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 enzyme activities were examined in granulocytes and lymphocytes from two unrelated patients with Chediak-Higashi syndrome (CHS) in "accelerated phase" and from their family members. In CHS granulocytes, there was a marked reduction of alpha-mannosidase (E.C. 3.2.1.24), alpha-galactosidase (E.C. 3.2.1.22), and alpha-fucosidase (E.C. 3.2.1.51) activities, which were below 21, 24, and 43% of mean control values, respectively. In CHS lymphocytes, beta-glucuronidase (E.C. 3.2.1.31) and alpha-mannosidase activities were also decreased. In granulocytes of family members, the activities of acid phosphatase (E.C. 3.1.3.2), N-acetyl-beta-glucosaminidase (E.C. 3.2.1.30), aryl sulphatase (E.C. 3.1.6.1), and beta-glucuronidase were significantly higher than the control values (P < 0.001), which were 262, 218, 414, and 180% of mean control values. Neither the inhibitor in CHS granulocytes nor the activator in the heterozygous granulocytes to those enzymes could be found by mixing experiments with normal ones.
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PMID:Chediak-Higashi syndrome: abnormal lysosomal enzyme levels in granulocytes of patients and family members. 625 36

The condition for maximal activity (pH, buffer, saturating substrate concentration, range of linear relationships between enzyme activity versus incubation time, and versus enzyme concentration) in the fluorimetric assay of several glycohydrolases of lysosomal origin in human plasma and serum have been established. The following enzymes were studied: alpha-galactosidase, beta-galactosidase, beta-N-acetylglucosaminidase, beta-glucosidase, beta-glucuronidase, alpha-mannosidase, alpha-fucosidase. All examined enzymes turned out to be more or less unstable upon storage at 37 degrees C, 4 degrees c, and -20 degrees C in both serum and plasma. The only exceptions were beta-glucuronidase, which was stable in plasma and serum, and alpha-fucosidase which was stable only in plasma. Generally the degree of instability was greater in serum than in plasma. The levels of some enzymes (alpha-galactosidase, beta-galactosidase, beta-N-acetyl glucosaminidase, beta=glucuronidase) were markedly higher in serum than in plasma; conversely the levels of the same enzymes in "platelet free" serum equalled those in plasma. This stresses the necessity to use freshly prepared plasma for lysosomal glycohydrolase assay. Under the procedural conditions recommended for the assay the methods for the determination of lysosomal glycohydrolases in plasma appeared to be simple, sensitive and reproducible.
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PMID:Enzymes of lysosomal origin in human plasma and serum: assay conditions and parameters influencing the assay. 625 26

The enzyme activities of alpha-fucosidase (pH 4.0 and pH 5.5), alpha-galactosidase, beta-galactosidase, alpha-glucosidase (pH 4.5 and pH 6.0), beta-glucosidase, beta-glucuronidase, beta-hexosaminidase, and alpha-mannosidase (pH 4.5 and pH 5.5) were investigated in sera from cystic fibrosis (CF) patients. Several of these activities were significantly increased in sera from patients compared to age-matched control children. CF-patients in a more advanced stage of the disease had a tendency to higher values of some of these hydrolases than those in better condition. No new isoenzymes of these hydrolases were found. Only minor differences could be detected in the pH-profiles of alpha-mannosidase and acid phosphatase from age-matched normal controls, heterozygotes and homozygotes for CF. With our technique, alpha-mannosidase and acid phosphatase showed the same thermostability in CF-patients. CF-heterozygotes and age-matched controls, except at 56 degrees C, when the activity of acid-phosphatase in the plasma from adult CF-heterozygotes decreased more than that from adult controls
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PMID:Acid hydrolases in sera and plasma from patients with cystic fibrosis. 626 20

The beta-N-acetylhexosaminidase, beta-glucuronidase, alpha-galactosidase, beta-galactosidase and alpha-L-fucosidase activities, in six different species of molluscs, have been studied. The optimum pH was acid in all cases, in agreement with the lysosomal origin of these enzymes. They generally show several pI in their isoelectrofocusing profiles. Kinetic studies with enzymes having several activities in one protein, i.e. beta-N-acetylhexosaminidase and beta-galactosidase, have been carried out with mixed substrates in order to determine the occurrence of several active sites. The action of these enzymes on glycosidic rests containing natural substrates has been studied by enzymatic hydrolysis.
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PMID:[Glycosidases of various mollusks: general properties, kinetic studies and action on natural substrates]. 629 19

It has been suggested that high levels of urinary beta-glucuronidase may increase an individual's risk of bladder cancer by releasing free carcinogens from their inactive glucuronide conjugates in the bladder. The hypothesis derives in part from the high levels of urinary beta-glucuronidase observed in bladder cancer patients. Because most of the individual variation in levels of urinary beta-glucuronidase and other lysosomal enzymes in the normal population is genetically determined, we would expect that, if high glucuronidase levels were a predisposing factor in the disease, bladder cancer patients would transmit this trait to their progeny. We have tested this hypothesis and find that levels of urinary beta-glucuronidase and three other lysosomal enzymes, alpha-galactosidase, beta-galactosidase, and beta-hexosaminidase, are not significantly elevated in 34 progeny of bladder cancer patients compared to 34 matched controls. Additionally, 15 bladder cancer patients judged to be disease free for a median time of 5 years did not have elevated levels of urinary beta-glucuronidase when compared to a normal population of 125 individuals. Thus, the high levels of glucuronidase observed in bladder cancer patients are most likely a consequence of disease rather than a cause.
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PMID:Role of urinary beta-glucuronidase in human bladder cancer. 633 54

Ten enzymes, all known to be glycoproteins, were examined by electrophoresis or gel isoelectric focusing in 12 different patients with primary or secondary sialidase deficiency. Aberrant electrophoretic mobilities of many of the enzymes attributable to abnormal sialylation were found in all the patients. In ten of the patients seven of the enzymes were affected. The unaffected enzymes were beta-galactosidase, alkaline phosphatase and beta-glucuronidase. In the cells from the two patients with I cell disease (mucolipidosis II) in which sialidase is one of many deficient enzymes, beta-galactosidase, alpha-galactosidase, alpha-fucosidase and alpha-mannosidase were undetectable, alkaline phosphatase showed a normal electrophoretic mobility and acid phosphatase, adenosine deaminase, alpha-glucosidase and beta-D-N-acetylhexosaminidase showed aberrant mobilities.
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PMID:Electrophoretic analysis of glycoprotein enzymes in the sialidoses and mucolipidoses. 645 53

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


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