Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:3.1.6.1 (sulfatase)
3,205 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Placental steroid sulfatase deficiency is an unusual cause of low estriol production during pregnancy. Its importance lies in the differentiation of this disorder from the more ominous fetal defects that result in low estriol levels. Serum free estriol levels were found to be low or absent in a 25-year-old gravida 3, para 2 woman, while placental lactogen and chorionic gonadotropin levels were normal. An abdominal x-ray revealed no apparent congenital abnormalities and an oxytocin challenge test was negative. The dehydroepiandrosterone sulfate (DHEA-S) level in the patient's amniotic fluid was 6.8 to 18.4 times greater than those found in control amniotic fluids. The patient's amniotic fluid cortisol level was normal. Twenty-four hours following a normal, spontaneous labor and delivery at 39 weeks, the male infant underwent a synthetic ACTH1-24 stimulation test, with serum cortisols rising from 3.7 to 46 mug/dl at 1 hour. The placenta was morphologically normal on gross, light, and electron microscopic examinations. Steroid 3-alcohol sulfatase and arylsulfatase activities in the patient's placenta were virtually absent. These data indicate that this benign cause of low serum estriol levels may be diagnosed prenatally by elevated amniotic fluid DHEA-S levels.
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PMID:Prenatal diagnosis of placental steroid sulfatase deficiency. 13

The expression of steroid sulfatase (SS; sterol-sulfatase; sterol-sulfate sulfohydrolase, EC 3.1.6.2), a microsomal enzyme that catalyzes the hydrolysis of a variety of 3beta-hydroxysteroid sulfates, was evaluated in mouse-human hybrid clones. The mouse parental line, A9, was found to have little SS as determined by activity measurements. Human SS can be separated from mouse SS by electrophoresis. Two human fibroblast lines, one carrying an X/13 translocation [46,X,t(X;13)(p22;q12)] and the other carrying an X/20 translocation [46,X,t(X;20)(Xp20q;Xq20p)] were used as the human parental lines. Several independently derived hybrid clones from each of the two fusion experiments were analyzed for the expression of human SS by activity measurements and electrophoresis. Cytogenetic analyses were done on these hybrid clones at the same passage level. The results showed that the expression of human SS in these cell hybrids was concordant only with the presence of the distal half (p22-->pter) of the short arm of the human X chromosome, thus assigning the locus for SS to Xp22-->Xpter. Earlier studies have shown that the deficiency of SS is the basis for the dermatologic condition X-linked ichthyosis, the gene for which is known to be located approximately 10 centimorgans from the Xg blood group locus. The localization of SS on the X chromosome indicates that Xg locus may be on the short arm of X and possibly on its distal half. The Xg locus is thought to escape X-inactivation in man, and recent investigations suggest that the SS locus also escapes X-inactivation. Our results thus provide evidence for the location of an apparently noninactivated site on the distal half of the short arm of the human X-chromosome that contains the locus for SS and possibly the Xg locus.
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PMID:Regional assignment of the steroid sulfatase-X-linked ichthyosis locus: implications for a noninactivated region on the short arm of human X chromosome. 29 82

We report on three independent cases with a partial deficiency of placental steroid sulfatase (E.C.3.1.6.2). Upon routine pregnancy monitoring these patients were detected on the basis of low estriol excretion and failing induction of labor. In all three cases a male was delivered and subsequently the diagnosis of partial deficiency of placental steroid sulfatase was confirmed enzymatically in placenta homogenates. In one case, fibroblast cultures were established from skin explants of mother and son. In fibroblasts of the child, as in placental tissue, the activity of steroid sulfatase was only 34% of normal. Similar values were obtained for arylsulfatase C, though this enzyme is clearly separable from steroid sulfatase by electrophoresis. In cells of the mother, enzyme activities were unremarkable.
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PMID:Clinical and biochemical investigations on patients with partial deficiency of placental steroid sulfatase. 42 3

Steroid sulfatase of human placenta has been solubilized by treatment of the microsomal fraction with an amphoteric surface active agent, Miranol H2M and ultrasound. Criteria of solubility include non-sedimentation of the activity following centrifugation at 160,000 x g, its retention on Sepharose 6B and a single peak of activity after polyacrylamide gel electrophoresis. Enzyme activity was located in the same gel fractions for the two substrates tested; cholesterol sulfate and dehydroisoandrosterone sulfate. The addition of dithiothreitol was found necessary to maintain the stability of the enzyme indicating the presence of sulfhydryl groups in the molecule. A molecular weight of approximately 330,000 has been estimated from the elution volume of the enzyme system on a column of Sepharose 6B. It is believed that this protein represents a sulfatase enzyme complex composed of subunits with different specificities. From kinetic studies, a Km of 6.2 x 10(-5)M for the cleavage of dehydroisoandrosterone sulfate and a Km of 2 x 10(-6)M for the cleavage of cholesterol sulfate have been calculated.
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PMID:Solubilization and partial purification of steroid sulfatase of human placenta. 69 67

Placental steroid sulfatase deficiency is a genetic disorder only recently reported in the medical literature. Most documented cases of placental sulfatase deficiency have been marked by delay in onset of labor, lack of cervical dilatation, and relative refractoriness of oxytocic agents and amniotomy. We have studied the placenta, cultured fibroblasts, and amniotic fluid cells from an affected patient. The activities of estrone sulfatase, pregnenolone sulfatase, dehydroepiandrosterone sulfatase, and arylsulfatase C in the placenta from the patient were severely deficient. Arylsulfatases A and B were present at levels within the normal range for this tissue. Fibroblast dehydroepiandrosterone sulfatase activity was virtually absent in the patient's cells and present at normal levels in individuals with a variety of lysosomal disorders. It would thus appear that the mutation responsible for steroid sulfatase deficiency is genetically and biochemically distinct from those involved in the lysosomal sulfatase deficiency states. The cell culture studies further suggest that the defect is a generalized one which should be detectable in midtrimester of pregnancy and may have phenotypic consequences in later postnatal life.
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PMID:Steroid sulfatase deficiency. 88 10

Multiple sulfatase deficiency (MSD) is an inherited lysosomal storage disease characterized by the deficiency of at least seven sulfatases. The basic defect in MSD is thought to be in a post-translational modification common to all sulfatases. In accordance with this concept, RNAs of normal size and amount were detected in MSD fibroblasts for three sulfatases tested. cDNAs encoding arylsulfatase A, arylsulfatase B, or steroid sulfatase were introduced into MSD fibroblasts and fibroblasts with a single sulfatase deficiency by retroviral gene transfer. Infected fibroblasts overexpressed the respective sulfatase polypeptides. While in single-sulfatase-deficiency fibroblasts a concomitant increase of sulfatase activities was observed, MSD fibroblasts expressed sulfatase polypeptides with a severely diminished catalytic activity. From these results we conclude that the mutation in MSD severely decreases the capacity of a co- or post-translational process that renders sulfatases enzymatically active or prevents their premature inactivation.
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PMID:Multiple sulfatase deficiency: catalytically inactive sulfatases are expressed from retrovirally introduced sulfatase cDNAs. 134 58

Steroid sulfatase desulfates a number of 3 beta-hydroxysteroid sulfates, converting inactive steroid hormone to the active form. I have developed an enzyme-linked immunosorbent assay (ELISA) using polyclonal antibody against the sulfatase which was purified from human placenta to measure an amount of the enzyme protein in sera of gynecologic cancer patients. By this method, it was found that the serum steroid sulfatase level is significantly elevated in patients with endometrial carcinoma (p less than 0.05) and ovarian carcinoma (p less than 0.01) as compared to that of normal women. Steroid sulfatase deficiency, X-linked ichthyosis (XLI) is an inherited skin disorder. The sulfatase gene and the enzyme protein were examined in patients with XLI. When the first and last (exon 10) exons of the sulfatase gene were amplified by PCR using patients' genomic DNA as templates, no product was detected in all six cases examined. In addition, neither mRNA of the sulfatase nor the enzyme protein was detected in a patient with XLI. These observations suggest that most Japanese XLI patients are caused by an extensive deletion of the steroid sulfatase gene.
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PMID:[Biochemical study on steroid sulfatase and its clinical application to the obstetrics and gynecology]. 142 99

Several human sulfatase cDNAs have recently been cloned, revealing highly conserved domains of protein similarity. We have used this information for the isolation of sulfatase genes in different species using the polymerase chain reaction (PCR). Degenerate oligonucleotide primers corresponding to these regions of identity among human arylsulfatases A, B, and steroid sulfatase (ARSA, ARSB, and STS) were designed. The primers were used in the PCR amplification of reverse transcribed RNA (RT-PCR) from multiple tissues in human and mouse. Amplification products were obtained from mouse liver and from human liver, lymphoblasts, kidney, intestine, heart, muscle, and brain cDNA samples. Each of the PCR products was subcloned into a plasmid vector, and several subclones were characterized by colony hybridization and DNA sequencing. All the previously identified human ARSA, ARSB, and STS were found among our clones, indicating the power of the technique. Sequence analysis of two mouse clones showed high degrees of homology with the human ARSA and ARSB sequences, respectively, and likely represent the murine homologues of these enzymes. These are the first sulfatase genes isolated in the mouse. A murine equivalent for STS could not be identified, suggesting its strong diversity from the human homologue.
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PMID:The sulfatase gene family: cross-species PCR cloning using the MOPAC technique. 157 48

We describe eight patients with multiple sulfatase deficiency (MSD, or Austin's disease) who differ phenotypically from classic neonatal-, childhood-, or juvenile-onset MSD. The age of onset was in childhood. The patients presented with somatic and facial features of mucopolysaccharidosis reminiscent of Maroteaux-Lamy and Morquio syndromes. They differed from classic MSD by the presence of corneal cloudiness, macrocephaly, severe dysostosis multiplex, and gibbus and the absence of ichthyosis, retinal degeneration, severe deafness, severe mental retardation, and dementia. The main neurologic presentation was cervical cord compression due to axis abnormalities. Despite neuroradiologic evidence of white-matter changes, neurologic presentation was not like metachromatic leukodystrophy. The sulfatase deficiencies were more marked than in the classic juvenile form of MSD, but less marked than in the classic childhood-onset form of MSD. Steroid sulfatase activity was spared except in one patient. This Saudi variant of MSD accounts for 5% of all lysosomal storage diseases in the Cell Repository Registry of our Inborn Errors of Metabolism Laboratory.
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PMID:Saudi variant of multiple sulfatase deficiency. 158 9

Steroid sulfatase was purified approximately 170-fold from normal human placental microsomes and properties of the enzyme were investigated. The major steps in the purification procedure included solubilization with Triton X-100, column chromatofocusing, and hydrophobic interaction chromatography on phenylsepharose CL-4B. The purified sulfatase showed a molecular weight of 500-600 kDa on HPLC gel filtration, whereas the enzyme migrated as a molecular mass of 73 kDa on sodium dodecyl sulfate polyacrylamide gel electrophoresis. The isoelectric point of steroid sulfatase was estimated to be 6.7 by isoelectric focusing in polyacrylamide gel in the presence of 2% Triton X-100. The addition of phosphatidylcholine did not enhance the enzyme activity in the placental microsomes obtained from two patients with placental sulfatase deficiency (PSD) after solubilization and chromatofocusing. This result indicates that PSD is the result of a defect in the enzyme rather than a defect in the membrane-enzyme structure. Amino acid analysis revealed that the purified human placental sulfatase did not contain cysteine residue. The Km and Vmax values of the steroid sulfatase for dehydroepiandrosterone sulfate (DHA-S) were 7.8 microM and 0.56 nmol/min, while those for estrone sulfate (E1-S) were 50.6 microM and 0.33 nmol/min, respectively. The results of the kinetic study suggest the substrate specificity of the purified enzyme, but further studies should be done with different substrates and inhibitors.
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PMID:Purification and properties of steroid sulfatase from human placenta. 160 23


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