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)

Whereas the phosphorolytic breakdown of liver glycogen is known to be of great physiological importance, the functional role of the hydrolytic glycogenolysis in the lysosomal system is less well understood. In the present study the effects of fasting, alpha- and beta-adrenoceptor antagonism and insulin-induced hypoglycaemia on liver lysosomal glycogen-hydrolysing enzyme activity were investigated in mice. In freely fed mice the glycogen-hydrolysing activity (acid amyloglucosidase) was only 50% of the maltose-hydrolysing activity (acid maltase). Starvation for 24 h reduced the acid amyloglucosidase activity by approximately 30% (P less than 0.001), whereas the activities of acid maltase, acid phosphatase and beta-glucuronidase appeared unaffected. N-acetyl-beta-D-glucosaminidase activity was moderately (20%; P less than 0.01) enhanced by fasting. Thus, liver lysosomal enzyme activities may change independently of each other during fasting. Further, during short-term hypoglycaemic conditions (45 min) induced by endogenous or exogenous insulin, the activity of liver acid amyloglucosidase was found to be moderately reduced (15-20%). Blockade of alpha- and beta-adrenoceptors by phentolamine and propranolol did not result in any apparent influence on acid amyloglucosidase activity except for the indirect effect exerted by the phentolamine-induced hypoglycaemia. A moderate negative correlation (r = -0.51; P less than 0.001) between total liver glycogen concentration and acid amyloglucosidase activity was observed in a series of 43 freely fed NMRI mice. Our data show that in mouse liver the acid maltase activity predominates over the acid amyloglucosidase activity.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Glycogen and glycogen-hydrolysing lysosomal enzyme activity in mouse liver: effects of fasting, adrenoceptor antagonism and insulin-induced hypoglycaemia. 289 Feb 62

The effect of subcutaneous injection of hydrocortisone and corticosterone on the activity values of some subcellular fractions marker enzymes from rat liver and brain was investigated and compared with controls (without treatment with hormones). The following enzymes were studied (subcellular fraction are shown between parentheses): N-acetyl-beta-D-glucosaminidase and beta-glucuronidase (lysosomes); succinate dehydrogenase = SDH (mitochondria); glucose-6-phosphatase (endoplasmic reticulum); 5'-nucleotidase and Na+-K+-Mg2+ ATPase (plasma membrane). The specific activity of lysosomal enzymes from liver showed no change when rats were injected either with hydrocortisone or corticosterone. The same enzymes from brain showed significant increases in their activities with both hydrocortisone or corticosterone except beta-glucuronidase; this enzyme gave activity values remaining between the control levels, after treatment with corticosterone. The activity of mitochondrial SDH was increased after corticosterone injection either in liver or brain. After hydrocortisone injection, its activity rises significantly in brain (72%), but it falls in liver compared to the control values. Glucose-6-phosphatase behaves similarly in brain or liver fractions; its activity increases always after corticosterone treatment and decreases by hydrocortisone. The plasma membrane marker enzymes did not change practically in brain fractions, excepted Na+-K+-Mg2+ ATPase which tends to rise its activity after hydrocortisone injection. In liver fractions, both 5'-nucleotidase and Na+-K+-Mg2+ ATPase activities increase either by corticosterone or hydrocortisone treatment, except 5'-nucleotidase which specific activity decreases in liver after hydrocortisone treatment.
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PMID:Alterations in the activities of subcellular fractions marker enzymes in rat liver and brain by hydrocortisone and corticosterone treatment. 298 17

Activity of N-acetyl-beta-D-glucosaminidase, beta-glucuronidase, and acid phosphatase and myeloperoxidase was determined in neutrophils and lymphocytes of patients with cancer of the larynx and precancerous states of the larynx as well as--for comparative reasons--in patients with malignant tumors of female generation organs, breast carcinoma, cancer of the stomach and endometriosis. The main result of investigations performed was in fact that intracellular deficiency of beta-glucuronidase within the neutrophils characterizes patients with cancer and precancerous states of the larynx. Patients with cancer of the larynx show additionally a deficiency of neutrophil myeloperoxidase. Deficiency of N-acetyl-beta-D-glucosaminidase occurs, in contrast, in patients with malignancies of female generation organ. Activity of myeloperoxidase in neutrophils from patients with gastric carcinoma is slightly elevated.
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PMID:Enzymatic deficiencies of the immune system cells in patients with cancer of the larynx and other malignancies. 299 16

In Creutzfeldt-Jakob disease (CJD), there are prominent ultrastructural alterations of the plasma membrane, which contains many glycolipids and glycoproteins. Glycosidases can degrade glycolipids and glycoproteins. Gangliosides, a subset of glycolipids, are decreased in amount at the terminal stages of CJD, and CJD infectivity is closely associated with membrane rich fractions. We therefore studied 10 glycosidases, and found a statistically significant increase in beta-xylosidase, beta-glucuronidase, N-acetyl-beta-D-glucosaminidase and N-acetyl-beta-D-galactosaminidase activities in CJD. In contrast, alpha-glucosidase, beta-glucosidase, alpha-galactosidase, alpha-mannosidase, alpha-fucosidase, and beta-galactosidase were not significantly changed. The above results are consistent with degenerative membrane changes observed morphologically, and with increased degradation of sugar residues on lipids and/or proteins. These changes may be effected by the accumulation of the CJD agent in cell membranes. We suggest that the higher activities of these enzymes in CJD may be partially responsible for some of the structural and biochemical alterations in CJD infected brains.
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PMID:Cerebral glycosidases in experimental Creutzfeldt-Jakob disease. 328 70

Composition of the aqueous phase of mammary secretions during the nonlactating and postpartum periods was determined in nine cows. Protein concentrations increased until several days before parturition and then declined precipitously. Lactose declined rapidly in early involution, remained low during the middle of the nonlactating period, and increased rapidly prepartum. The pH of secretions followed an inverse pattern to lactose and was negatively correlated with lactose during the nonlactating period but not the postpartum period. Peroxidase activity initially increased in secretions in early involution, then declined until parturition when peroxidase activity again increased. Activities of the glycosidic enzymes N-acetyl-beta-D-glucosaminidase, beta-glucuronidase, and alpha-mannosidase increased through the nonlactating period until 2 to 3 wk prepartum, from which time all three enzyme activities declined through the postpartum period. The magnitude of increase in the glycosidases was not the same; peak activity of N-acetyl-beta-D-glucosaminidase increased 20-fold over the activity at d 1 of involution, whereas beta-glucuronidase and alpha-mannosidase increased 4 to 5-fold over the same period.
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PMID:Mammary function during the nonlactating period: enzyme, lactose, protein concentrations, and pH of mammary secretions. 357 23

The influence of repeated aluminium (Al) administration (0.05 or 0.5 mg 100 g-1 b.w.t. i.p. 5 times weekly for 12 weeks) on the lysosomal enzymes N-acetyl-beta-D-glucosaminidase (beta-NAG) and beta-glucuronidase (beta-Gluc) in serum, liver, spleen and kidneys of adult female rats with intact kidneys, (NR), or following partial nephrectomy (5/6 NX) was investigated. After A1 loading, at the high dose only, the beta-NAG in serum and the free beta-NAG in liver, spleen and kidneys increased. Latent beta-NAG levels decreased in all three organs the effect being dose related. Following A1 loading no elevation in total enzyme activity was observed, with one exception. Depending on A1 doses the spleen of the non-operated animals, the liver of both groups of animals and the serum showed a decrease in beta-Gluc activity. No effect on beta-Gluc activity was observed in the spleen of 5/6 NX animals or in the kidneys of either group of animals. The results confirm that high doses of Al induce toxic effects and damage the lysosomes in the liver, the spleen and the kidneys. The results indicate that the extent of lysosomal damage correlates with dose and duration of Al loading. Repeated administration of Al also interferes selectively with enzyme synthesis.
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PMID:Aluminium induced damage of the lysosomes in the liver, spleen and kidneys of rats. 362 85

Methods are described for the quantitative measurement of N-acetyl-beta-D-glucosaminidase, alpha-mannosidase and beta-glucuronidase in peripheral blood leukocytes of the bovine. Enzyme kinetics and stability were determined. Activities of the glycosidases in polymorphonuclear leukocytes and mononuclear leukocytes were determined using the optimized assays. Polymorphonuclear leukocytes had greater activities of N-acetyl-beta-D-glucosaminidase and alpha-mannosidase, and similar levels of beta-glucuronidase, when compared to mononuclear leukocytes.
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PMID:Assays and activities of glycosidic enzymes in bovine peripheral blood leukocytes. 367 96

Leukocytes from mammary secretions in dairy cows were collected during the nonlactating and postpartum periods. Differential cell counts, viability and activity of peroxidase, N-acetyl-beta-D-glucosaminidase (NAGase, beta-glucuronidase and alpha-mannosidase in cells were determined. Cell viability (trypan blue exclusion) was 75-80% during most of the nonlactating period, but declined to 45-50% by parturition. Polymorphonuclear neutrophils (PMN) predominated during the first week of involution, after which macrophages were the predominant cell type. Peroxidase activity in leukocytes from mammary secretions was high in early involution, probably reflecting the predominant peroxidase-containing PMN. Peroxidase activity declined through the remaining nonlactating and postpartum periods. The activity of NAGase was variable in early involution, then increased to a peak during the mid-nonlactating period, before declining prior to parturition. Activity of beta-glucuronidase generally was unchanged during the nonlactating period, although NAGase and beta-glucuronidase activities were significantly and positively correlated throughout the period studied. Activity of alpha-mannosidase changed in a manner similar to peroxidase activity.
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PMID:Lysosomal enzymes in bovine mammary leukocytes during the nonlactating period. 367 97

A quantitative study was carried out on the lysosomal enzyme activities of the bovine corneal endothelium-Descemet's membrane preparation. The corneal endothelium and Descemet's membrane were peeled off together. Cathepsin D was assayed using hemoglobin as substrate; N-acetyl-beta-D-glucosaminidase, beta-glucuronidase, acid phosphatase, and alpha-mannosidase were also examined using p-nitrophenyl derivatives as substrate. The proportions of N-acetyl-beta-D-glucosaminidase, cathepsin D, and beta-glucuronidase of the Descemet's membrane-endothelium complex were particularly high: 11.5%, 12.6%, and 12.5% of the whole cornea, respectively. Corneal endothelial cells also showed high activities of acid phosphatase and alpha-mannosidase (3.8%, and 5.0% of the whole cornea, respectively), while the protein and DNA contents were 0.5% and 0.5% in the complex. Lysosomal enzyme activities in the complex were also compared with those in other ocular tissues and were determined by the same methods at the same time.
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PMID:Lysosomal enzyme activities of the bovine corneal endothelium. 371 Jan 95

The activities of acid phosphatase, N-acetyl-beta-D-glucosaminidase, alpha-mannosidase, alpha-fucosidase, beta-glucuronidase, arylsulfatase, and cathepsin D were biochemically investigated in the bovine cornea by separating the tissue into two layers, epithelium and stroma-endothelium. Acid phosphatase, alpha-mannosidase, alpha-fucosidase, and arylsulfatase disclosed much higher activities in the epithelial layer than in the stroma-endothelial layer. The other enzymes showed little difference in enzyme activity between the two layers.
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PMID:Acid hydrolases in the bovine corneal epithelium. 375 93


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