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)

Significant increases in activities of epoxide hydrolase, UDP-glucuronosyltransferase, and glutathione S-transferase, and marked reductions in cytochrome P-450 mixed-function oxidase systems occur in hyperplastic nodules induced in rat liver by chemical mutagens. In contrast, activities of both oxidative (Phase I) and conjugative (Phase II) enzymes are decreased in hepatocellular carcinomas induced by peroxisome proliferators. The present work compares alterations induced by chemical mutagens or peroxisome proliferators with changes in enzyme activities that occur in primary and secondary hepatic tumors in man. The above activities, along with beta-glucuronidase and arylsulfatase, were measured in liver samples from 6 normal livers obtained at immediate autopsy, and liver specimens obtained by surgical biopsy from the following patients: 8 with hepatomas, 5 with nonmetastatic colorectal carcinomas, and 14 with metastatic colorectal carcinomas. Cytochromes P-450MP and P-450NF in addition to epoxide hydrolase were measured by immunoquantitation. Enzymes involved in conjugation reactions were either assayed fluorometrically (UDP-glucuronosyltransferase, beta-glucuronidase, sulfotransferase, and sulfatase) or spectrophotometrically (glutathione S-transferase) using umbelliferyl substrates or 1-chloro-2,4-dinitrobenzene. Secondary hepatic tumors showed no significant change in drug-metabolizing enzymes, in contrast to primary hepatomas, which displayed decreases in all of the measured drug metabolizing enzymes. Arylsulfatase was markedly depressed in primary hepatomas (14% of normal values). Thus, activities of drug-metabolizing enzymes in human primary tumors resemble those associated with altered hepatic foci induced by peroxisome proliferators such as ciprofibrate. The marked decreases in sulfatase that occurred in primary but not in secondary human tumors suggest that sulfation of endogenous compounds and xenobiotics may differ in patients with primary and secondary hepatic tumors.
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PMID:Hepatic drug-metabolizing enzymes in primary and secondary tumors of human liver. 302 21

A case of infantile agranulocytosis with survival into adolescence is presented. The polymorphonuclear leukocyte is considered an important source of lysosomal enzymes in gingival crevicular fluid, and evaluation of connective tissue-degrading enzymes in the fluid was performed. The activity of beta-glucuronidase, a ground substance-degrading enzyme that may serve as a marker for polymorphonuclear leukocytes, was markedly reduced in the fluid compared to samples from systemically healthy adults with periodontitis. The activities of the ground substance-degrading enzyme arylsulfatase, and collagenase, were in the low-normal range. The plaque microbiology, as characterized by dark-field microscopy and selective culturing, was consistent with advanced periodontitis. A review of the medical history revealed a series of bacterial infections since infancy. Improvement in the systemic health of the patient occurred at about the age of 15, and the intake of antibiotics to control infections was correspondingly reduced after this time. An exacerbation of the patient's periodontal disease, as evaluated by loss of alveolar bone on radiographs, occurred 1 to 2 years later. The progression of periodontal disease observed in this patient was apparently associated with the withdrawal of antibiotics administered for control of systemic (nonoral) infections.
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PMID:Infantile agranulocytosis with survival into adolescence: periodontal manifestations and laboratory findings. A case report. 302 96

Activities of six lysosomal enzymes in the cerebellum of jaundiced homozygous (jj) Gunn rats were examined from 5 to 20 days of life and compared with those in heterozygotes (j+). Significantly higher enzyme activities were first detected at 8 days. The jj/j+ activity ratios of all enzymes peaked at 15 days. The ratios of beta-glycerophosphatase, beta-mannosidase, and acid lipase were only 1.3-1.7, whereas those of arylsulfatase and cathepsin were 2.0 and 3.1, respectively. The most striking increase in activity was observed with beta-glucuronidase, the ratio of which was 8.4. These results indicate a selective increase in activities of certain lysosomal enzymes in the hypoplastic cerebellum of jj rats.
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PMID:Different behaviors among lysosomal enzymes in the cerebellum of jaundiced Gunn rats with cerebellar hypoplasia. 303 52

Previous reports have described a method by which multiple constituents can be analyzed from a sample of gingival crevicular fluid (GCF) collected with a precut filter paper strip. In this study the relationship of changes in GCF levels of the vertebrate (lysosomal) enzymes beta-glucuronidase (BG) and arylsulfatase (AS) and the cytoplasmic enzyme lactate dehydrogenase (LDH) was evaluated longitudinally in reference to loss of clinical attachment in patients with existing chronic adult periodontitis. Thirty-six patients were followed for six months. Clinical attachment loss was recorded as the change between the baseline and three month examinations, and the three- and six-month examinations. GCF analysis was performed at baseline and three months. Three groups of patients were identified based on disease progression. Group I patients (N = 5) displayed a generalized form of disease activity. In these patients we observed clinical attachment loss of at least 2.0 mm at a minimum of three unrelated sites. Group II patients (N = 4) displayed a localized form of disease activity. In these patients clinical attachment loss of at least 2.5 mm occurred at one site, or two anatomically related sites. Group III patients (N = 27) did not display clinical attachment loss as defined here. Enzyme analysis was evaluated as a whole mouth score (the per cent of samples from a patient in which enzyme activity was at least twice the population mean) and at individual samples. Group I patients could be identified by elevated whole mouth scores for BG, while Group II patients could not be identified by whole mouth scores for any of the enzymes.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Enzyme activity in crevicular fluid for detection and prediction of clinical attachment loss in patients with chronic adult periodontitis. Six month results. 305 19

The effect of selenium (SeO2) and glutathione (GSH) on the bioaccumulation of mercury (HgCl2) and on the activities of lysosomal enzymes in four species of tropical estuarine lamellibranchs is reported. A definite correlation between mercury levels in the external medium and tissue uptake and physiological behaviour--opening and closing of shell valves, response to mechanical stimulus, mucus secretion, and incidence of bleeding--was evident. In the clams exposed to Hg (range 0.1-5.0 mg l-1), bioaccumulation was dependent on the ambient concentration of Hg. The highest bioaccumulation of Hg occurred during the initial 24 h exposure period. Further exposure of up to 7 days did not increase the body burden of Hg. Of the four bivalve species exposed to 0.1 mg Hg l-1, Perna viridis showed the highest levels of Hg (approximately 47 ppm) followed by Anadara granosa, A. rhombea (approximately 25 ppm) and Meretrix casta (approximately 9 ppm). The uptake of Hg by A. granosa was greatly reduced by GSH, whereas Se enhanced it by 50% when administered in combination with Hg. However, the presence of Hg did not influence the uptake of Se. Exposure to combined GSH and Hg resulted in almost complete inhibition of Hg uptake in all four bivalve species. Prior exposure to GSH, however, did not have the same influence on their uptake of Hg. Nevertheless, exposure of clams to GSH following initial exposure to Hg resulted in complete depuration of accumulated Hg. The activities of lysosomal enzymes--arylsulfatase, acid phosphatase, beta-galactosidase and beta-glucuronidase--varied considerably. Treatment with Hg and GSH, separately and in combination, significantly enhanced the levels of beta-galactosidase (P less than 0.05) and beta-glucuronidase (P less than 0.001) in the digestive gland after 96 h exposure. Although Se increased beta-glucuronidase activity (P less than 0.001), it had no effect on beta-galactosidase. On exposure to Hg + Se the activity of both enzymes decreased, except in P. viridis where it increased by 39%. The results show unequivocally that Se does not offer any protection against the toxic effects of mercury in marine lamellibranchs, whereas in many marine vertebrates it does. GSH, a thiol-rich tripeptide, on the other hand, completely nullifies the toxic effects of Hg, both in vivo and in vitro.
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PMID:Do selenium and glutathione inhibit the toxic effects of mercury in marine lamellibranchs? 323 22

The biochemical analysis of gingival crevicular fluid (GCF) may offer a sensitive means of determining periodontal disease activity, including the transition of gingivitis to periodontitis. To continue our evaluation of the relationship between clinical and GCF parameters, 552 sites with shallow to intermediate (2.0-5.0 mm) probing depths (PD) were examined. The data were collected at baseline from 33 periodontitis patients participating in a longitudinal trial examining the relationship of changes in GCF biochemistry to attachment loss. Mesiobuccal sites were scored for dichotomous measures of bleeding on probing, gingival redness, suppuration, and plaque accumulation. In addition, GCF was collected using filter paper strips inserted into the sulcus for 30 seconds, eluted in buffer and assayed for activity of the enzymes beta-glucuronidase (BG), arylsulfatase (AS), and lactate dehydrogenase (LDH), markers for ground substance-degradation and cellular necrosis, respectively. Clinical and GCF parameters were evaluated by increasing PD. Plaque accumulation and bleeding on probing increased with increasing PD, although there was considerable overlap across groups. Suppuration was present in only a very small number of sites and the proportion of sites displaying gingival redness was not related to PD. GCF volume was grouped in 0.25-microliter increments, revealing a progressive shift with increasing PD toward a normal distribution around the median range of 0.51 to 0.75 microliter at 5.0 mm. Mean enzyme activities of BG, and to a lesser extent AS and LDH increased sharply from 2.0 to 3.0 mm, were relatively stable from 3.5 to 4.5 mm, and were significantly higher in 5.0 mm than 4.5 mm sites.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Lysosomal and cytoplasmic enzyme activity, crevicular fluid volume, and clinical parameters characterizing gingival sites with shallow to intermediate probing depths. 330 52

3-Hydroxy-trans-7,8-dihydroxy-7,8-dihydrobenzo[a]pyrene (3-OH-BP-7,8-diol) was isolated from arylsulfatase/beta-glucuronidase-treated bile of rats to which 3-hydroxybenzo[a]pyrene (3-OH-BP) has been administered. This triol was investigated for mutagenicity in Salmonella typhimurium (reversion to histidine prototrophy of strains TA 97, TA 98, TA 100 and TA 1537) and in V79 Chinese hamster cells (acquisition of resistance to 6-thioguanine). When no exogenous metabolizing system was added the triol was inactive, while 3-OH-BP showed weak mutagenic effects with all four bacterial strains. In the presence of NADPH-fortified postmitochondrial supernatant fraction (S9 mix) of liver homogenate from Aroclor 1254-treated rats, the mutagenicity of 3-OH-BP was potentiated, and the triol was activated to a mutagen(s). In the presence of S9 mix, the triol was 5-18 times more mutagenic than 3-OH-BP in strains TA 97, TA 100 and TA 1537, but both compounds showed similar mutagenic potencies with strain TA 98. These strain differences strongly suggest that the mutagenicity of 3-OH-BP in the S9 mix-mediated test was not exclusively due to metabolites of 3-OH-BP-7,8-diol. Trans-7,8-dihydroxy-7,8-dihydrobenzo[a]pyrene (BP-7,8-diol), like the triol, showed mutagenic effects only in the presence of S9 mix. Strain TA 1537 was reverted by the triol but not by the diol. In the other bacterial strains the diol was more mutagenic than the triol, the difference in potency being largest in strain TA 100 (2.5- to 10-fold, depending on the experimental conditions). In V79 cells, the diol was a potent mutagen, while the triol showed only very weak mutagenic effects. However the triol was more cytotoxic than the diol. High cytotoxicity of the triol was observed even in the absence of S9 mix. The results of the present study demonstrate that metabolites of 3-OH-BP-7,8-diol are biologically-active derivatives of benzo[a]pyrene. Comparison of the mutagenic effectiveness in different bacterial strains also reveals that metabolites of 3-OH-BP-7,8-diol and of BP-7,8-diol substantially differ in the kind of genetic alterations they evoke.
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PMID:Metabolic activation to a mutagen of 3-hydroxy-trans-7,8-dihydroxy-7,8-dihydrobenzo[a]pyrene, a secondary metabolite of benzo[a]pyrene. 331 46

Strenuous prolonged running causes muscle fibre necrosis in skeletal muscles. The muscle injury is associated with inflammation and a strong increase in the total activities of certain acid hydrolases a few days after exertion. The activity changes of acid hydrolases quantitatively well reflect the severity of histopathological changes during the myopathy (for review see Salminen, Acta Physiol Scand [Suppl 539] 1985). In this study male NMRI-mice were exposed to a protocol of fasting and refeeding together with or without a 6 h run on a treadmill at 13.5 m.min-1. The animals were killed 4 days after the exercise and samples from the red part of quadriceps femoris were analyzed for arylsulfatase (ASase) and beta-glucuronidase (GUase) activities. Starvation protocols did not affect ASase or GUase. Running caused a 3.2-fold increase in ASase and a 5.1-fold increase in GUase. If mice were exercised in the fasted condition a normal exercise response occurred in both activities, but when mice were exercised 2 days after the finish of fasting the exercise response was greatly diminished. Thus food deprivation followed by 2 days refeeding induces a protection against exercise myopathy in mice. The protection greatly resembles that induced by regular endurance training preceding strenuous prolonged exertion.
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PMID:Food deprivation decreases the exertion-induced acid hydrolase response in mouse skeletal muscle. 334 83

To distinguish lysosome populations of HeLa cells, acid phosphatase, beta-glucuronidase, arylsulfatase and esterase were demonstrated using various substrates and couplers with different fixations, pHs and inhibitors. The substrates chosen were for acid phosphatase, naphthol AS-BI phosphate with fast red violet LB at pH 4.6; for beta-glucuronidase, naphthol AS-BI beta-D-glucuronide with fast red violet LB at pH 4.4; for arylsulfatase, p-nitrocatechol sulfate, with lead as the capturing ion, at pH 4.8 and 5.6; and for esterase, naphthol AS-D acetate with fast blue BB at pH 6.5. In the azo-dye methods, the coupling was always simultaneous and results were satisfactory with unfixed cells. For optimal demonstration of arylsulfatase, cells were fixed in glutaraldehyde in 0.1 M cacodylate buffer pH 7.2, 2% for 24 hr or 6.25% for 2 hr, and washed for 1-9 days in 0.1 M veronal acetate buffer pH 7.2, 7.5% with respect to sucrose. Two groups of lysosomes were distinguished. One comprised small bodies, probably primary lysosomes, which lay in a cluster near the nucleus. They had quite stable membranes and were mostly acid phosphatase-positive. They sometimes contained beta-glucuronidase or esterase, but rarely arylsulfatase. The other group included all the acid hydrolase-positive bodies scattered throughout the rest of the cytoplasm. They were mostly larger, with more labile membranes, and contained beta-glucuronidase, esterase or arylsulfatase, but rarely acid phosphatase.
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PMID:Acid hydrolases in HeLa cells: comparison of methods for light microscopy. 343 9

A method for the preparation of calibration curves for acetaminophen glucuronide (NAPAG) and acetaminophen sulfate (NAPAS) in rabbit urine without use of authentic compounds in high-performance liquid chromatography was examined. Rabbits were dosed intravenously with acetaminophen (NAPA, 30 mg/kg). Urine was collected and diluted. A plot of the peak area ratio of NAPAG to internal standard against NAPA concentration after the hydrolysis of diluted urine with beta-glucuronidase was linear and passed through the origin. A linear tendency was also observed in the plot of the peak area ratio of NAPAS to internal standard against NAPA concentration calculated by the difference between the peak area ratio of NAPA after the hydrolysis with beta-glucuronidase and that with beta-glucuronidase/arylsulfatase. Thus, once the calibration curve has been prepared following the enzyme hydrolysis of NAPAG and NAPAS, then the concentration of NAPAG and NAPAS in the sample solution can be calculated from the peak of NAPAG and NAPAS, respectively. The method is simple, and has the advantage that pure standards of the individual NAPA metabolites are not required.
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PMID:A method for the preparation of calibration curves for acetaminophen glucuronide and acetaminophen sulfate in rabbit urine without use of authentic compounds in high-performance liquid chromatography. 344 75


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