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:3.2.1.31 (beta-glucuronidase)
7,680 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The effects of acute and chronic administration of D-Galactosamine (GalN), Ethanol and Phenobarbital were investigated on the activities of lysosomal enzymes, i.e.; acid phosphatase, beta-glucuronidase and n-acetyl-beta-glucosaminidase, and others such as gamma-GTP and adenosine triphosphatase. The histochemical distribution of gamma-GTP in the liver was also studied on biopsy specimens from patients with chronic hepatitis, and gamma-GTP levels in the serum of patients receiving drugs inductable of hepatic microsomal enzymes. 1) After a single intraperitoneal injection of GalN, the lysosomal enzyme activities were lowered in the necrotic areas, but raised in the perinecrotic areas, the proliferative Kupffer cells and intra- and/or extra-cellular eosine bodies. 2) gamma-GTP activities in rat liver after chronic administration of GalN were markedly increased in bile canalicular membrane of periportal parenchymal cells, the epithelium of bile duct and ductules, and som inflammatory cells of portal fields. Levels of serum gamma-GTP were also elevated. On histochemical studies with biopsy specimens from patients with chronic active hepatitis showing elevated gamma-GTP activity, the activity was revealed a similar localization to GalN-treated rats. These data suggested that the increased activities might be reflected on the active stage in chronic hepatitis. 3) Chronic ethanol treatment in rats induced clearly-stained lysosomes varied in size, especially large-sized. The activities of hepatic gamma-GTP were slightly increased in the bile canalicular membrane of periportal parenchymal cells and the epithelium of proliferative bile ductules. 4) It has been shown by histochemical and biochemical techniques that hepatic gamma-GTP activity was increased after phenobarbital administration in rats. A significant rise in serum gamma-GTP was observed in patients on long-term treatment with anti-epileptic drugs. These data indicated that the increased activities of serum gamma-GTP might be accompanied with induction of hepatic microsomal drug-metabolizing enzymes.
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PMID:[Clinical and experimental histochemical studies on the activities of liver lysosomal enzymes and gamma-glutamyl transpeptidase (gamma-GTP) (author's transl)]. 3 25

The potency of the calcium ionophore A23187 in inducing three activities of human leukocytes (histamine secretion from basophils, enzyme secretion from PMNs, and proliferation of lymphocytes) was markedly dependent on the solvent (DMSO versus ethanol versus aqueous buffer) used for its initial sonication. While 0.1 micrograms/ml of DMSO- and ethanol-solubilized A23187 induced maximal histamine release from basophils and histaminase release from PMNs, concentrations of aqueous buffer-sonicated ionophore of greater than or equal to 1 microgram/ml were required for an equivalent response. Ionophore sonicated in organic solvents caused a maximum release of 40% of PMN beta-glucuronidase, at an optimal concentration tenfold higher than that required for maximal histaminase release; ionophore sonicated in aqueous buffers, even at high concentrations, effected a release of less than 5% of cellular beta-glucuronidase. A23187 also induced lymphocyte proliferation over a narrow concentration range; 0.05 micrograms/l of DMSO-sonicated ionophore induced optimal proliferation and concentrations greater than or equal to 0.2 micrograms/ml were toxic. Twofold higher concentrations of ethanol-sonicated ionophore and fourfold higher concentrations of aqueous-sonicated ionophore were necessary for maximal proliferation, and the magnitude of the maximal response with aqueous-sonicated A23187 was only one-half that of DMSO-solubilized agent. Ionophore-induced release of histamine from basophils and enzymes from PMNs was not cytotoxic, since ionophore induced neither LDH nor histamine release from heat-treated (47 degrees C) cells. These results explain several previous, discordant reports on the presence or absence of an effect of A23187 on cellular secretory events, on differing dose-response relationships, and on cytotoxic versus noncytotoxic mechanisms of action.
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PMID:Effect of solvent on the histamine-releasing, enzyme-releasing, and mitogenic properties of the calcium ionophore A23187. 9 71

Radiolabeled diethylstilbestrol (DES) was administered to one pregnant and three normal female rhesus monkeys. One normal female chimpanzee was also included in the study. Regardless of the mode of presentation (oral versus intravenous), the urine was the principal route of excretion for each species. The urine contained no non-polar radioactivity, and Sephadex LH-20 (MeOH/EtOH-50:50) resolved the radioactivity into five fractions (A, B, C, D, E). Fractions A,B, C, and D were hydrolyzable with beta-glucuronidase, and the principal aglycones were identified with GC/MS as cis-trans DES and dienestrol. The fecal excretory products were extracted with dimethoxy methane/methanol (50:50) and the radioactivity partitioned between benzene and H2O. The polar radioactivity was resolved by LH-20 (MeOH/EtOH-50:50) into chromatographic fractions similar to the urinary conjugates. These fecal conjugates were, however, less sensitive to beta-glucuronidase hydrolysis. The primary non-polar fecal radioactivity was chromatographically similar to DES (LH-20 and HPLC) in both species, and in the rhesus monkey the principal products identified were cis-trans DES and dienestrol.
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PMID:The metabolism of diethylstilbestrol in the rhesus monkey and chimpanzee. 10 73

Rat preputial gland beta-glucuronidase [ED 3.2.1.31] was purified by ammonium sulfate precipitation, ethanol fractionation, gel filtration on Sephadex G-200 and crystallization. The purified enzyme appeared homogeneous on electrophoresis in polyacrylamide gel, and on analytical ultracentrifugation and had a molecular weight of approximately 320,000, and a sedimentation coefficient of 12S. SDS polyacrylamide gel electrophoresis indicated that the enzyme consisted of subunits with molecular weight of 79,000, so the native enzyme appeared to be a tetramer. The Km with p-nitrophenyl beta-D-glucosiduronic acid as substrate was about 0.53 mM. The enzyme had a single pH optimum at 4.5. The enzyme had a very low content of sulphur-containing amino acid and contained 5.7 per cent carbohydrate, consisting of mannose, glucose, fucose, galactose, and glucosamine in a ratio of 44;9;6;2;41. Sialic acid was not detected in the crystallized enzyme.
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PMID:Beta-glucuronidase of rat preputial gland. Crystallization, properties, carbohydrate composition, and subunits. 23 93

A method is described for the preparation of pure beta-glucuronidase from bovine liver. The procedure includes ammonium sulfate, acetone and ethanol fractionation and a simple two-step ion exchange chromatography. The yield is acceptable and the method requires only standard laboratory equipment. The pure enzyme is easily crystallized from ammonium sulfate. Some practical applications of the pure beta-glucuronidase are discussed.
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PMID:Preparation of crystalline bovine liver beta-glucuronidase. 66 5

In order to examine a role of lysosomes in the pathogenesis of fatty livers, analysis was made on possible etiologic factors, clinical signs and symptoms as well as laboratory data of routine liver function tests in 32 subjects with fatty livers. Of 18 cases, enzyme activities of serum acid phosphatase (Acp), beta-glucuronidase (betaG) and n-acetyl-beta-glucosaminidase (nbetaG) were measured and compared with those obtained in 20 normal subjects. Subjective symptoms were observed in 75% of the cases examined, liver swelling in 56%, positive GOT, GPT and BSP retention were in 59, 75 and 68%, respectively. The activity of serum lysosomal enzymes such as Acp, betaG and nbetaG were significantly increased and their incidence was 28, 89 and 78%, respectively. In animal experiments, activities of these enzymes in both serum and liver homogenate were examined in rats with choline-deficient, ethionine-treated, and alcoholic fatty livers. Results obtained were as follows: 1) Lysosomal enzyme activity in sera and livers of choline-deficient rats showed a significant decrease in lysosome-rich fraction and a significant increase in supernatant fraction and sera. 2) The enzyme activity in ethionine-treated rats decreased significantly in lysosome-rich fraction and tended to increase in supernatant fraction. The activity of betaG in sera increased markedly. 3) In rats given ethanol for 4 weeks, the enzyme activity of sera and liver homogenates significantly increased in lysosome-rich fraction. These results indicate that the analysis of serum lysosomal enzyme activity, in the light of clinical features and laboratory data of routine liver function tests, is useful for the diagnosis of the fatty liver. A discussion is given of a possible mode of variation of lysosomal enzymes in rats with fatty livers.
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PMID:[Clinical and experimental studies on changes in lysosomal enzyme activity in fatty livers (author's transl)]. 71 Nov 25

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

Effect of ethanol on functional activity of isolated perfused rat liver was studied (rate of O2 utilization, absorption of bromosulpholeine from perfusate, bile formation); total activity and activity in supernatant of nine marker enzymes were also determined (malate dehydrogenase, beta-glucuronidase, arylsulphatases A and B, beta-galactosidase, beta-glucosidase, acetylesterase, glucoso-6-phosphatase, alanine aminotransferase and aspartate aminotransferase). Activity of the enzymes was simultaneously studied in perfusate. Ethanol (0.5%) caused distinct impairement in functional activity of isolated liver; rate of bile formation and absorption of bromosulpholeine from perfusate were primarily altered. Degree of impairements in functional activity of liver tissue correlated with the concentration of ethanol in perfusate. In analysis of correlation between the total activity of the enzymes in liver tissue and their activity in supernatants and perfusate it was shown that the concentration (1%) of ethanol used did not produce damaye effect on plasma membranes and membranes of subcellular structures of hepatocytes, but, within certain limits, it displayed a stabilizing effect.
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PMID:[Effect of ethanol on stability of cell membranes in experiments using isolated liver]. 121 Jan 8

The 70% EtOH extract of Scoparia dulcis showed inhibitory activity against beta-glucuronidase from bovine liver. Bioassay-directed fractionation of the active extract led to the isolation of three labdane-type diterpene acids, scoparic acid A [1] [6-benzoyl-12-hydroxy-labda-8(17), 13-dien-18-oic acid], scoparic acid B [2] [6-benzoyl-14,15-dinor-13-oxo-8(17)-labden-18-oic acid], and scoparic acid C [3] [6-benzoyl-15-nor-14-oxo-8(17)-labden-18-oic acid], the structures of which were established by spectral means, including X-ray analysis. Scoparic acid A was found to be a potent beta-glucuronidase inhibitor.
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PMID:Scoparic acid A, a beta-glucuronidase inhibitor from Scoparia dulcis. 129 95

Recent studies indicate that altered lysosomal function may be involved in the early stages of pancreatic injury. Chronic consumption of ethanol increases rat pancreatic lysosomal fragility. The aim of this study is to determine whether the lysosomal fragility observed after chronic ethanol consumption is mediated by ethanol per se, its oxidative metabolite acetaldehyde or cholesteryl esters (substances which accumulate in the pancreas after ethanol consumption). Pancreatic lysosomes from chow fed rats were incubated for 30 minutes at 37 degrees C with ethanol, acetaldehyde or phosphatidylcholine vesicles containing cholesteryl oleate. Lysosomal stability was then assessed by determination of: (a) Latency--that is, the per cent increase in lysosomal enzyme activity after addition of Triton X-100 and (b) Supernatant activity--that is, the proportion of lysosomal enzyme remaining in the supernatant after resedimentation of lysosomes. Acid phosphatase, N-acetyl glucosaminidase, beta-glucuronidase and cathepsin B were assayed as lysosomal marker enzymes. Lysosomes incubated with homogenising medium alone or equivalent volumes of phosphatidylcholine vesicles without cholesteryl oleate were used as controls. Cholesteryl oleate at concentrations of 15 and 20 mM increased pancreatic lysosomal fragility as shown by decreased latency and increased supernatant enzyme. In contrast, ethanol (150 mM) and acetaldehyde (5 mM) had no effect on lysosomal stability in vitro. These results suggest that increased pancreatic lysosomal fragility observed with ethanol may be mediated by cholesteryl ester accumulation rather than by ethanol or acetaldehyde.
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PMID:Effects of ethanol, acetaldehyde and cholesteryl esters on pancreatic lysosomes. 139 35


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