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)

Dehydroepiandrosterone-sulfate (DHEA-S), the main secretory product of the human adrenal, requires the presence of steroid sulfatase, 3 beta-hydroxysteroid dehydrogenase/delta 5-delta 4 isomerase (3 beta-HSD), 17 beta-hydroxysteroid dehydrogenase (17 beta-HSD), 5 alpha-reductase, and aromatase to form the active androgen dihydrotestosterone (DHT) and the estrogens 17 beta-estradiol (E2) and 5-androst-ene-3 beta,17 beta-diol (delta 5-diol) in peripheral target tissues. Because humans, along with non-human primates are unique in having adrenals that secrete large amounts of DHEA-S, the present study investigated the tissue distribution of the enzymatic activity of the above-mentioned steroidogenic enzymes required for the formation of active sex steroids in the male and female rhesus monkey. Estrone and DHEA sulfatase activities were measured in all 25 tissues examined, and with the exception of the salivary glands, estrogenic and androgenic 17 beta-HSDs were present in all the tissues examined. The adrenal, small and large intestine, kidney, liver, lung, fat, testis, prostate, seminal vesicle, ovary, myometrium, and endometrium all possess the above-mentioned enzymatic activities, thus suggesting that these tissues could possibly form the biologically active steroids E2 and DHT from the adrenal precursor DHEA-S. On the other hand, the oviduct, cervix, mammary gland, heart, and skeletal muscle possess all the enzymatic activities required to synthesize E2 from DHEA-S. The present study describes the widespread tissue distribution of steroid sulfatase, 3 beta-HSD, 17 beta-HSD, 5 alpha-reductase, and aromatase activities in rhesus monkey peripheral tissues.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Widespread tissue distribution of steroid sulfatase, 3 beta-hydroxysteroid dehydrogenase/delta 5-delta 4 isomerase (3 beta-HSD), 17 beta-HSD 5 alpha-reductase and aromatase activities in the rhesus monkey. 782 1

The murine steroid sulfatase (mSTS) is a microsomal enzyme, important in steroid metabolism. In the mouse, the gene encoding mSTS is pseudoautosomal and thus escapes X-inactivation. We have purified steroid sulfatase approximately 30-fold from mouse liver microsomes and its properties have been investigated. The major steps in the purification procedure included solubilization with Triton X-100, gel filtration chromatography, DEAE-Sephadex chromatography and HPLC gel filtration chromatography. The purified sulfatase showed a relative molecular weight of 128 kDa on HPLC gel filtration, whereas the enzyme migrated as two bands of 60 and 68 kDa on sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The isoelectric point of steroid sulfatase was estimated to be 6.2 by column chromatofocusing. Polyclonal antibodies to the purified protein were prepared. An Enzyme Linked Immunosorbent Assay (ELISA) was developed using purified monospecific anti-mSTS antibodies labelled with peroxidase. The standard criteria of precision and reproducibility were satisfied. The assay was applicable to routine determination of mSTS samples in research laboratories. Differences in mSTS liver concentrations were used to identify putative alleles for the mSTS gene (Sts). Results in ELISA confirmed the polymorphism previously demonstrated for an enzymatic mSTS activity assay in two inbred mouse strains.
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PMID:Murine steroid sulfatase (mSTS): purification, characterization and measurement by ELISA. 785 78

All major enzymes involved in catecholamine synthesis and metabolism have been cloned. In addition to some genetic defects of these enzymes responsible for well-defined clinical syndromes, several enzymatic abnormalities may be due to environmental (e.g. pharmacological and nutritional) or biological (e.g. aging) factors, which may modify genome expression. The enzymes involved in catecholamine metabolism either lead to metabolites which cannot be reconverted to the parent catecholamine (such as products of monoamine oxidation and catechol-O-methylation), or metabolites, which can be reconverted to the free catecholamine from which they are generated (such as products of sulfoconjugation). Reversible sulfoconjugation is partly regulated by the recently cloned enzyme, sulfatase. The importance of this reversible step is that it reconverts inactive into biologically active catecholamines. The balance of the sulfoconjugation-deconjugation interplay may have physiological implications; in addition to catecholamine release, it may determine the availability of free catecholamines during diurnal rhythms and stress or modify their renal excretion. Circumstantial evidence, including a close homology within the aryl sulfatases and steroid sulfatase gene, the first implicated in catecholamine metabolism, the second in steroid metabolism, suggests a genetic defect of sulfatases in essential hypertension. A similar, but secondary, sulfatase defect may affect catecholamine metabolism and action in chronic renal failure.
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PMID:Clinical implications of genetic and acquired defects in catecholamine synthesis and metabolism. 798 99

To study steroid sulfatase activity in women in the field of obstetrics and gynecology, especially to differentiate carrier women with steroid sulfatase deficiency (recessive X-linked ichthyosis, RXLI) from normal women, steroid sulfatase activity was assayed in peripheral blood leukocytes from normal nonpregnant women, pregnant women, patients with RXLI, carriers of RXLI and in other normal males of different age. Steroid sulfatase activity in pmol/mg protein/min was significantly lower in patients with RXLI than in the other groups and significantly higher in the 3rd trimester pregnant women than in nonpregnant women and adult men. In addition, sulfatase activity was significantly higher in the 3rd trimester pregnant women than in fetuses. However, it was difficult to differentiate carrier women with RXLI from normal women because of considerable overlap between the two groups. The biochemical control mechanism of steroid sulfatase is the subject of further research.
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PMID:Steroid sulfatase activity in human leukocytes. 800 74

Steroid sulfatase (STS) desulfates a number of 3 beta-hydroxysteroid sulfates, converting inactive steroid hormone to the active form. We have established an enzyme-linked immunosorbent assay (ELISA) of STS by using polyclonal antibody against STS purified from human placenta to measure the amount of the enzyme protein in sera. ELISA was performed by a 'Sandwich' method using a peroxidase conjugated anti-STS IgG Fab' fragment. A range of STS of 10-1,500 ng/ml in serum was assayed by this method. When the serum STS from the patients with gynecologic carcinomas was assayed by the ELISA, the level was significantly elevated in endometrial carcinoma (P < 0.05) and ovarian carcinoma (P < 0.01), respectively, as compared with that of normal healthy women.
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PMID:Serum levels of steroid sulfatase protein in gynecologic carcinomas. 807 Jan 31

To develop an experimental model for somatic gene therapy we have tried to correct the steroid sulfatase (STS) deficiency in tissue-cultured primary epidermal keratinocytes from patients suffering from recessive X-linked ichthyosis. An efficient Epstein-Barr virus-based vector was constructed, in which full-length steroid sulfatase cDNA is located between an SV40 early promotor and processing signals. After STS gene transfer into cultured basal cells from ichthyotic skin, the cells produce large amounts of enzymatically active steroid sulfatase protein. The subpopulation of transfected cells can be made to produce approximately 100 times more STS activity than normal keratinocytes. Keratinocytes from patients suffering from recessive X-linked ichthyosis display an abnormal phenotype when developing a multilayered tissue in culture: Initially an extensive burst of keratinization is observed, followed by rapid, premature shedding and degradation of most suprabasal cell layers, leaving a culture with hyperproliferative relatively immature keratinocytes. Transfection of these immature ichthyotic cells with the functional STS construct led to an increase in the amount of retained cell material in the culture medium, indicating an increased cell maturation. It is possible to genetically label individual transfected epidermal cells with a reporter gene. Cotransfection experiments with STS and reporter gene vectors show that the cohort of transfected cells had a tendency to develop less rapidly since they became overrepresented in the smaller size classes at the same time the total population was somewhat shifted toward higher cell sizes. We interpret these results as an indication that restoration of the enzymatic activity induces a more normal maturation of the transfected keratinocytes.
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PMID:Correction of steroid sulfatase deficiency by gene transfer into basal cells of tissue-cultured epidermis from patients with recessive X-linked ichthyosis. 826 59

X-linked ichthyosis results from steroid sulfatase (STS) deficiency; 90% of affected patients have a complete deletion of the entire 146 kb STS gene on the distal X chromosome short arm (Xp22.3). In these families prenatal diagnosis and carrier testing can be completed in 2 days by hybridizing simultaneously 2 different cosmid probes labeled with fluorescein or Texas red and counterstaining interphase nuclear DNA with DAPI. An STS gene probe labeled with Texas red hybridizes specifically to the steroid sulfatase gene on the X chromosome. A second flanking probe labeled with fluorescein hybridizes to both the normal Y chromosome and normal and STS deleted X chromosomes. In this fashion the interphase nuclei of normal males, affected males, normal females, and carrier females can be distinguished unambiguously. Because normal males and carrier females each show two yellow-green fluorescein spots and one Texas red STS spot, use of this test prenatally requires determining fetal sex independently with repetitive X and Y chromosome-specific probes. This procedure can be used with lymphocytes, direct and cultured chorionic villus cells, direct and cultured amniocytes, and fibroblasts. Similar methods are anticipated to be useful for rapid diagnostic assessment of other aneuploid gene disorders.
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PMID:Prenatal in situ hybridization test for deleted steroid sulfatase gene. 836 7

This study analyzes the role of pre or postpubertal stage and sex on the steroid sulfatase activity of human leukocytes. The prepubertal female group (2-7 yrs) presented a higher sulfatase activity than the prepubertal male group (2-7 yrs, 1.99 +/- 0.64 vs 0.99 +/- 0.31 pmol/mg protein, respectively) (p < 0.001), with a female/male ratio of 2.01. The postpubertal subjects (15-40 yrs) showed an activity of 0.77 +/- 0.19 (females) vs 0.56 +2- 0.11 pmol/mg protein (males) and a female/male ratio of 1.37. Enzymatic activity of prepubertal subjects paired by sex was higher than the postpubertal individuals (females p < 0.001 and males p < 0.005). These findings show differences in the steroid sulfatase activity of pre and postpubertal groups suggesting the possible influence of hormones secreted since puberty on the expression of this enzyme.
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PMID:Comparative analysis of human steroid sulfatase activity in prepubertal and postpubertal males and females. 840 26

Nucleotides and calcium ions have been implicated in the regulation of biosynthesis of steroids, although the exact locus of calcium activity is not yet known. The administration of Ca2+ to Leydig cells increases testosterone production. Steroid sulfatase activity is reported to be enhanced by adenine nucleotides. In the present study the testicular sulfatase was evaluated in subcellular fractions by conversion of sulfate to free steroids in the presence or absence of Ca2+ and Mg2+ ions. The specific activity of the enzyme, which was located predominantly in submitochondrial fraction, showed a positive correlation with calcium, increasing 1.5-fold in the presence of 2.54 mM of calcium (62 nmol/h mg protein-1). In contrast, magnesium inhibited the enzymatic activity 1.79-fold in presence of 1.18 mM (23 nmoles/h mg protein-1). It would appear that testicular sulfatase is predominantly located in the mitochondria, which is recognized as one of the major sites of control of intracellular metabolism, and that its enzymatic activity could be modulated by calcium regulating the levels of potentially active androgens.
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PMID:Effectiveness of calcium and magnesium on testicular sulfatase activity. 847 Sep 43

The spontaneously hypertensive rat (SHR) has a Y chromosome locus that increases blood pressure. This locus requires an androgen receptor and testosterone for maximum expression. Steroid sulfatase (STS) catalyzes the conversion of steroid sulfates to their active nonconjugated form. In some mammals the steroid sulfatase locus (Sts) is on the Y chromosome, although the rat Sts is on the X chromosome. We measured STS activity levels in SHR and normotensive Wistar Kyoto (WKY) males. SHR had significantly higher STS activity in testes, adrenal gland, liver, and hypothalamus. The Km values for STS in the two strains were not significantly different; thus, activity differences were likely due to differences in enzyme amounts. STS activity was measured in the backcross strains SHR/y and SHR/a to test and/or confirm a Y chromosome influence on STS. STS activity levels in these strains were intermediate between those of SHR and WKY. Because the blood pressures of SHR/y and SHR/a were also intermediate between SHR and WKY, the STS activity could be a secondary response to the hypertension. An alternative hypotheses is that a regulatory locus in addition to the structural locus is responsible for STS activity levels, and this regulatory locus is on the rat Y chromosome. Further study is needed to discriminate between these possibilities, and until the second hypothesis can be eliminated, the Sts locus or its modifier loci remain a potential component of the Y chromosome hypertensive locus.
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PMID:Steroid sulfatase and the Y chromosome hypertensive locus of the spontaneously hypertensive rat. 853 76


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