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)

Administration of zinc (Zn) simultaneously with lead (Pb) into the chick egg yolk sac reduced the accumulation of Pb and Pb-induced alterations in the activities of acid phosphatase, beta-glucuronidase and ribonuclease in the brain of the embryo. The results suggest protection against toxic effects of Pb by Zn.
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PMID:Effect of zinc on lead-induced changes in brain lysosomal enzymes in the chick embryo. 669 89

Biochemical analysis of 328 human prostatic fluid samples were performed. The urea concentration of 69 samples was similar to that of serum and not indicative of significant contamination with urine. The pH of normal fluids was acidic (mean pH = 6.7). The interrelationships between zinc, citrate, acid phosphatase aminopeptidase, beta-glucuronidase, diamine oxidase and pH were investigated by factor analysis. Two significant factors were extracted, the first accounted for 89% of their common variance and the second for 11%. Zinc, citrate, acid phosphatase and aminopeptidase were positively and pH was negatively related to factor one. Beta-glucuronidase was positively related to factor two and diamine oxidase was largely independent of both factors. It was concluded that variables related to factor one share a common secretory control and mechanism, that some other mechanism operates in the case of beta-glucuronidase and that diamine oxidase may not be a true secretory product of the prostate.
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PMID:The interrelationships between acid phosphatase, aminopeptidase, diamine oxidase, citric acid, beta-glucuronidase, pH and zinc in human prostatic fluid. 681 44

282 human prostatic fluid samples have been investigated for their pH value, zinc, and citrate concentration and their acid phosphatase, leucine aminopeptidase, diamine oxidase, and beta-glucuronidase activities. The results have been analysed in terms of the clinical status of the patients. Significant differences between patient categories were found with all but diamine oxidase and beta-glucuronidase. These differences were mainly found between men with apparently healthy prostates and prostatitis patients; the pH being raised and the acid phosphatase, leucine aminopeptidase, zinc and citrate being reduced. The diagnostic value of these parameters was evaluated, each could be used to classify correctly 90% of patients from these 2 groups. Zinc, citrate and leucine aminopeptidase showed no age relationship and were better than acid phosphatase and pH in discriminating between BPH and prostatitis. Evidence was also found for a return of normal secretory function sometime after an episode of prostatitis. Zinc and citrate are likely to be the most useful parameters for clinical evaluation.
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PMID:The response of seven prostatic fluid components to prostatic disease. 717 28

The effects of graded doses of zinc sulfate pretreatment on reserpine-induced gastric ulceration and on lysosomal fragility both in vivo and in vitro, were studied in rats. Reserpine treatment (5 mg/kg, i.p., 18 h before sacrifice) induced marked gastric glandular ulceration and elicited the release of free beta-glucuronidase from lysosomes in the gastric mucosa. A similar effect on release of this enzyme from isolated rat hepatic lysosomes was observed after in vitro incubation with reserpine. Zinc sulfate (22, 44 or 88 mg/kg, i.p., 30 h before reserpinization, or 10(-3) M in vitro) inhibited the reserpine-induced response, and zinc sulfate alone (10(-11)--10(-3) M) also stabilized lysosomal membrane permeability to beta-glucuronidase. No direct effect of zinc or reserpine on purified beta-glucuronidase activity was observed. In conclusion, it is postulated that the stabilizing effect of zinc on lysosomal membranes, as manifest by reduced release of beta-glucuronidase from isolated lysosomes, is one of the protective mechanisms of zinc against reserpine-induced ulceration.
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PMID:Reserpine-induced gastric ulcers: protection by lysosomal stabilization due to zinc. 737 12

The effect of zinc ions on the stability of rat liver lysosomes was studied. Zinc was added by several methods: feeding the animals a high-zinc diet; infusion of zinc into the liver through the portal vein, or by adding zinc to the lysosomal fraction either before or after isolation of this fraction from rat liver homogenates. By all techniques, addition of zinc reduced the release of beta-glucuronidase from liver lysosomes. Lysosomes and lysosomal membranes from rats fed a high-zinc diet were found to be relatively high in zinc. These lysosomes were less fragile than lysosomes from the liver of control animals. The stabilizing effect of zinc ions could be reversed by treatment of lysosomes with phosphate buffer. We concluded that increasing the zinc content in the liver by any of these methods results in stabilization of liver lysosomes.
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PMID:Reversible stabilization of liver lysosomes by zinc ions. 737 39

In vitro studies on rat hepatic lysosomal stability, as assessed by release of beta-glucuronidase, were undertaken to demonstrate the comparative influence of surface-active agents which act by various mechanisms. Bile acids, short chain alcohols, acetylsalicylic acid, and Triton X-100 were studied, as well as their interaction with zinc. The detergents and alcohols enhanced release of this acid hydrolase in a dose dependent fashion, but acetylsalicylic acid did not. Zinc antagonized these effects in a non-specific manner. It is postulated that zinc stabilized lysosomes by direct action on the lysosomal membrane, such as by surface protein interactions, but the precise mechanism remains unknown.
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PMID:Modulating effect by zinc on hepatic lysosomal fragility induced by surface-active agents. 738 47

A combined in vivo and in vitro study was undertaken with rats to test the hypothesis that zinc would protect against cold water immersion--restraint gastric ulcers, and that this phenomenon was mediated in part by stabilization of lysosomal membranes. This postulate was confirmed by observed activity changes in released beta-glucuronidase in mucosal tissue, as well as by dose-response in vitro data on isolated hepatic lysosomes exposed to zinc. Histamine, a known ulcer-enhancing agent, induced the opposite effect and increased the lysosomal release of this marker acid hydrolase.
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PMID:Studies of zinc and histamine on lysosomal fragility: possible role in stress ulceration. 740 19

We determined the 5'-flanking sequences of two nuclear genes (SodCc1 and SodCc2) encoding cytosolic copper/zinc-superoxide dismutase in rice (Oryza sativa L.). Utilizing transient beta-glucuronidase (GUS) reporter assays, functional promoter-GUS analysis was performed in rice protoplasts exposed to the phytohormone abscisic acid (ABA) or the antioxidant sulfhydryl reagent, dithiothreitol (DTT). Transcriptional activities from both SodCc-GUS fusions were stimulated by DTT, which induces the promoter activity of the tobacco SodCc gene [Proc. Natl. Acad. Sci. USA 90 (1993) 3108-3112]. ABA had no effect on SodCcl-GUS expression but specifically induced the gene expression of the SodCc2-GUS fusion. The simultaneous application of ABA and gibberellin A3, however, abolished the enhancing effect of ABA. These results indicated that two rice SodCc promoters differentially respond to externally supplied ABA and that one of the regulatory factors for plant SodCc expression is ABA in addition to cellular redox-modulating antioxidants.
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PMID:Structure and differential response to abscisic acid of two promoters for the cytosolic copper/zinc-superoxide dismutase genes, SodCc1 and SodCc2, in rice protoplasts. 782 31

Superoxide dismutases (SODs; superoxide: superoxide oxidoreductase, EC 1.15.1.1) play a key role in protection against oxygen radicals, and SOD gene expression is highly induced during environmental stress. To determine the conditions of SOD induction, the promoter of the cytosolic copper/zinc SOD (Cu/ZnSODcyt) gene was isolated in Nicotiana plumbaginifolia and fused to the beta-glucuronidase reporter gene. Oxidative stress is likely to alter the cellular redox in favor of the oxidized status. Surprisingly, the expression of the Cu/ZnSODcyt gene is induced by sulfhydryl antioxidants such as reduced glutathione, cysteine, and dithiothreitol, whereas the oxidized forms of glutathione and cysteine have no effect. It is therefore possible that reduced glutathione directly acts as an antioxidant and simultaneously activates the Cu/ZnSODcyt gene during oxidative stress.
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PMID:Redox-activated expression of the cytosolic copper/zinc superoxide dismutase gene in Nicotiana. 846 30

The effect of zinc compounds on osteoclast-like cell formation in rat marrow culture in vitro was investigated. The bone marrow cells were cultured for 7 days in alpha-minimal essential medium containing a well-known bone resorbing hormone (1, 25-dihydroxyvitamin D3 and parathyroid hormone [1-34]). Osteoclast-like cell formation was estimated by staining for tartrate-resistant acid phosphatase (TRACP), a marker enzyme of osteoclasts. The presence of 1, 25-dihydroxyvitamin D3 (10(-8) M) or parathyroid hormone (PTH; 10(-8) M) induced a remarkable increase in osteoclast-like multinucleated cells (MNC). These increases were clearly inhibited by the presence of zinc sulfate or zinc-chelating dipeptide (beta-alanyl-L-histidinato zinc; AHZ) in the concentration range of 10(-7) to 10(-5) M. The inhibitory effect was seen at the earlier stage of osteoclast-like MNC formation. However, zinc compounds (10(-6) M) did not have an effect on PTH (10(-8) M)-induced osteoclast-like cell formation in the presence of EGTA (5 x 10(-4) M), dibucaine (10(-5) M) or staurosporine (10(-9) M). Moreover, when osteoclasts isolated from rat femoral-diaphyseal tissues were cultured for 24 h in the presence of zinc compounds (10(-7) to 10(-5) M), the compounds did not have an effect on cell numbers or lysosomal enzymes activity (acid phosphatase and beta-glucuronidase) in the cells. The present study clearly demonstrates that zinc compounds inhibit osteoclast-like cell formation at the earlier stage with differentiation of marrow cells.
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PMID:Zinc compounds inhibit osteoclast-like cell formation at the earlier stage of rat marrow culture but not osteoclast function. 881 79


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