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)

Urinary excretion of lactate dehydrogenase, hydroxybutyrate dehydrogenase, gamma-glutamyltransferase, alkaline phosphatase, arylsulphatase A, alpha-glucosidase, beta-galactosidase, trehalase, N-acetyl-beta-glucosaminidase, beta-glucuronidase, and leucinearylamidase was studies in a carefully selected group of 100 healthy subjects, 50 women and 50 men. Enzyme activities were assayed in 3-h morning samples after gel filtration of the urine. Activities were related to time volume, and to urinary creatinine concentration. Several transforming functions had to be applied to enzyme output data to obtain an approximation to gaussian frequency distribution. Men showed a significantly higher excretion of gamma-glutamyltransferase, alpha-glucosidase, trehalase, N-acetyl-beta-glucosaminidase,beta-glucuronidase, and leucine arylamidase activity than did women if enzyme activity was related to urinary time volume. Women excreted more lactate dehydrogenase, hydroxybutyrate dehydrogenase, gamma-glutamyltransferase, alkaline phosphatase, alpha-glucosidase, trehalase, and N-acetyl-beta-glucosaminidase activity than did men, if urinary creatinine was used as the basis of reference. Reference intervals were calculated as 2.5 and 97.5 percentiles for both sexes.
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PMID:Normal limits of urinary excretion of eleven enzymes. 1 92

We studied the influence of chlorpromazine on the release of enzymes (beta-glucuronidase, EC 3.2.1.31; lactate dehydrogenase, EC 1.1.1.27; pyruvate kinase, 2.7.1.40) and proteins using human granulocytes isolated and maintained at 37 degrees C. Chlorpromazine had a biphasic effect on enzyme release and the inhibition of the glycolytic pathway could be demonstrated only at high concentrations of chlorpromazine, after one hour's incubation. The NAD+/NADH ratio was significantly perturbed at all the concentrations. This effect is time dependent. The action of 4 other phenothiazine derivatives made it possible to establish a relationship between their physico-chemical properties and protein release. The results are compared with those from other studies using other biological materials.
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PMID:Protein and enzyme release from human leukocytes: influence of phenothiazine derivatives. 2 5

Assay conditions have been developed for the determination of urinary beta-glucuronidase, beta-galactosidase, alpha-galactosidase, and beta-hexosaminidase using fluorometric substrates. The assay conditions for beta-glucuronidase overcome interference by both low and high molecular weight inhibitors, a problem that has confused earlier studies of enzyme excretion. The four lysosomal enzymes are excreted corrdinately: although their absolute levels (in units per milligram of creatinine) vary during the day and from one day to the next, the ratio of one enzyme to another remains relatively constant. The lack of correlation betweem plasma and urine enzyme levels, together with the high molecular weights of these enzymes, suggests that the urinary enzymes are not derived by glomerular filtration. The lack of coordinacy with lactate dehydrogenase suggests they are not derived from exfoliated cells. by analogy with experimental animals, they may be derived from lysosomes extruded into the lumen of the proximal tubule by epithelial cells. There is considerable variation among a population of 125 healthy adult subjects for total enzyme excretion. Both total enzyme excretion and coordinacy ratios are log-normally distributed, suggesting that they are the resultants of many factors, each of which has a relative, or proportional, effect on enzyme excretion. About one-half the population variation resides in a process common to the excretion of all four enzymes (possibly the lysosome extrusion pathway), and about one-half resides in factors affecting each enzyme independently.
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PMID:Coordinacy of lysosomal enzyme excretion in human urine. 2 85

Peritoneal macrophages were obtained from untreated mice and from mice treated with thioglycollate medium (TA), proteose peptone medium (PP), or a suspension of streptococcus A cell wall material (SA). The biochemical and secretory properties of these cells in long term cultures (up to 2 wk) were compared. TA-elicited macrophages contained more protein, lactate dehydrogenase, lysosomal hydrolases, and in particular, more plasminogen activator than the other cells studied. All types of macrophages studied were found to release considerable amounts of lysosomal hydrolases (beta-glucuronidase, N-acetyl-beta-glucosaminidase, alpha-mannosidase, and acid phosphatase) into the medium. Release was independent of phagocytosis and must, therefore, be regarded as true secretion. In both elicited and nonelicited macrophages, the rates of lysosomal enzyme secretion were virtually identical in the presence and in the absence of serum, and they were not enhanced by increasing serum concentrations. Lysosomal enzyme secretion in macrophages appears to depend on protein synthesis, since it was blocked by low concentrations of cycloheximide which neither affected cell viability nor lowered the intracellular enzyme levels. The amounts of lysosomal hydrolases secreted were highest in TA-elicited macrophages. The rates of secretion of PP- or SA-elicited and of nonelicited macrophages were about one-fourth of that of the TA-elicited cells. This difference, although significant, is much smaller than that observed for the secretion of plasminogen activator which was 20-50 times higher in TA-elicited cells. Acid glycosidases were also found in the peritoneal lavage media used for cell harvesting from both treated and nontreated mice. This indicates that active secretion of lysosomal hydrolases may be an in vivo property of the macrophage.
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PMID:Secretion of lysosomal hydrolases by stimulated and nonstimulated macrophages. 2 35

Activities of 9 enzymes were determined biochemically in the endometrium. In Trial I (five women) 25 mg progesterone were injected i.m. on day 9 of the cycle; and endometrial biopsy taken 24 hours later was compared with endometrium from day 10 and day 21, taken in two untreated cycles from the same volunteers. Similarly, in Trial II (five women) 50 mg progesterone were injected on day 9, biopsy taken on day 11 and compared with days 11 and 21 from untreated cycles. The specific activites of lactate dehydrogenase, isocitrate dehydrogenase (ICDH), malate dehydrogenase, glutamate dehydrogenase, beta-glucuronidase, acid phosphatase (ACP) and alkaline phosphatase (AP) were significantly higher in the secretory phase. Twenty-five milligrams progesterone (after 24 hours) caused increases of some enzymes, significant only for AP. Fifty milligrams (after 48 hours) increased significantly the activity of ICDH and ACP. Biochemical changes, especially increase of ICDH, can be used for detection of the effect of progesterone on the endometrium.
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PMID:Effect of endogenous and exogenous progesterone on human endometrial enzymes. 3 Jul 6

The urinary excretion of lactate dehydrogenase, gamma-glutamyltransferase, alkaline phosphatase, arylsulphatase A, alpha-glucosidase, beta-galactosidase, trehalase, N-acetyl-beta-glucosaminidase, beta-glucuronidase, and leucine arylamidase was studied in 68 patients with biopsy-proved glomerular, 54 with interstitial renal disease and in 97 patients suffering from primary hypertension. The enzyme output of these 219 patients was compared to that of a reference population of 100 thoroughly selected healthy subjects. The highest incidence of elevated enzyme excretion was observed for N-acetyl-beta-glucosaminidase with 88% in glomerulopathies and 78% in interstitial disease, followed by beta-galactosidase. 94% of the patients with glomerular kidney disease, 90% of those with interstitial disease and about 60% of the subjects with primary benign hypertension revealed an output of at least one enzyme above upper reference limit. The highest average enzymuria occured in glomerulopathies, particularly high values in patients with the nephrotic syndrome. Application of discriminant analysis to the urinary enzyme pattern of glomerular and interstitial renal diseases resulted in an overall correct classification into the appropriate group of 89% of all patients. The discrimination between glomerular and interstitial disease was better in patients with normal renal function than in those with reduced function. Results show, that the analysis of urinary enzyme patterns may be a helpful adjunct for differential diagnosis of kidney diseases.
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PMID:Evaluation of urinary enzyme patterns in patients with kidney diseases and primary benign hypertension. 3 57

The following enzymatic activities were measured in serum of patients with benign and malignant ovarian tumors before treatment: alkaline and acid phosphatases, aspartyl (AspAT) and alanyl (AlAT) aminotransferases, leucyl (LAP) and alanyl (AAP) aminopeptidases, lactate dehydrogenase (LDH), gamma-glutamyl transpeptidase, cathepsin, alkaline ribonuclease (RNase) and beta-glucuronidase. It was shown that at least three determinations (phosphatases and LAP) are practically useless in a discrimination between the examined groups. RNase in combination with AspAT (AlAT) or RNase with AAP and LDH were found to give the best results as marker enzymes.
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PMID:Serum enzymes in ovarian carcinoma. 4 48

The ability of Escherichia coli which possess or lack mannose-sensitive adherence factors (adhesins) to associate with human peripheral leukocytes in vitro in the absence of serum was studied. E. coli 19+, which have mannose-sensitive adhesins, were derived from E. coli strain 19 by culturing in static Trypticase soy broth at 37 degrees C. E. coli 19-, which lack mannose-sensitive adhesins, were derived from E. coli 19 by culturing in agitated Trypticase soy broth at 30 degrees C. E. coli 19+ attached to leukocytes and stimulated the release of lysozyme but not beta-glucuronidase or lactate dehydrogenase. In contrast, E. coli 19- showed poor attachment to the leukocytes and failed to stimulate lysosomal enzyme release. During a 60-min incubation with the leukocytes, the number of viable 19+ organisms decreased, whereas the number of viable 19- remained constant. Purified type 1 pili from E. coli 19+ agglutinated the leukocytes but did not stimulate lysosomal enzyme release. Pretreatment of leukocytes with type 1 pili failed to prevent the adherence of E. coli 19+. The association of 19+ with leukocytes and subsequent release of lysozyme could be blocked by alpha-methyl-D-mannoside but not by equivalent concentrations of dextrose and sucrose. These results show that mannose-sensitive adhesins on E. coli mediate association of the organisms with leukocytes in the absence of serum components. The identity of the adhesins involved in leukocyte association has yet to be determined.
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PMID:Mannose-sensitive interaction of Escherichia coli with human peripheral leukocytes in vitro. 4 3

In order to determine the possible mechanisms whereby interactions between phagocytic cells and crystals of monosodium urate (MSU) lead to cell death with simultaneous release of both cytoplasmic and lysosomal enzymes, phagocytic leukocytes of the smooth dogfish shart Mustelus canis were studied by means of light and electron microscopy, and biochemistry. Lysosomes of these cells can be stained supravitally with toluidine blue and are large enough (0.7-0.8 mu) to be clearly resolved with the light microscope. Light microscopic observations showed that of cells exposed to MSU 87% of those containing visible ingested crystals died within 1 hour, whereas 92% of adjacent cells in the same wet mount without such srystals survived. Cell death occured after a latent period of 10-15 minutes following fusion of lysosomes with crystal-containing phagosomes. Electron microscopic examination of both dogfish and human leukocytes exposed to MSU for more than 1 hour and then fixed in situ revealed occasional discontinuities or ruptures in secondary lysosome membranes. Endogenous peroxidase activity could be cytochemically localized in primary and secondary lysosomes and in the cytoplasm adjacent to such ruptured secondary lysosomes. It was not seen adjacent to primary lysosomes, a result indicating that the cytoplasmic reaction product was not a diffusion artifact. To exclude the possibility that crystals were exercising their affect primarily upon the plasma membrane, suspensions of dogfish buffy coat cells were incubated with cytochalasin B (5 mug/ml, 10 minutes), which inhibits phagocytosis but not exocytosis of lysosomal enzymes by stimulated phagocytes. Whereas cells exposed to MSU crystals released 30% of their content of lysosomal beta-glucuronidase activity and 28% of their cytoplasmic lactate dehydrogenase (LDH) activity within 3 hours, preincubation with cytochalasin B reduced the release of LDH activity within that period to 6% but reduced the release of beta-glucuronidase activity only to 20%. Preincubation with 10-3 M cyclic adenosine monophosphate (cAMP) and theophylline (10-3 M), which inhibit lysosomal fusion, reduced the release of both LDH and beta-glucuronidase activities to 7% and 6% respectively. Cells that were preincubated with both cytochalasin B and cAMP + theophylline released only 1% LDH activity and 4% beta-blucuronidase activity. These results are compatible with the "suicide sac" hypothesis of lysosomal enzyme release mediated by MSU for the following reasons: a) cell death was seen to follow uptake, not mere exposure to crystals, b) ultrastructural studies indicated that the primary injury was to the secondary lysosome membrane, and c) cell death was reduced when either phagocytosis or lysosomal fusion was inhibited.
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PMID:Mechanisms of lysosomal enzyme release from leukocytes. IV. Interaction of monosodium urate crystals with dogfish and human leukocytes. 4 82

Several pharmacologic agents were tested for inhibition of phagocyte-induced release of lysosomal enzymes from guinea-pig alveolar mononuclear cells and peritoneal leukocytes. The activities of the lysosomal enzyme beta-glucuronidase and the cytoplasmic enzyme lactate dehydrogenase were determined in the cells and media following a 2-hour incubation period of cells and zymosan particles. Adrenergic and cholinergic agents, the 3,'5'-adenosine and guanosine cyclic nucleotides, and theophylline had no effect on phagocytosis or release of beta-glucuronidase or lactate dehydrogenase from alveolar cells. Cytochalasin B stimulated lysosomal but not cytoplasmic enzyme release from these cells in the absence of zymosan. Colchicine and hydrocortisone inhibited phagocytosis and beta-glucuronidase extrusion, and phenylbutazone inhibited only beta-glucuronidase release. Colchicine and phenylbutazone also inhibited enzyme release stimulated by cytochalasin B indicating that they were affecting postphagocytic events. The cyclic nucleotides and theophylline were without effect on the peritoneal leukocytes; dexamethasone and phenylbutazone inhibited enzyme release with only the former antagonizing phagocytosis.
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PMID:Effects of pharmacologic agents on release of lysosomal enzymes from alveolar mononuclear cells. 16 51


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