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)

The enzyme liberated by some treatments and the changes in arylsulfatase C activity in chronic hepatic damage were investigated in rat liver. 1. The enzyme activity liberated by ultrasound was the highest in the conditions studied. 2. Arylsulfatase C was assayed using p-nitrophenyl sulfate in 0.25 M Tris/acetate buffer as substrate. It is shown that this method can be used to measure arylsulfatase C activity in a mixture of arylsulfatases A and B. 3. The enzyme is mainly located in the microsomal fraction in rat liver. In toxic hepatic damage, the enzyme activity decreases from the early stage; decreasing markedly in chronic hepatic damage. The activity seems to reflect damage to the microsomes and therefore arylsulfatase C activity can be a good indicator of injury to liver microsomes.
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PMID:Degradation of arylsulfate by hepatic microsomes. 0 16

Isoelectric focusing was used to investigate the multiple forms of acid phosphatase, arylsulfatase, beta-glucuronidase, beta-galactosidase and beta-N-acetylhexosaminidase in the following, previously characterized subcellular fractions from rat kidney: a special rough microsomal fraction, enriched up to 9-fold over the homogenate in acid hydrolases; a smooth microsomal fraction; a Golgi membrane fraction enriched about 2.5-fold in acid hydrolases and 10- to 20-fold in several glycosyl transferases; and a lysosomal fraction enriched up to 25-fold in acid hydrolases. The electro-focusing behavior of the hydrolases in these fractions was markedly sensitive to the autolytic changes that occur under acidic conditions, even at 4 degrees C. Autolysis was minimized by extracting fractions in an alkaline medium (0.2% Triton X-100, 0.1 M sodium glycinate buffer, pH 10, 0.1 % p-nitrophenyloxamic acid) and adding p-nitrophenyloxamic acid (0.1 %), AN INHIBITOR OF LYSOSOMAL NEURAMINIDASE AND cathepsin D, to the pH gradient. The enzymes in the lysosomal fraction displayed a characteristic bimodal or trimodal distribution. Arylsulfatase, beta-glucuronidase and beta-N-acetylhexosaminidase occurred in an acidic form with an isoelectric point of 4.4, and a basic form with an isoelectric point of 6.2, 6.7 and 8.0, respectively. Acid phosphatase and beta-galactosidase occurred in an acidic, intermediate and basic form with isoelectric points of about 4. 1, 5.6 and 7.4, respectively. In the special rough microsomal fraction these enzymes were mostly in a basic form with isoelectric points between 7.5 and 9; these were 1-2 units higher than the corresponding basic forms in the lysosomal fraction. Treatment of extracts of the rough microsomal fraction with bacterial neuraminidase raised the isoelectric points of all five hydrolases by 1-2.5 units, indicating the presence of some N-acetylneuraminic acid residues in these basic glycoenzymes. The hydrolases in the Golgi fraction were largely in an acidic form with isoelectric points similar to or lower than those of the corresponding acidic components in the lysosomal fraction. The hydrolases in the smooth microsomal fraction showed isoelectric-focusing patterns intermediate between those in the rough microsomal and the Golgi fractions. These findings support the following scheme for the synthesis, transport and packaging of the lysosomal enzymes. Each hydrolase is synthesized in a restricted portion of the r
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PMID:Changes in electronegativity of lysosomal hydrolases during intracellular transport. An isoelectric-focusing study in subcellular fractions of rat kidney. 23 56

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

Phenobarbital was given to male rats as a single injection and as repetitive injections for 7 days. The effects of treatment on the lysosomal hydrolases acid phosphatase, cathepsin D, and aryl sulfatase were analyzed at different intervals ranging from 1 to 15 days after seven injections, and from 1 to 48 h after a single injection. In both cases, microsomal protein and NADPH-cytochrome c reductase were measured to ensure proper induction. After a single injection, a slight decrease in hydrolytic activities was observed. Repetitive administration of phenobarbital gave rise to a marked decrease of lysosomal enzyme activities 1 day after cessation of treatment. This decrease was followed by a continuous increase in activity up to day 3 and 4. One or 2 weeks after treatment, enzyme activities declined to control values. The increase in activity of lysosomal hydrolytic enzymes was correlated with the onset of induced autophagy of endoplasmic reticulum membranes described as occurring in liver upon cessation of phenobarbital exposure. It is concluded that phenobarbital treatment per se decreases lysosomal enzyme activities, whereas the induced autophagy following cessation of exposure is associated with enhanced levels of lysosomal hydrolases in rat liver.
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PMID:Induction of liver lysosomal enzymes during the autophagic phase following phenobarbital treatment of rat. 40 31

A procedure was devised for the preparation of enriched populations of subcellular organelles from homogenized bovine spleen. The fractions obtained were characterized for arylsulfatase, succinate dehydrogenase, UDPgalactosyltransferase and 5'-nucleotidase activities. The distribution of sialidase (acylneuraminyl hydrolase, EC 3.2.1.18) activity directed towards either endogenous substrate or exogenous ganglioside substrate suggests that it is enriched in the plasma membrane/microsomal fractions. Sialidase activity towards exogenous sialoglycoproteins, isolated from erythrocyte membrane, was enriched in the least dense of the plasma membrane/microsomal-containing fractions. The endogenous sialidase substrates were primarily the sialoglycolipids, hematoside and disialogangliosides. At the pH optimum, 3.8, and 37 degrees C, release of endogenous sialic acid was linear with time for 3 h. At the end of this time, 85% or more of the available endogenous substrate was hydrolyzed.
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PMID:Distribution in spleen subcellular organelles of sialidase active towards natural sialogylcolipid and sialoglycoprotein substrates. 48 91

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

Different cellular fractions of guinea-pig placenta were incubated in the presence of (7n-3H) testosterone. Microsomal aromatization of 3H-testosterone into estrone and estradiol-17beta was demonstrated in the presence of NADPH. The predominance of estrone after incubation with 17beta-hydroxylated precursors, (7n-3H) testosterone and (6,7-3H) estradiol-17beta, indicate that there is a microsomal 17beta-hydroxysteroid dehydrogenase activity. In this report, cytosolic sulfurylation of estrogens is demonstrated. This latter activity represents a quite original characteristic of the placental metabolism of estrogens in guinea-pigs. In contrast with the human placenta where there is considerable sulfatase activity, the guinea-pig placenta can sulfurylate estrogens.
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PMID:Conversion, in vitro, of (7n-3H) testosterone to estrone and estradiol-17beta and their 3-sulfate conjugate by the guinea-pig placenta. 71 21

The effects of low and high doses of three anticancer agents, cyclophosphamide, vincristine, and prednisone (given individually or in various combinations), on oxidative and conjugation pathways were studied in Sprague-Dawley male rats. Cyclophosphamide used alone at low doses decreased aniline hydroxylase and ethylmorphine demethylase activities by about 20% and at high doses produced a 30%-50% decrease in the specific activities of several microsomal mixed-function oxygenase activities, in the contents of cytochromes P-450 and b5, and in the magnitudes of type I and II drug-binding spectrum. The levels of microsomal glucouronidase, glucuronyl transferase, and sulfatase per gram of liver were also decreased (30%-50%) by the high dose of cyclophosphamide. The high dose of cyclophosphamide in conjunction with either vincristine or prednisone also produced a noticeable decrease in several activities tested; however, when cyclophosphamide was given at either low or high doses in combination with vincristine and prednisone, the activities tested were comparable to those seen in untreated controls. The mechanism of this protection is presently unknown. Vincristine, at both low and high doses, produced little effect on oxidative pathways; however, at low doses it caused a significant increase (80%) in the specific activity of hepatic microsomal sulfatase. This effect was also discernible when vincristine was given in combination with cyclophosphamide and prednisone. Other than producing a 15% decrease in liver weight and a 40% decrease in the specific activity of microsomal glucuronidase, the high dose of prednisone used had no effect on various activities tested. Results of these studies indicate a potential for drug interaction among anticancer agents and supportive drugs used in combination cancer chemotherapy.
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PMID:Studies of the effects of cyclophosphamide, vincristine, and prednisone on some hepatic oxidations and conjugations. 101 65

Hepatic microsomes and isolated hepatocytes in short term culture desulfate T3 sulfate (T3SO4). We, therefore, wished to determine whether T3SO4 could mimic the action of thyroid hormone in vitro. T3SO4 had no thyromimetic effect on the activity of Ca(2+)-ATPase in human erythrocyte membranes at doses up to 10,000 times the maximally effective dose of T3 (10(-10) mol/L). In GH4C1 pituitary cells, T3SO4 failed to displace [125I]T3 from nuclear receptors in intact cells or soluble preparations. Thus, T3SO4 was not directly thyromimetic in either an isolated human membrane system or a pituitary cell system in which nuclear receptor occupancy correlates with GH synthesis. Thyroid hormones inhibit [3H]glycosaminoglycan synthesis by cultured human dermal fibroblasts, and T3SO4 displayed about 0.5% the activity of T3 at 72 h. Human fibroblasts contained roughly the same level of microsomal p-nitrophenyl sulfatase activity as that previously observed in hepatic microsomes. Propylthiouracil (50 mumol/L) did not affect the action of T3SO4, suggesting that deiodination was not important for this activity of T3SO4. Thus, it appears T3SO4 has no intrinsic biological activity, but, under certain circumstances, may be reactivated by desulfation.
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PMID:Studies on the biological activity of triiodothyronine sulfate. 153 27

The purification and characterization of a low-molecular-mass binding protein from female guinea-pig liver cytosol is reported. Its molecular mass (14.4 kDa), amino acid composition, abundance and biological properties identify it as belonging to the Z class of liver cytosolic proteins [Levi, A.J., Gatmaitan, Z. & Arias, I.M. (1969) J. Clin. Invest. 48, 2956-2167]. Among the most important members of this class of proteins are the fatty-acid-binding proteins (FABPs) and the sterol carrier protein2 (SCP2). The guinea-pig Z protein (G-ZP) has some similarities in its amino acid composition and NH2-terminal sequence with those of the rat liver FABP, but its isoelectric point is basic (pI 8.85), like that of SCP2. We also examined its binding affinities for a number of ligands bound by these two proteins. The results show that the purified G-ZP binds dehydroepiandrosterone sulfate, estrone sulfate, oleic acid and cholesterol, but shows no affinity for free steroids such as estrone and DHEA. Thus it can be said that G-ZP has some characteristics of FABPs and some of SCP2 but seems, however, to be different from both these proteins. The purified G-ZP inhibits microsomal DHEA sulfate sulfatase activity in a mixed noncompetitive way. This protein could be involved in the transport and/or metabolism of sulfated steroids.
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PMID:Purification and characterization of a binding protein related to the Z class of cytosolic proteins in guinea-pig liver cytosol (guinea-pig Z protein). 157 97


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