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)

The microsomal sulfatases are known to be deficient in the X-linked recessive inherited type of ichthyosis (XLI), which is closely related to the placental steroid-sulfatase deficiency. Our group demonstrated biochemically the deficiency of steroid-sulfatase activity as well as arylsulfatase C activity in cultured skin fibroblasts and leukocytes of patients with XLI, whereas all cases of ADI investigated hitherto expressed high activities of microsomal sulfatase. On the other hand, the analysis of microsomal sulfatase in membranous preparations of uncultivated skin and hair follicles failed to distinguish between XLI, ADI, and controls. Possible relations between this enzyme defect and the hyperkeratotic condition of XLI are discussed.
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PMID:[Microsomal sulfatase deficiency in X chromosome-linked ichthyosis]. 695 21

Steroid sulfatase and aryl sulfatase C activities were assayed simultaneously in peripheral blood leucocytes of 4 patients with X-linked ichthyosis (XLI) and 4 patients with autosomal-dominant ichthyosis; 11 healthy subjects served as controls. The deficiency of steroid sulfatase as well as of aryl sulfatase C found in leucocytes of patients with XLI was confirmed by the histochemical demonstration of aryl sulfatase C deficiency in skin sections. Although results are obtained earlier with the histochemical method than with the biochemical assay in leucocytes, several disadvantages brought us to the conclusion that the biochemical assay of microsomal sulfatase activity in leucocytes offers a fast and safe method for the identification of patients with XLI.
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PMID:Rapid laboratory diagnostic of X-linked ichthyosis. 695 38

The intramembranous disposition of arylsulfatase C [EC 3.1.6.1] was studied. The lack of stimulation by Triton X-100 of microsomal arylsulfatase C activity indicated the outside location of the active site of the enzyme in microsomal vesicles. The exposure of arylsulfatase C on the surface of microsomal vesicles was also suggested by the binding of antibodies against the purified enzyme to intact microsomes. However, larger amounts of the antibodies were bound to microsomes in the presence of a low concentration of Triton X-100, suggesting the presence of other antigenic sites of the enzyme not available to the antibodies in intact microsomes. The treatment of solubilized and microsome-bound arylsulfatase C with transglutaminase indicated two susceptible glutamine residues per subunit of the enzyme molecule. One of the glutamine residues was labeled with transglutaminase in intact microsomes, whereas the other one became available to transglutaminase only after the addition of Triton X-100 to microsomes. These observations suggested that endoglycosidase H-sensitive carbohydrate chains of arylsulfatase C are located in the lumen of microsomal vesicles. We conclude that microsomal arylsulfatase C is a transmembranous protein and exposed on both outer and inner surfaces of the membrane.
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PMID:Transmembranous disposition of arylsulfatase C in microsomal membranes of rat liver. 695 92

Arylsulfatases A and B were measured in the stratum corneum of four normal controls and two individuals with sex-linked ichthyosis. For arylsulfatase A, the mean delta optical density/hr/mg protein value was 1.6 for controls and 2.0 for patients, whereas for arylsulfatase B values of 1.5 for controls and 1.4 for patients were observed. Assay of arylsulfatase C in the callus of four normal controls showed a mean delta optical density/hr/100 mg callus of 0.63, whereas no or trace activity was detected in callus from four patients with x-linked ichthyosis. The assay of steroid sulfatase is best for studying microsomal sulfatase activity. Table 1 shows the activity of this enzyme in nails, callus, and hair bulbs from controls and patients with x-linked ichthyosis. No steroid sulfatase could be demonstrated in patients with x-linked ichthyosis. The values in normal controls and obligate heterozygotes are compared in Table 2. The mean value of the two groups is statistically different with P less than or equal to 0.05 using the Student t test.
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PMID:Sulfatase activity of keratinizing tissues in X-linked ichthyosis. 720 52

A new method has been developed for measuring the total covalent binding of metabolically activated compounds to cellular macromolecules. This method employs equilibrium dialysis, in the presence of the detergent sodium dodecyl sulfate (SDS), to remove unbound radiolabeled compound and its metabolites from cellular macromolecules. [14C] Bromobenzene (80 microM), [14C]aflatoxin B1 (5 microM) or 3-[14C]methylcholanthrene (100 microM) was incubated (37 degrees C) with primary hepatocytes or liver microsomes isolated from Fischer-344 rats. The covalent binding of 14C-radiolabel to hepatic or microsomal macromolecules was measured by SDS-equilibrium dialysis and compared with that measured by exhaustive extraction. After 1 h of incubation with hepatocytes or microsomes, 2--7 times more covalent binding was detected by SDS-equilibrium dialysis, than by exhaustive extraction. The radioactivity associated with these hepatic or microsomal macromolecules migrated to discrete positions on SDS-polyacrylamide disc gels. The non-dialysable radioactivity from incubations with [14C] bromobenzene could not be extracted with diethyl ether even after treatment of the dialysin with beta-glucuronidase-sulfatase or dilute acid. This was taken to indicate that the radioactivity in the dialysin did not include free bromobenzene or its metabolites, a conclusion supported by thin-layer chromatography analysis of the dialysin. The lower amount of covalent binding detected by exhaustive extraction may be related to the inability of trichloroacetic acid to quantitatively precipitate small molecular weight macromolecules. SDS-equilibrium dialysis is an easy, rapid and non-destructive technique for measuring covalent binding. The macromolecular integrity of the sample is maintained and allows further studies concerning the specificity of the covalent interactions.
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PMID:A new method for measuring covalent binding of chemicals to cellular macromolecules. 742 16

Antioxidative inhibition by protoporphyrin (PP) of peroxidative damage in lysosomes, mitochondria and microsomes of rat liver was investigated at 24 h after an intravenous administration of PP. Using a lysosome-containing (3500 x g) fraction, the release of lysosomal marker enzymes, acid phosphatase and aryl sulfatase, from lysosome which had been stimulated by L-ascorbic acid (AsA), was decreased dose-dependently, as was the inhibition of lipid peroxidation by PP in the fraction. Swelling of mitochondria induced by Fe2+ and AsA was also inhibited in the PP-injected rat. In microsomes, lipid peroxidation stimulated by AsA caused a decrease in activity of a microsomal marker enzyme, glucose 6-phosphatase, and in P450 content. The extent of the decrease by AsA, both in activity and content, was diminished in PP-administered rat liver microsomes. These results indicate that PP protects those subcellular fractions from deterioration by lipid peroxidation.
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PMID:Resistance of hepatic lysosomes, mitochondria and microsomes of protoporphyrin-administered rats to peroxidative damage. 755 Jan 33

The uterine endometria of rabbits induced into pseudopregnancy by intramuscular injection of 17 beta-estradiol, followed by intravenous injection of human chorionic gonadotropin, expressed cholesterol sulfate at a significantly high concentration. The highest concentration of cholesterol sulfate was observed 4 days after the injection of gonadotropin for formation of the corpus luteum, being 10 times higher than that in nonpregnant endometria, and 15.2% of the total cholesterol in the endometrium was converted to the sulfated form, whose percentage in nonpregnant endometrium was 3.2%. However, no significant change in the concentration of gangliosides was observed during the period of pseudopregnancy. In the pseudopregnant endometria, the activity of cholesterol sulfotransferase, a cytosolic thiol enzyme, was increased thirtyfold over that in the nonpregnant endometria, whereas cholesterol sulfate sulfatase, a microsomal enzyme, exhibited approximately one-tenth of the activity in nonpregnant endometria. Arylsulfatase C, but not arylsulfatases A and B, exhibited the same change in activity as cholesterol sulfate sulfatase. Thus, the striking increase in cholesterol sulfate after induction of pseudopregnancy was found to be due to the activation of cholesterol sulfotransferase and the simultaneous inhibition of cholesterol sulfate sulfatase.
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PMID:Pseudopregnancy-dependent accumulation of cholesterol sulfate due to up-regulation of cholesterol sulfotransferase and concurrent down-regulation of cholesterol sulfate sulfatase in the uterine endometria of rabbits. 785 87

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

To clarify the role of cholesterol sulfate (CS) in the process of epidermal differentiation in vivo, we investigated the concentration of CS and the specific activities of cholesterol sulfotransferase (CST), cholesterol sulfate sulfatase (CS sulfatase) and epidermal transglutaminase (ETG) in murine skin in the pre- and postnatal periods. In the skin at day 14 of gestation, CS was not detected with TLC and the specific activities of all the enzymes were low. However, concomitant with the formation of the multilayered structure of the epidermis (at day 16), the specific activities of CST steeply increased. Although the insoluble CS sulfatase in the microsomal fraction remained at a relatively constant level, the soluble CST in the cytosol fraction showed a 6-fold increase from day 14 to day 16, and the activity decreased continuously in the following period, reaching one forty-sixth of the maximum level at 4-months-old mice. Reflected by the increase in activity, CS was detected in fetal skin at day 15, and the concentration in epidermis significantly increased during the gestation period, reaching maximum level at day 17. Furthermore, the changes in the concentration of cholesterol sulfate were identical with those of N-(O-linoleoyl)-omega-hydroxy fatty acyl sphingosine and its glucosyl derivative in the epidermis. On the other hand, the specific activity of ETG increased after birth. Thus, the activation of CST and ETG was shown to occur separately in association with the formation of the multilayered structure and thickening of the stratum corneum, respectively.
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PMID:Programmed expression of cholesterol sulfotransferase and transglutaminase during epidermal differentiation of murine skin development. 794 2

This study deals with the development of a sensitive and simple microassay for measuring cytochrome P450IA1 and P450IIB1 activities in intact human and rat hepatocytes. The method is based on the metabolism by cells cultured in microwells of appropriate substrates at noncytotoxic concentrations (8 microM 7-ethoxyresorufin and 15 microM 7-pentoxyresorufin). After incubation of the probes with the cells, the dealkylated resorufin formed and released into culture medium was quantified. To ensure the hydrolysis of the resorufin conjugates eventually formed, culture supernatants were incubated in the microwells with beta-glucuronidase and arylsulfatase. The fluorescence was then read using a microplate fluorescence reader. A high correlation between the monooxygenase activity measured by this procedure and that measured by conventional procedures in the microsomal fraction of the same cells was found. The major advantages of this method are: (1) the small number of cells required; (2) a drastic reduction in assay time; (3) that the assay is performed in intact cells; and (4) the possibility of performing repeated assays with the same cell monolayer over a period of several days since no injury to cells is detectable during the assay. This method proved to be very convenient for studying cytochrome P450 induction by xenobiotics in primary cultures of human hepatocytes.
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PMID:A microassay for measuring cytochrome P450IA1 and P450IIB1 activities in intact human and rat hepatocytes cultured on 96-well plates. 823 78


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