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)

Acid phosphatase and beta-glucuronidase activities have been determined cytochemically in T, B and null lymphocytes as part of an effort to charaterize the human haemopoietic stem cell. A combination of weak acid phosphatase activity and strong beta glucuronidase staining, in the form of a single large granule, has been shown to be specific for T cells. On the basis of this approach alone, non-T cells could not be further subclassified. Further cytochemical evaluation is being explored.
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PMID:Lysosomal acid hydrolases in human lymphocyte subpopulations. 108 46

Early changes in lysosomal enzymes must occur if their role is significant in irreversible myocardial injury. Therefore, we ligated the anterior descending coronary artery in 14 dogs and after 60 min excised epicardial and endocardial samples from the ischemic and adjacent normal heart. The collateral flow measured with radioactive microspheres in the endocardial samples averaged 19% of control. The muscle was disrupted and fractionated by ultracentrifugation into nuclear pellet (NP), heavy lysosomal pellet (HL), light lysosomal pellet (LL), microsomal pellet (M) and supernate (S). Electron microscopy demonstrated changes characteristic of sichemia in whole tissues and sedimented fractions. Acid phosphatase reaction product was present in residual bodies in the HL fraction and membrane-bound vesicles in the LL fraction and in the intact tissue. Significant decreases in the specific activity of N-acetyl-beta-glucosaminidase and beta-glucuronidase occurred in the endocardial LL fraction, while significant increases in both were found in the ts fraction (P less than 0.05). Losses of acid phosphatase occurred in both LL and S fractions. Moreover, decreases of total N-acetyl-beta-glucosaminidase in the HL fraction and of total beta-glucuronidase and acid phosphatase in the LL fraction were positively correlated (P less than 0.01) with the degree of ischemia measured with radioactive microspheres. Only insignificant enzymatic changes were found when the collateral flow was greater than 40%, and the differences were less significant in epicardial samples where the flow averaged 29%. The early loss of enzymes from the lysosomal fractions in severe ischemia suggests a role for lysosomal hydrolases in the necrosis that follows coronary occlusion.
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PMID:Effect of collateral flow on epicardial and endocardial lysosomal hydrolases in acute myocardial ischemia. 115 94

Extracellular matrix vesicles, which have been shown to be associated with initial calcification of cartilage, were isolated, characterized, and studied with 45calcium isotope to determine whether they could form mineral in vitro. It was found that the isolated matrix vesicles contain a phosphatase, active at neutral pH, which has a very wide specificity and will hydrolyze a variety of nucleotide triphosphates, diphosphates, monophosphates, and other phosphate-containing substrate and metabolites. Acid phosphatase, beta-glucuronidase, and cathepsin D were found to be in the cell fractions, in lysosomes; these enzymes are not present in matrix vesicles and this is additional evidence for the difference between matrix vesicles and lysosomes. Matrix vesicles were found to take up 45Ca even in the presence of low levels of Ca and P1 and also to facilitate precipitation of hydroxylapatite when incubated under physiological conditions in the presence of ATP and other phosphate-containing substrates. Systematic electron probe analysis of a septum of epiphyseal cartilage indicates that matrix vesicles gradually accumulate calcium and then phosphorus and thus facilitate the advance of the calcification front. Adjoinging nonvesicular matrix in the hypertrophic zone, cell cytoplasm, and cell processes had very low levels of calcium and phosphorus in a region where matrix vesicles showed high levels of these elements. New concepts are put forward that take accounts of these findings which provide a better understanding of the sequence of mineralization in growth cartilage.
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PMID:Analysis of matrix vesicles and their role in the calcification of epiphyseal cartilage. 124 46

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

1. Harderian gland porphyrin concentrations were 1.5-fold higher in Fischer-344 male rats than in Sprague-Dawley male rats and there were no differences due to exposure to LD 14:10 (LP) or LD 10:14 (SP) lighting conditions for 8 weeks in either strain. 2. 24-hr periodic regression analyses of porphyrin concentration detected a significant rhythm in both lighting conditions in both strains, with no differences in acrophase due to lighting conditions. 3. In both strains, porphyrin levels were highest in the late phase-early dark period and fell during the early part of the dark period. 4. Acid phosphatase activity did not vary with time (circadian rhythm), strain or photoperiodic lighting condition. 5. Circadian rhythms in beta-glucuronidase, alpha-mannosidase and hexosaminidase activity were present in some instances, but, probably due to the low amplitude to these rhythms, a consistent effect of strain or housing condition was not found. When 24-hr rhythms were observed in either strain, the acrophase occurred during the afternoon-early evening daylight period. 6. A significant effect of strain on mean values of type II 5'-deiodinase activity was noted in Fischer-344 rats. 7. Significant rhythms in type II 5'-deiodinase activity were found in both strains exposed to LD 10:14.
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PMID:Harderian gland porphyrin, lysosomal and type II 5'-deiodinase rhythms in Sprague-Dawley and Fischer-344 rats kept under chronic long- or short-photoperiod conditions. 177 97

Acid phosphatase (AcP), beta-glucuronidase (GR) and N-acetyl-beta-D-glucosaminidase (NAG) activity was determined, using semiquantitative cytochemical methods, in the peritoneal fluid lymphocytes obtained from 50 patients with terminal renal failure treated by intermittent peritoneal dialysis. The control group included 30 subjects with normal renal function. The percentage of AcP and NAG-positive lymphocytes was significantly lower and that of the GR-positive cells significantly higher in dialysed patients than in the control group. A group of 22 dialysed patients with bacterial peritonitis showed a significant increase of the percentage of NAG-positive lymphocytes as compared with both the subjects in the control group and the peritonitis-free dialysed ones. Changes of the lymphocytes enzymatic activities were distinct in cells exhibiting the granular reaction type, and to a much lesser extent in those showing granular diffuse reaction.
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PMID:Activity of some lysosomal enzymes in peritoneal lymphocytes from patients with terminal renal failure treated by intermittent peritoneal dialysis. 178 45

Female B6C3F1 mice were injected intraperitoneally with ammonium metavanadate (2.5 or 10 mg V/kg), ammonium chloride, or sodium phosphate buffer (0.1 M, pH 7.2) every 3 d for 6 wk. Resident peritoneal macrophage (PEM) cytolysates were prepared and assayed for intracellular enzyme activities of beta-glucuronidase, N-acetyl-beta-D-glucosaminidase, acid phosphatase, and lysozyme, to investigate possible reasons for the depressive effect of ammonium metavanadate on the intracellular killing of Listeria monocytogenes by murine PEM. Acid phosphatase activity per 10(6) cells for the 2.5 and 10 mg V/kg groups was depressed by 22.8 and 44.7%, respectively, when compared to phosphate buffer controls. No significant effect by vanadium treatment was observed with regard to the other three enzymes. Kinetic studies (in vitro) on the effect of ammonium metavanadate (5, 10, 15, and 20 mM) on the above enzymes showed similar patterns of effect by vanadium. Lineweaver-Burk analysis of acid phosphatase indicated linear noncompetitive inhibition by vanadium with a Kj of 14.8 mM. NH4Cl and 10 mg V/kg treatments also enhanced extracellular secretion of beta-glucuronidase and lysozyme from PEM, which could be attributed to the presence of ammonium ion. The decrease in acid phosphatase activity might contribute, in part through its interference in the phosphorylation/dephosphorylation, to the diminished intracellular killing ability of PEM.
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PMID:Effect of ammonium metavanadate on the mouse peritoneal macrophage lysosomal enzymes. 203 45

The age-dependent change in activities of seven lysosomal enzymes (cathepsin D, beta-glucuronidase, acid phosphatase, acid/alkaline DNases and acid/alkaline RNases) was studied in four brain regions (cerebrum, hippocampus, pons and cerebellum) of Wistar rats. The activity of cathepsin D was significantly increased with aging in the four regions. The age-dependent change in activities of acid and alkaline DNases showed the characteristic regional difference, and the ratio of acid to alkaline DNases was increased with aging in all regions. Acid RNase showed the lowest activity in 18-month-old rats, and alkaline RNase activity was decreased with aging. The activity of beta-glucuronidase was higher in 2-month-old rats in all of the regions studied. Acid phosphatase showed no significant age-dependent change except in pons. The study demonstrated that all of the lysosomal enzyme activities do not change in parallel with aging, and that the age-dependent change showed the characteristic regional difference.
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PMID:Age-dependent change in activities of lysosomal enzymes in rat brain. 263 Aug 33

Endothelial injury has been proposed as a feature of a wide variety of vascular diseases, and release of endothelial lysosomal hydrolases could contribute to the pathological changes seen. We have determined the relative activities of 14 glycosidases, two esterases and four peptide hydrolases in human umbilical vein endothelial cells and investigated whether known agonists of endothelial function, or materials known to modulate hydrolase secretion in other phagocytic cells, influenced the activity or secretion of these enzymes by human umbilical vein endothelial cells. Hexosaminidase, beta-galactosidase, beta-glucuronidase and alpha-iduronidase accounted for most of the measured glycosidase activity. Acid phosphatase activity greatly exceeded arylsulphatase activity, and most of the measured peptidase activity was due to acid peptidases. Optimum pH and apparent Km values were determined for the most abundant hydrolases. Exposure of human umbilical vein endothelial cells to bradykinin, thrombin or interleukin-1 resulted in negligible release of either hexosaminidase or lactate dehydrogenase (LDH), in contrast to phorbol myristate acetate, which caused a parallel, dose-dependent release of both enzymes. Treatment of these cells with calcium ionophore A23187, trypsin or platelet-activating factor, caused less than 10% release of either hexosaminidase or LDH. Agents known to modulate lysosomal enzyme secretion by other phagocytic cells failed to induce selective secretion of lysosomal enzymes by human umbilical vein endothelial cells.
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PMID:Lysosomal hydrolases of human vascular cells: response to agonists of endothelial function. 264 39

Five different enzyme activities were estimated in ejaculates obtained from 96 men visiting our infertility clinic. Sperm count showed a significant positive correlation with aspartate-aminotransferase (GOT) and alanine-aminotransferase (GPT). Acid phosphatase was positively correlated with gamma-glutamyl transpeptidase (GGTP) and citrate and negatively with fructose. GGTP showed similar relationships with citrate and fructose. For beta-glucuronidase a low positive correlation with GGTP and GOT was detected. The enzyme activities of 27 ejaculates with a high viscosity were not significantly different from the activities of ejaculates with normal liquefaction. The conclusion is reached that insufficient prostatic enzyme secretion is not the cause of abnormal liquefaction in these patients.
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PMID:Enzyme activity of human ejaculates, relation with abnormal liquefaction. 285 13


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