein electrophoresis and steroid sulfatase testing.

We report two cases with ichthyosis vulgaris, hypogenitalism and hypogonadism. So far, little endocrinological information has been available on this association and the exact type of ichthyosis was unknown. Our first patient suffered from very severe hypergonadotropic hypogonadism, whereas the second patient showed normal levels of luteinizing hormone, but slightly elevated follicle stimulating hormone values. In lipoprotein electrophoresis we found fast moving beta-lipoproteins in the first patient and a normal electrophoretic mobility of pre- beta and beta-lipoproteins in the second patient. Correspondingly, steroid sulfatase (STS) testing revealed STS deficiency in the first patient and normal STS activity in the second patient, thus excluding X-linked recessive ichthyosis. These two different types in the association of ichthyosis with hypogenitalism and hypogonadism could not be discriminated by clinical, morphological and cytogenetic studies.

Abnormalities, Multiple↗
PubMed1987

Incidence of placental sulfatase deficiency on the mode of termination of pregnancy.

The mode of termination of pregnancy in case of placental sulfatase deficiency (PSD) has been considered in a 28-case series from our laboratory. After comparison with 75 other cases collected from the literature and also with reports concerned with normal pregnancies it appears that in the case of PSD: first, the gestation length is not increased; second, the parity of the patients has no influence on the mode of delivery; third, spontaneous vaginal delivery can occur (67.8% in our series, 43% in the literature series); fourth, the failure rate of labor, especially when induced, is higher than in a normal population; fifth, the high rate of C-section, largely due to the failure of labor, is enhanced by untimely interventions mostly in case of isolated PSD. If a pejorative incidence of PSD on the mode of delivery exists it must be at a moderate level, and intervention is unnecessary in absence of associated fetal and/or maternal complications.

Amenorrhea↗
PubMed1987

Pathochemistry, pathogenesis and enzyme replacement in multiple-sulfatase deficiency.

Multiple-sulfatase deficiency (MSD) is now considered to be heterogeneous and could be classified into three or four clinical phenotypes according to the onset of the disease: neonatal, late infantile, juvenile and possibly adult type. Neonatal-type MSD shows severe clinical involvement and practically no arylsulfatase A, B and C activities in cultured skin fibroblasts. Furthermore, arylsulfatase A activity in neonatal-type MSD was not enhanced by the addition of thiosulfate. Therefore, it is distinct from late infantile-type MSD. The degradation of 14C-sulfatide can occur in MSD-cultured skin fibroblasts and was much higher than in late infantile-type MLD. The addition of thiol protease such as leupeptin to cultured MSD skin fibroblasts enhanced arylsulfatase A activity as well as the degradation of 14C-sulfatide. This suggests that the decreased activities of arylsulfatase A is due to an acceleration of the enzyme degradation. Enzyme replacement by the addition of arylsulfatases of different sources (human liver, brain, fungus) was carried out in cultured MSD skin fibroblasts. Human enzymes of arylsulfatase A and B were mostly taken up by MSD cells rather than those of fungus origin. By the exposure to leukocytes to cultured skin fibroblasts, MSD cells corrected arylsulfatase A and B activities.

Adolescent↗
PubMed1990

Steroid sulfatase expression in human placenta: immunocytochemistry and in situ hybridization study.

Steroid sulfatase (STS), an important enzyme in the pathway of estrogen synthesis from sulfated steroid precursors, was localized to the syncytial trophoblast of human placentas during different periods of pregnancy by using a mouse monoclonal antibody and immunocytochemical techniques. Preembedding immunoelectron microscopy revealed STS immunoreactivity associated with the rough endoplasmic reticulum of the syncytial trophoblast. STS mRNA was also localized to this outermost layer of the human trophoblast. At a cellular level, both STS message and immunoreactivity seemed to be more abundant during the late first and early second trimesters than in term placentas. Although the syncytial trophoblast is known to originate from the cytotrophoblast, neither STS immunoreactivity nor STS mRNA was detected in the cytotrophoblast at any stage of placental development studied.

Arylsulfatases↗
PubMed1989

[Study on the steroid sulfatase (STS) activity in normal individuals and patients with abnormal sexual differentiation].

The STS (steroid sulfatase) gene which has been assigned to the short arm of human X chromosome (band p22) is thought to have escaped from Lyon's inactivation. For that reason, the STS enzyme activities differ between male and female according to the number of X chromosomes in cells. In this report, the STS enzyme activities were studied in different human tissues such as placentas, lymphocytes, and cultured fibroblasts of normal individuals and sex anomaly patients. Tritium labelled dehydroepiandrosterone sulfate (DHA-S) was used as the reaction substrate. The placental STS activities between normal male and female subjects showed a significant difference in spite of wide variances that were ascertained not to be the effects of methodological alterations involving enzyme purification, substrate concentration, and activity calculation (units per mg of protein or DNA). Further, lymphocytes and fibroblasts which had low levels of enzyme concentration compared with placentas, the STS enzyme activities were also significantly different between both sexes. These results confirmed that the STS gene in cells of tissue tested here seemed to be inactive at the gene level and followed the gene dosage effect to some extent. The enzyme activity was also studied in 17 patients with sex anomalies using lymphocytes and cultured fibroblasts. The cells of 45,X Turner Syndrome and of Klinefelter syndrome with 47,XXY or other karyotypes, showed slightly lower levels of enzyme activity when compared with control values of normal males or females. The enzyme activity in intersexual disturbances, especially XX male and XX true hermaphrodites, showed intermediate levels between normal male and female values. This result may give support to the concept that at least one X chromosome in these diseases is genetically abnormal due to X-Y interchanges, something that has been partly proved recently by analysis of H-Y antigen and Y-specific DNA probes. The present study on the STS enzyme activity revealed the presence of a gene dosage effect of STS gene between males and females not precise but rather rough in quantity, and it pointed out problem, some of which were related to genetic and environmental factors modifying the STS gene expression in normal individuals as well as sex anomaly patients.

Arylsulfatases↗
PubMed1977

Very low arylsulfatase A and cerebroside sulfatase activities in leukocytes of healthy members of metachromatic leukodystrophy family.

Very low levels of arylsulfatase A (ASA) have been found in the leukocytes of healthy members of a metachromatic leukodystrophy (MLD) family. The cerebroside sulfate sulfatase (CSS) activities in the same individuals are about 10% of the control level. Arguments favoring a dominant mutation different from that of classical MLD are presented. This report reinforces the relationship between the two enzymatic activities.

Age Factors↗
PubMed1990

Steroid sulfatase gene in XX males.

The human X and Y chromosomes pair and recombine at their distal short arms during male meiosis. Recent studies indicate that the majority of XX males arise as a result of an aberrant exchange between X and Y chromosomes such that the testis-determining factor gene (TDF) is transferred from a Y chromatid to an X chromatid. It has been shown that X-specific loci such as that coding for the red cell surface antigen, Xg, are sometimes lost from the X chromosome in this aberrant exchange. The steroid sulfatase functional gene (STS) maps to the distal short arm of the X chromosome proximal to XG. We have asked whether STS is affected in the aberrant X-Y interchange leading to XX males. DNA extracted from fibroblasts of seven XX males known to contain Y-specific sequences in their genomic DNA was tested for dosage of the STS gene by using a specific genomic probe. Densitometry of the autoradiograms showed that these XX males have two copies of the STS gene, suggesting that the breakpoint on the X chromosome in the aberrant X-Y interchange is distal to STS. To obtain more definitive evidence, cell hybrids were derived from the fusion of mouse cells, deficient in hypoxanthine phosphoribosyltransferase, and fibroblasts of the seven XX males. The X chromosomes in these patients could be distinguished from each other when one of three X-linked restriction-fragment-length polymorphisms was used. Hybrid clones retaining a human X chromosome containing Y-specific sequences in the absence of the normal X chromosome could be identified in six of the seven cases of XX males.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗
PubMed1978

[Preparation of iduronate sulfatase from the human placenta].

The preparation of the enzyme iduronate sulfatase from human placenta has been undertaken. The substrate O-(alpha-L-idopyranosyluronic acid 2-sulfate) (1 leads to 4)-2,5-anhydro-D-[3H]mannitol 6-sulfate was used to measure the enzymatic activity. The enzyme shows a pH optimum of 4.0 in 0.1 M sodium formiate or acetate buffer. Chromatography on DE-52 gives a 5.4 fold purification. The enzyme is inhibited by NaCl or KCl: in 20 mM salt the reaction rate was only 63% and 34% respectively. Inhibition by salt can be removed by extensive dialysis after the chromatographic step.

Humans↗
PubMed1985

Familial X-linked ichthyosis, steroid sulfatase deficiency, mental retardation, and nullisomy for Xp223-pter.

Steroid sulfatase (STS)-deficient X-linked ichthyosis was diagnosed in a man with short stature and mental retardation. His generation includes five similarly affected male members. A translocation chromosome is segregating in this Newfoundland kindred. The proband's mother and grandmother have normal skin and are of normal intelligence. From his carrier mother, the proband inherited an X short arm (Xp) to Y long arm (Yq) translocation chromosome, with the entire Y short arm and the X short arm terminal segment deleted (Xp223-pter). His cells are completely deficient in STS activity, confirming assignment of the STS locus to Xp223-pter. Effective management of his ichthyosis included treatment with 6% salicylic acid gel under plastic occlusion and removal of the scales by scrubbing.

Adult↗
PubMed1979

Arysulfatase A modulation with pH in multiple sulfatase deficiency disorder fibroblasts.

It has been observed that multiple sulfatase deficiency disorder (MSDD) fibroblasts contained from profoundly deficient to near normal amounts of arylsulfatase (ARS) A depending on the medium in which they were cultured. Our present findings show that the major factor determining the enzyme level is the pH of the medium during growth. In media which became acidic or was maintained at low pH (less than 7), the cells expressed the enzymopathy, while in high pH media (7.4), the cells produced enzyme. The high and low enzyme states were reversible. The ARS A deficiency in MSDD must, therefore, be a secondary manifestation of a mutation in another system.

Cerebroside-Sulfatase↗
PubMed1981

The genetics of the aryl sulfatase A locus.

A genetic analysis was performed in an isolate in which metachromatic leukodystrophy (MLD) and aryl sulfatase A (ASA) pseudodeficiency are relatively frequent. The frequency of matings at risk and the frequency of ASA pseudodeficiency among parents of MLD patients are compatible with allelism between the gene determining MLD and the gene determining ASA pseudodeficiency. Two independent pedigrees including MLD patients and ASA-deficient healthy individuals also fit the model of allelism.

Alleles↗
PubMed1981

Cerebroside sulfatase activator deficiency induced metachromatic leukodystrophy.

Two siblings of consanguineous parents had presented with a variety of findings indicative of juvenile metachromatic leukodystrophy (MLD). However, instead of the expected profound deficiency of arylsulfatase A (ARS A), their enzyme levels were about half-normal, and enzyme from fibroblasts had properties identical with the properties of enzyme from normal fibroblasts. Nevertheless, the hydrolysis of cerebroside sulfate by growing fibroblasts was markedly attenuated. Supplementation of the fibroblasts with cerebroside sulfatase activator normalized the response in the loading test. These results imply that the fibroblasts, and by extension the patients, are deficient in activator. Although the defective catabolism of cerebroside sulfate and the clinical manifestations in these patients mimic MLD, the molecular basis is distinct from the classical forms of the disorder.

Cerebroside-Sulfatase↗
PubMed1983

[Purification and characterization of cerebroside sulfatase activator].

Cerebroside sulfatase (CSase) activator was isolated from human liver by acetone precipitation, anion-exchange chromatography, gel filtration and polyacrylamide gel electrophoresis. The CSase activator was a heat-stable protein with an isoelectric point of 4.54. Molecular weight (Mr) of the activator was estimated as 22,000 with the gel permeation and about 8,000 by gel electrophoresis in the presence of sodium dodecyl sulfate, suggesting that the native activator is a trimer of a subunit with Mr 8,000. The CSase activator formed a complex with an equimolar amount of cerebroside sulfate (CS), when examined by gel permeation experiments. The activator also bound to galactosylceramide and GM2 ganglioside but scarcely to GM1 ganglioside, and activated to some extent beta-N-acetyl-hexosaminidase A and beta-galactosidase, although the CSase activator could be clearly distinguished from the GM1 beta-galactosidase activator so far known. Though the affinity chromatography using glycolipid ligands, the CSase activator did not recognize sulfate group of CS, but appeared to have a relatively broad specificity for lipid-linked hexose.

Amino Acids↗
PubMed1983

Evidence for a dosage effect at the X-linked steroid sulfatase locus in human tissues.

Steroid sulfatase (STS) is an X-linked enzyme whose locus escapes X inactivation in human somatic cells. STS activity was determined in human fibroblasts varying in X-chromosome number from one to four. Greater STS activity was detected in 2X cell strains when compared to 1X cell strains; however, increased STS activity was not found in 3 and 4X strains as compared with the 2X strains. Greater STS activity was also observed in female hair follicles when compared with male hair follicles. These data provide evidence of a gene dosage effect at the STS locus in human tissues.

Alleles↗
PubMed1984

The steroid sulfatase locus on structurally abnormal inactive X chromosomes is expressed.

In mammalian somatic cells, sex-chromosome dosage compensation is achieved by random inactivation of one of the two X chromosomes. The Xg blood group antigen (Xg) and steroid sulfatase (STS) loci on the distal end of the short arm of the X chromosome have been shown to escape this inactivation. However, it has been reported that on structurally abnormal inactive X chromosomes Xg and STS are inactivated. This discrepancy requires further consideration since whatever process accounts for the lack of inactivation of these loci on structurally normal, inactive X chromosomes might be anticipated to be operative on structurally abnormal, inactive X chromosomes. To investigate this issue, we examined the expression of STS activity in mouse-human somatic-cell hybrids retaining two different, deleted, inactive human X chromosomes. These studies provide evidence for lack of inactivation of STS on structurally abnormal, inactive X chromosomes.

Animals↗