Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.1.6.1 (sulfatase)
 3,205 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A 25-year-old white female returned from West Africa with a two-year history of epidosic swelling, pruritus, and pain in a wrist, associated with peripheral eosinophilia. Serologic and immediate skin tests with Dirofilaria immitis antigen were positive, and blood smears transiently showed microfilariae of Acanthocheilonema perstans after the patient had been treated with diethylcarbamazine. Before treatment, both the serum concentration of IgE and the eosinophil content of arylsulfatase, an enzyme that selectively inactivates slow-reacting substance of anaphylaxis, were elevated; the patient's peripheral leukocytes released histamine and eosinophil chemotactic factor of anaphylaxis when challenged with D. immitis antigen. After one course of diethylcarbamazine, the clinical manifestations and abnormal in vitro immunologic results resolved. Host response to A. perstans infection appears to involve both IgE-mediated hypersensitivity and alterations in an eosinophil enzyme.
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PMID:Studies of immediate hypersensitivity in a patient with Acanthocheilonema perstans filarial infection. 107 19

Adult pregnant mice were given i.v. injections of (3H)3-methylcholanthrene (20 muCi in 1.1 mug/mouse) or (14C)3-methylcholanthrene (1.0 muCi in 48 mug/mouse). Ethanol extracts of their tissues were chromatographed on Sephadex LH-20. Three groups of 3-methylcholanthrene metabolites were obtained: one group as yet unidentified, one containing the hydrocarbon and hydroxylated derivatives, and a third consisting of conjugated metabolites from the treated adult mice and their fetuses. The conjugated metabolites in tissue and in bile were separated into two fractions; one was acted on by beta-glucuronidase and to a lesser extent by arylsulfatase, and the other was resistant to these enzymes but completely susceptible to acid hydrolysis. The hydrolysis resulted in altered chromatographic behavior characteristic of the hydroxy compounds, which also appear in tissue. The enzyme-resistant conjugates were predominant in brain, muscle, and lung, and the enzyme-labile conjugates were predominant in the kidney, liver, and bile of adult mice. These conjugated metabolites were also demonstrated in fetal mice; some appeared in the fetus as early as the thirteenth day of gestation, the most immature fetus so far examined. The resistant group was predominant in the early developmental stages of the fetus and the susceptible group was increased in the excretory organs such as the kidney, liver, and contents of the intestinal tract as the fetuses approached term. transplacental transfer of conjugated metabolites from the mother to the fetus did not take place, although the parent 3-methylcholanthrene and its nonconjugated metabolites were transferred. We therefore assume that drug-metabolizing enzymes, including hydroxylases and conjugases, are active in the fetal mouse tissues as well as in the adult.
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PMID:Chromatographic analyses of 3-methylcholanthrene metabolism in adult and fetal mice and the occurrence of conjugating enzymes in the fetus. 111 25

In Klebsiella aerogenes, arylsulfatase synthesis was repressed by inorganic sulfate, sulfite, sulfide, thiosulfate, and cysteine, but not by methionine under normal growth conditions. We isolated cysteine-requiring mutants (Cys minus), and mutants (AtsS minus, AtsR minus) in which the regulation of arylsulfatase synthesis was altered. In the cysteine auxotroph, enzyme synthesis was also repressed by inorganic sulfate or cysteine. Kinetic studies on mutants of the cysteine auxotroph showed that inorganic sulfate repressed arylsulfatase synthesis and that this was not due to cysteine formed by reduction of sulfate. Arylsulfatase synthesis in the AtsS minus mutant was not repressed by inorganic sulfate but was repressed by cysteine. This mutant strain had a normal level of inorganic sulfate transport. Another mutant strain, defective in the inorganic sulfate transport system, synthesized arylsulfatase in the presence of inorganic sulfate but not in the presence of cysteine. The AtsS minus mutant could synthesize the enzyme in the presence of inorganic sulfate but not cysteine. The AtsR minus mutant could synthesize the enzyme in the presence of either inorganic sulfate or cysteine. These results suggest that there are two independent functional corepressors of arylsulfatase synthesis in K. aerogenes.
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PMID:Regulation of arylsulfatase synthesis by sulfur compounds in Klebsiella aerogenes. 111 90

The green algae Chlamydomonas reinhardti synthesizes arylsulfatase (arylsulfate sulfohydrolase EC 3.1.6.1) by derepression when the concentration of SO4-2-minus in the growth medium is less than about 5-10-minus 5 M. The following observations indicate that the arylsulfatase enzyme is stable while its mRNA was unstable: (1) The increase in enzyme activity stopped and remained constant after addition of cycloheximide to derepressed cells. (2) After readdition of SO4-2-minus the increase in enzyme activity continued at a lower rate whereafter it remained constant. (3) No decay of radioactivity was observed after readdition of SO4 2-minus in labelled enzyme protein isolated from pulse-labelled --S cells. The maximum rate of arylsulfatase synthesis. Measurements of this capacity in cells taken at different developmental stages from a selection synchronous and from a light-dark synchronized culture showed that: (1) Arylsulfatase was derepressible at all stages of the life cycle. (2) The same periodic capacity patterns were found, both with the synchronized and the synchronous cells. Furthermore, the rate of accummulation of RNA and protein changed in the same periodic manner during the life cycle as did the enzyme capacity.
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PMID:The capacity for arylsulfatase synthesis in synchronous and synchronized cultures of Chlamydomonas reinhardti. 113 60

After injection of Triton WR 1339 and dextran into mice, phagolysosomes containing both compounds were obtained from the liver regardless of the order of injection of these materials. This suggests that phagososomes containing the other material. The recoveries of various lysosomal enzymes differed in phagolysosomes after injection of Triton WR 1339 with or without dextran: recoveries of beta-glucuronidase, beta-N-acetylglucosaminidase and arylsulfatase were high, and that of acid phosphatase was low.
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PMID:Formation of phagolysosomes containing dextran and Triton WR 1339 in mouse liver. 113 62

The effects of various compounds on ascorbate-2-sulfate sulfohydrolase and arylsulfatase (EC 3.1.6.1) activities in the copurified preparation from the liver of Charonia lampas were investigated. The former activity was competively inhibited by inorganic phosphate and sulfate. The latter was not affected by sulfate. Higher concentrations of sodium chloride inhibited the former and activated the latter. Neither of the activities was inhibited by sulfhydryl reagents. Both activities were competively inhibited by the other substrate.
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PMID:Effects of various compounds on the ascorbate-2-sulfate sulfohydrolase and arylsulfatase activities copurified from the liver of Charonia lampas. 115 Jun 40

Chronic exposure of rats to 10% aerosols of papain or trypsin resulted in marked increases in lung weights and lung beta-glucuronidase and arylsulfatase activities. Destruction of alveolar walls was demonstrated microscopically as a decrease in the number of air spaces touching a line of known length. The pregnenes, progesterone and medroxyprogesterone acetate, but not the 19-nortestosterone derivative norethindrone, partially prevented the papain-induced breakdown of alveolar septa and elevation of beta-glucuronidase. The steroidal anti-inflammatory agent, paramethasone, completely inhibited the rise in lung weight and beta-glucuronidase activity, but did not prevent destruction of alveolar walls. The non-steroidal anti-inflammatory agent, indomethacin, afforded little or no protection. Limited prophylaxis against both histological and enzymatic changes was observed in rats treated with the anti-metabolite, cyclophosphamide, and the proteolytic enzyme inhibitor, aprotinin. The various lung abnormalities resulting from papain inhalation may thus be individually influenced by specific pharmacologic agents.
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PMID:Lung enzymes in emphysematous rats: effects of progestagens, antiphlogistics and metabolic inhibitors. 116 8

The metabolism and excretion of silybin (as N-methyl-glucamine salt) was investigated after intravenous and oral administration to rats. In the urine, silybin was excreted mostly in the unchanged form after intravenous as well as oral application, whilst in the bile it appeared above all in the form of metabolites. By hydrolysis with arylsulfatase/beta-glucuronidase, the metabolites were identified as sulfate and glucuronide conjugates of silybin and dehyrosilybin; the latter appeared in small quantities as a dehydrated product of silybin. After intravenous injection of 20 mg silybin per kg body weight, the excreted amount of silybin after 48 h was 8%, whereas 76% was eliminated in the bile within the same period of time. After oral application of 2--20 mg silybin/kg body weight 20% after 40 mg/kg 35% and after 120 mg/kg 20% of the administered silybin was excreted in the bile during 48 h. The maximum excretion rate was achieved at application of 20 mg/kg p.o. after 1 h. At this dosage, 2--5% was eliminated within the same time in the urine. The excretion of silybin mainly took place (more than 80% of the total of excreted bilybin) in the bile, both after oral and intravenous administration.
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PMID:[Studies of the metabolism and excretion of silybin in the rat]. 117 27

Acid hydrolase activities were compared in human leucocytes, guinea pig and human alveolar macrophages. Several enzymes were characterized: N-acetyl-beta-D-glucosaminidase, N-acetyl-alpha- and beta-D-galactosaminidase, alpha and beta-D-galactosidase, alpha-D-mannosidase, alpha-L-fucosidase, beta-D-glucuronidase, neuraminidase, acid phosphatase and arylsulfatase. The enzymatic activities were lower in leucocytes than in alveolar macrophages, higher in human macrophages than in guinea pig macrophages, except for beta-D-glucuronidase, acid phosphatase and arylsulfatase activities.
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PMID:[Comparative studies of the acid hydrolases of human leucocytes and human and guinea pig alveolar macrophages. I. Study of the activities of glycosidases, arylsulfatase and acid phosphatase (author's transl)]. 117 6

Fine structural localization of arylsulfatase in the rabbit blood platelets has been investigated in this study. Among many cell organellae, reaction products were exclusively observed in the alpha granules of the platelets. Within the alpha granules, arylsulfatase activity appeared to localize in variable patterns, i.e. reaction products confined mainly at the peripheral region in many granules, while they deposited heavily throughout the granule matrices in some others. In a blood platelets, each alpha granule showed the different staining pattern which indicated more variable functional heterogeneity in the granules.
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PMID:Fine structural localization of arylsulfatase B activity in the rabbit blood platelets. 118 18


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