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)

Nine lysosomal enzymes and alkaline phosphatase have been assayed in human pancreatic juice from controls and patients with chronic calcifying pancreatitis. Specific activities were evaluated by a nonparametric test (Wilcoxon) with a probability of 2 P less than or equal to 0.5. The values of acid phosphatase, alpha-glucosidase, beta-glucosidase and alpha-galactosidase are significantly higher in pathological juices; the values of alpha-mannosidase and beta-glucuronidase are also increased in the same patients but at the limit of significance. Alkaline phosphatase, beta-hexosaminidase and alpha-fucosidase follows the same trend but the values are not statistically significant between the two groups of patients. Studies on skin cultures of four patients with chronic calcifying pancreatitis demonstrate that the increased specific activities of lysosomal enzymes in the pathological juices do not correspond to a leakage of these enzymes into the extracellular space as described for cystic fibrosis.
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PMID:Alkaline phosphatase and acid lysosomal hydrolases in pancreatic juice and fibroblast cell cultures of patients with chronic calcifying pancreatitis. 680 85

Enzymatic characterization of 48 Aeromonas hydrophila complex isolates from various sources was determined with the API ZYM system (Analytab Products, Plainview, N.Y.). All isolates lacked valine and cystine aminopeptidases, chymotrypsin, alpha-mannosidase, alpha-fucosidase, alpha-galactosidase, and beta-glucuronidase but possessed caprylate esterase-lipase, leucine aminopeptidase, acid phosphatase, phosphoamidase, and N-acetyl-beta-glucosidase. Variability was found in the presence of alkaline phosphatase, butyrate esterase, myristate lipase, trypsin, beta-galactosidase, alpha-glucosidase, and beta-glucosidase. No significant differences were evident among the enzymatic profiles of isolates from various sources.
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PMID:Enzymatic characterization of Aeromonas hydrophila complex by the API ZYM system. 681 46

Activities of lysosomal hydrolases were measured in the leucocytes of cattle, sheep, goats, horses and pigs. There was high activity of arylsulphatase in leucocytes from cattle, high activities of alpha-fucosidase and beta-glucuronidase in leucocytes from horses and high activity of acid phosphatase in granulocytes from pigs. Within species, arylsulphatase and beta-galactosidase activities were higher in granulocytes than in mononuclear cells, but beta-glucuronidase, phosphodiesterase and alpha-galactosidase activities were higher in mononuclear cells than in granulocytes. Eosinophils of cattle, sheep, goats and horses contained at least 10 times the activity of alpha-mannosidase and arylsulphatase found in neutrophils. For most of the other enzymes studied, there were differences in cattle and goats but not in sheep, horses or pigs between their specific activities in neutrophils and eosinophils.
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PMID:Lysosomal hydrolase activity in leucocytes from cattle, sheep, goats, horses and pigs. 715 6

Retrovirus vectors were constructed to transfer and express the cDNA of the human lysosomal acid hydrolase beta-glucuronidase (GUSB) under control of the human GUSB promoter. Expression of the transcription unit (minigene) was evaluated in a GUSB-negative cell line established from a mouse with the lysosomal storage disease mucopolysaccharidosis (MPS) type VII. A vector designed to transfer single copies of the minigene (N2H beta H) expressed normal levels of GUSB activity in the deficient cells. GUSB expression was increased to several times greater than normal by inserting the minigene into a double-copy vector (DCH beta H), which places one copy of the transcription unit upstream of the retrovirus promoter in both the 3' and 5' long terminal repeats (LTRs) of the integrated provirus. The specific activity of GUSB and a control normal lysosomal enzyme, alpha-galactosidase (GLA), were higher in normal and in vector-corrected cells from confluent cultures than in subconfluent dividing cells. The ratios of GUSB to GLA were similar at all phases of cell growth, but the level of GUSB expression from the double copy vector was several-fold higher than from the single copy vector. To determine if this effect was controlled by the GUSB promoter, a vector was constructed using the thymidine kinase (TK) promoter to drive the human GUSB cDNA (NTK beta H). The levels of GUSB in cells corrected with this vector exhibited the same cell density dependent pattern as when the GUSB promoter was used, indicating that the variation in enzymatic activity was not a function of the GUSB promoter.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:High level expression and export of beta-glucuronidase from murine mucopolysaccharidosis VII cells corrected by a double-copy retrovirus vector. 771 36

The activities of five lysosomal hydrolases--namely beta-glucuronidase, beta-hexosaminidase, beta-galactosidase, alpha-galactosidase, and alpha-mannosidase--were measured in the plasma and urine of children (ages, 7 to 15 years) with sickle cell anemia (n = 11) and controls (n = 11) from Jos, Nigeria. The presence of SS hemoglobin was confirmed by electrophoresis of red cell hemolysates. Albuminuria was absent in all of the patients with sickle cell anemia. The creatinine-indexed urinary activity level (units of enzyme activity/milligrams creatinine) and the fractional enzyme excretion (FEE) value, which is defined as the ratio of enzyme clearance to creatinine clearance, were determined for each of the five lysosomal enzymes and compared between the two groups. The mean FEE values for beta-glucuronidase and alpha-galactosidase in the sickle cell patients were 10- and 3.5-fold lower, respectively, than the corresponding control values, and these differences were statistically significant (p < .03) for both enzymes; however, beta-hexosaminidase, beta-galactosidase, and alpha-mannosidase levels in urine were not different between the two groups. When indexed to creatinine, a comparison of the urinary enzyme levels of control and sickle cell patients showed significant differences for beta-glucuronidase (p < .01) and alpha-galactosidase (p < .05) but not for the other three enzymes. Differences in level of plasma enzyme activity between control and sickle cell patients were not significant, except for alpha-galactosidase (p < .05), which was increased slightly (25%) in the sickle cell group. These data indicate that there may be abnormalities in the metabolism of lysosomal enzymes in the kidneys of patients with sickle cell anemia.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Decreased urinary excretion of beta-glucuronidase in sickle cell anemia in Nigeria. 777 Jun 45

Recombinant mouse beta-glucuronidase administered intravenously to newborn mice with mucopolysaccharidosis type VII (MPS VII) is rapidly cleared from the circulation and localized in many tissues. Here we determine the tissue distribution of injected enzyme and describe its effects on the histopathology in 6-wk-old MPS VII mice that received either one injection of 28,000 U recombinant beta-glucuronidase at 5 wk of age or received six injections of 28,000 U given at weekly intervals beginning at birth. These mice were compared with untreated 6-wk-old MPS VII mice. The single injection decreased lysosomal distention in the fixed tissue macrophage system. MPS VII mice that received multiple injections had 27.8, 3.5, and 3.3% of normal levels of beta-glucuronidase in liver, spleen, and kidney, respectively. Brain had detectable beta-glucuronidase, ranging from 2.0-12.1% of normal. Secondary elevations of alpha-galactosidase and beta-hexosaminidase in brain, spleen, liver, and kidney were decreased compared with untreated MPS VII mice. Although no improvement was observed in chondrocytes, glia, and some neurons, the skeleton had less clinical and pathological evidence of disease and the brain had reduced lysosomal storage in meninges and selected neuronal groups. These data show that recombinant beta-glucuronidase treatment begun in newborn MPS VII mice provides enzyme to most tissues and significantly reduces or prevents the accumulation of lysosomal storage during the first 6 wk of life. Whether therapy begun later in life can achieve this level of correction remains to be established.
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PMID:Enzyme replacement therapy for murine mucopolysaccharidosis type VII. 820 Sep 66

Lysosomal storage diseases (LSD) are caused by deficient activity of specific lysosomal enzymes. Early diagnosis and selective termination is still the trend of therapy. The purpose of this study was to establish an assay system and investigate the reference range of lysosomal enzyme activity of cultured fetal cells in the Chinese population. Seventy amniotic fluid and 9 chorionic villi samples were collected and cultured in this study. Enzyme activity assay was done by synthesized 4-Mu-binded substrates. The activity was expressed as nmol/mg protein/hour. In cultured amniotic cells, the results showed 14-138 of alpha-glucosidase, 8-133 of alpha-galactosidase, 32-470 of alpha-mannosidase, 101-1121 of alpha-fucosidase, 106-1321 of beta-galactosidase, 15-268 of beta-glucosidase, 11-279 of beta-glucuronidase, 101-1193 of Hexosaminidase A, and 886-6204 of N-acetyl-alpha-glucosaminidase. In cultured chorionic villi samples, it showed 22-335 of alpha-glucosidase, 31-230 of alpha-galactosidase, 47-250 of alpha-mannosidase, 35-218 of alpha-fucosidase, 49-934 of beta-galactosidase, 34-329, of beta-glucosidase, 57-379 of beta-glucuronidase, and 328-3412 of Hexosaminidase A. The enzyme activity was not correlated with the gestation age when sample was obtained. Furthermore, there was no statistical significance among the range of amniotic cells, chorionic villi samples, skin fibroblasts and peripheral leukocytes for each enzyme studied. It is suggested that the synthesis of lysosomal enzymes has been mature since the early fetal state, and the samples obtained as early as 8 weeks of gestation age can be used for early diagnosis of lysosomal storage diseases.
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PMID:[Lysosomal enzyme activity of cultured fetal cells in Chinese and its clinical application]. 820 65

The activities of three lysosomal hydrolases and creatinine levels were measured in the plasma and urine of 11 adults (mean age, 28.1 years) with insulin-dependent diabetes mellitus and 14 non-diabetic controls (mean age, 27.9 years). All of the patients were free of diabetic complications and non exhibited microalbuminuria. Fractional enzyme excretion (FEE) values between the two groups of subjects were calculated and compared for the following enzymes: beta-hexosaminidase (N-acetyl-glucosaminidase), beta-glucuronidase and alpha-galactosidase. The FEE value was calculated as the ratio of enzyme clearance to creatinine clearance. Relative to the non-diabetic control group, the FEE value for beta-hexosaminidase was approximately 2-fold lower (P = 0.02) in the diabetic subjects (means, 0.424 vs. 0.242, respectively). The FEE values for beta-glucuronidase and alpha-galactosidase were not significantly different (P > 0.4) between the diabetic and control groups. These easily measured biochemical parameters in blood and urine and the resultant FEE value for beta-hexosaminidase may provide a means of assessing subtle deteriorative changes in renal function which occur in the early stage of diabetes before the onset of clinically evident complications.
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PMID:Decreased renal excretion of beta-hexosaminidase in adults with insulin-dependent diabetes mellitus and normal renal function. 822 63

Creatinine concentrations and the activities of five lysosomal hydrolases were measured in the serum and urine of 14 healthy nonpregnant control women and 19 healthy pregnant women. Fractional enzyme excretion (FEE) values for beta-glucuronidase, beta-hexosaminidase, alpha-galactosidase, beta-galactosidase, and alpha-mannosidase were calculated and compared between the two groups of subjects. Fractional enzyme excretion was calculated as the ratio of enzyme clearance to creatinine clearance. The FEE values for beta-galactosidase and alpha-mannosidase between the nonpregnant and pregnant populations were not statistically different; however, relative to the nonpregnant control group, the median FEE values for beta-glucuronidase (P < 0.03), beta-hexosaminidase (P < 0.06), and alpha-galactosidase (P < 0.02) were decreased approximately 1.5-, 1.8-, and 2.7-fold, respectively, in the pregnant population. The median urinary beta-galactosidase activity for the pregnant population, when expressed on the basis of creatinine, was twofold higher than that of the control group (P < 0.0005). These data indicate that with pregnancy there are marked changes in the urinary excretion of selected lysosomal enzymes, particularly alpha-galactosidase and beta-glucuronidase. When the molecular weights of these five hydrolases were compared between kidney homogenate and control urine, a correlation of 0.96 was observed, while the correlation between control serum and control urine was 0.69. This suggests that the FEE value differences between the pregnant and control groups are most likely due to changes in tubule cell metabolism, either decreased secretion or increased reabsorption. These biochemical changes may provide a means of assessing changes in renal function during pregnancy.
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PMID:Altered urinary excretion of lysosomal hydrolases in pregnancy. 823 9

An epidemiologic study of Pasteurella haemolytica serovar 1 (Ph1) in market-stressed feeder calves from 7 farms in eastern Tennessee was conducted. The nasal mucus of each calf was cultured sequentially at the farm of origin (day 0), at an auction market (day 133), and at a feedyard in Texas (days 141, 148, 155, and 169). Of the 103 calves tested, 77 were culture-positive, including 1 on day 0, 1 on day 133, 20 on day 141, 57 on day 148, 50 on day 155, and 14 on day 169. From the 143 Ph1 isolates, 20 enzyme profiles were determined by use of a commercial enzyme system that detects 19 enzymatic reactions; 4 antimicrobial susceptibility profiles were obtained, using the disk-diffusion method, which evaluated susceptibility to 11 antibacterial drugs. All isolates were positive for acid phosphatase and alkaline phosphatase, but were negative for alpha-galactosidase, alpha-mannosidase, beta-glucosidase, beta-glucuronidase, cystine aminopeptidase, N-acetyl-beta-glucosaminidase, and trypsin. Other positive enzyme reactions included: leucine aminopeptidase, 140 Ph1 isolates; phosphohydrolase, 90 isolates; alpha-fucosidase, 63 isolates; esterase (C4), 59 isolates; valine aminopeptidase, 30 isolates; esterase lipase (C8), 24 isolates; beta-galactosidase, 2 isolates; and alpha-glucosidase, chymotrypsin and lipase (C14), 1 isolate each. Thirty-four Ph1 profiles were identified, using combined enzyme and antimicrobial susceptibility profiles. The data indicate that the strains isolated during the feedyard period may have been determined more by farm of origin (P < or = 0.001) than by habitation with calves from other farms while in the feedyard.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Identification of Pasteurella haemolytica A1 isolates from market-stressed feeder calves by use of enzyme and antimicrobial susceptibility profiles. 842 78


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