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PubMed1989

Developmental and environmental regulation of a phenylalanine ammonia-lyase-beta-glucuronidase gene fusion in transgenic tobacco plants.

A 1.1-kilobase promoter fragment of the bean (Phaseolus vulgaris L.) phenylalanine ammonia-lyase (EC 4.3.1.5) gene PAL2 was translationally fused to the beta-glucuronidase reporter gene and transferred to tobacco by Agrobacterium tumefaciens-mediated leaf disk transformation. The distribution of beta-glucuronidase activity in these transgenic plants is very similar to that of endogenous PAL2 transcripts in bean, with very high levels in petals; marked accumulation in anthers, stigmas, roots, and shoots; and low levels in sepals, ovaries, and leaves. Histochemical analysis of the spatial pattern of beta-glucuronidase activity showed that the PAL2 promoter is highly active in the shoot apical meristem, the zone of cell proliferation immediately adjacent to the root apical meristem, and in the early stages of vascular development at the inception of xylem differentiation. Wounding and light evoke specific changes in the spatial pattern of beta-glucuronidase activity in stems, including induction in the epidermis. These data indicate that the PAL2 promoter transduces a complex set of developmental and environmental cues into an integrated spatial and temporal program of gene expression to regulate the synthesis of a diverse array of phenylpropanoid natural products.

Ammonia-Lyases↗
PubMed1990

The overexpressed human 46-kDa mannose 6-phosphate receptor mediates endocytosis and sorting of beta-glucuronidase.

We studied the function of the human small (46-kDa) mannose 6-phosphate receptor (SMPR) in transfected mouse L cells that do not express the larger insulin-like growth factor II/mannose 6-phosphate receptor. Cells overexpressing human SMPR were studied for enzyme binding to cell surface receptors, for binding to intracellular receptors in permeabilized cells, and for receptor-mediated endocytosis of recombinant human beta-glucuronidase. Specific binding to human SMPR in permeabilized cells showed a pH optimum between pH 6.0 and pH 6.5. Binding was significant in the presence of EDTA but was enhanced by added divalent cations. Up to 2.3% of the total functional receptor could be detected on the cell surface by enzyme binding. We present experiments showing that at very high levels of overexpression, and at pH 6.5, human SMPR mediated the endocytosis of beta-glucuronidase. At pH 7.5, the rate of endocytosis was only 14% the rate seen at pH 6.5. Cells overexpressing human SMPR also showed reduced secretion of newly synthesized beta-glucuronidase when compared to cells transfected with vector only, suggesting that overexpressed human SMPR can participate in sorting of newly synthesized beta-glucuronidase and partially correct the sorting defect in mouse L cells that do not express the insulin-like growth factor II/mannose 6-phosphate receptor.

Animals↗
PubMed1993

In vivo analysis of Chlamydomonas chloroplast petD gene expression using stable transformation of beta-glucuronidase translational fusions.

We have used the Escherichia coli beta-glucuronidase (uidA) gene as a reporter gene to localize the promoter and analyze the function of the 5' untranslated region (UTR) of the Chlamydomonas chloroplast petD gene. Using particle bombardment, petD-uidA transcriptional and translational fusion genes were introduced into the chloroplast genome in the large inverted repeat flanking the atpB gene. In transformants carrying a petD-uidA transcriptional fusion, uidA mRNA accumulated but was not translated. However, in a translational fusion that included the entire petD 5' UTR, uidA mRNA accumulated and a high level of beta-glucuronidase activity was detected. When approximately 70% of the petD 5' UTR was deleted from the translational fusion, uidA mRNA accumulation and beta-glucuronidase activity decreased 4- to 6-fold and 8-fold, respectively. Run-on transcription assays demonstrated that all strains transcribe the uidA gene at equivalent rates. Our results show that sequences essential for translation reside in the petD 5' UTR and also that sequences within the 5' UTR directly or indirectly affect mRNA stability. The expression of beta-glucuronidase under the control of chloroplast transcriptional and translational signals will facilitate further studies of chloroplast gene regulatory mechanisms.

Animals↗
PubMed2003

Klotho is a novel beta-glucuronidase capable of hydrolyzing steroid beta-glucuronides.

klotho mutant mice provide a unique model to analyze mechanisms of aging because their phenotypes resemble those of human aging-associated disorders. The klotho gene encodes Klotho, a type I membrane protein that shares sequence similarity with members of the glycosidase family 1. Because Klotho lacks the glutamic acid residues that have been shown to be involved in the catalytic activity of this family of enzymes, the function of this protein was unknown. Here, we have studied the biochemical characteristics of recombinant Klotho. The purified chimeric Klotho-human IgG1 Fc protein (KLFc) was assayed with a series of 4-methylumbelliferyl (4Mu) beta-glycosides as potential substrates. An enzymatic activity of Klotho was observed only with 4-methylumbelliferyl beta-D-glucuronide in contrast to bovine liver beta-glucuronidase, which exhibits a rather wide substrate specificity. Furthermore, the enzymatic activity of KLFc was reduced by the addition of specific inhibitors of beta-glucuronidase. A number of natural beta-glucuronides were screened by competitive inhibition for KLFc beta-glucuronidase. We found that steroid beta-glucuronides such as beta-estradiol 3-beta-D-glucuronide, estrone 3-beta-D-glucuronide, and estriol 3beta-D-glucuronide were hydrolyzed by KLFc. The artificial fluorescent substrate and the steroid conjugates share a common phenolic structure. Collectively, these data suggest that Klotho functions as a novel beta-glucuronidase and that steroid beta-glucuronides are potential candidates for the natural substrate(s) of Klotho.

Animals↗
PubMed1983

Receptor-mediated entry of beta-glucuronidase into the parasitophorous vacuoles of macrophages infected with Leishmania mexicana amazonensis.

125I-labeled rat preputial gland beta-glucuronidase was shown by light and electron microscopic radioautography to accumulate within the parasitophorous vacuoles of in vitro derived bone marrow macrophages infected with Leishmania mexicana amazonensis. beta-glucuronidase uptake was mediated by the mannose receptor, since the penetration of the ligand was inhibited by mannan. Uptake was detected as soon as 4 h after incubation of infected cells with the ligand, and increased at 24 and 48 h. The label persisted in the vacuoles for at least 24 h after a 24-h pulse with the ligand, a finding compatible with the relatively long half-life of labeled beta-glucuronidase in normal macrophages. Parasitophorous vacuoles were also labeled in macrophages exposed to the ligand only before infection, indicating that secondary lysosomes containing the ligand fused with the parasitophorous vacuoles. Another mannosylated ligand, mannose-BSA, which, in contrast to beta-glucuronidase, is rapidly degraded in macrophage lysosomes, did not detectably accumulate in the vacuoles. The results support and extend information previously obtained with electron opaque tracers that emphasizes the phagolysosomal nature of Leishmania parasitophorous vacuoles. In addition, the results suggest that appropriate mannosylated molecules may be used as carriers for targeting of leishmanicidal drugs to the parasitophorous vacuoles of infected macrophages.

Animals↗
PubMed1996

The influence of flaxseed and lignans on colon carcinogenesis and beta-glucuronidase activity.

Flaxseed, the richest source of mammalian lignan precursors, such as secoisolariciresinol diglycoside (SD), has been shown over the short term to decrease some early markers of colon cancer risk. This study determined whether over the long term flaxseed still exerts a colon cancer protective effect, whether its effect may, in part, be due to its high content of SD and whether any change in beta-glucuronidase activity plays a role in the protective effect. Six groups of male Sprague-Dawley rats were fed for 100 days either a basal high fat (20%) diet (BD), BD supplemented with 2.5 or 5% flaxseed or 2.5 or 5% defatted flaxseed (equivalent to the respective flaxseed diets) or BD with a daily gavage of 1.5 mg SD. All rats were injected with a single dose of azoxymethane (15 mg/kg body wt) 1 week prior to commencing the dietary treatments. Urinary lignan excretion, which is an indicator of mammalian lignan production, was significantly increased in the flaxseed and defatted flaxseed groups. The total activity of cecal beta-glucuronidase was significantly increased in a dose-dependent manner by the flaxseed and defatted flaxseed diet groups. Compared with the control the number of aberrant crypts per focus was significantly reduced in the distal colon of the treated rats. Four microadenomas and two polyps were observed in the control group, but not in the treated groups. The total activity of beta-glucuronidase was positively correlated with total urinary lignan excretion and negatively with the total number of aberrant crypts and the total number of aberrant crypt foci in the distal colon. There were no significant differences between the flaxseed and the corresponding defatted flaxseed groups. It is concluded that flaxseed has a colon cancer protective effect, that it is due, in part, to SD and that the protective effect of flaxseed is associated with increased beta-glucuronidase activity.

Animals↗
PubMed1985

Effect of exogenous beta-glucuronidase on the carcinogenicity of 1,2-dimethylhydrazine in rats: evidence that carcinogenic intermediates form conjugates and act through their subsequent enzymatic release.

Albino, outbred 3-month-old rats were given a single s.c. dose of 1,2-dimethylhydrazine dihydrochloride (DMH; 100 mg/kg) and, 6 or 24 h later, an i.v. dose of bovine liver beta-glucuronidase (3 X 10(4) Fishman units). After this treatment, the incidence of tumours of the large intestine and Zymbal gland, and of cystocholangiomas was similar to that found in rats treated with DMH alone; the incidence of malignancies in various other tissues was considerably higher than that in rats treated only with DMH, especially in animals exposed to beta-glucuronidase 24 h after administration of DMH. beta-Glucuronidase itself had no carcinogenic activity. The broadening of the spectrum of malignant tumours produced in DMH-treated rats by administration of beta-glucuronidase indicates that the carcinogenic effect of DMH may be exerted through formation of comparatively stable conjugates of its metabolites and their enzymic release in target tissues. The approach used in this study could be helpful in investigating the formation of conjugates from other carcinogens.

1,2-Dimethylhydrazine↗
PubMed1986

Beta-glucuronidase mutants of the nematode Caenorhabditis elegans.

Using a screening procedure that is based on a histochemical stain for the enzyme beta-glucuronidase, we have isolated several mutants of the nematode Caenorhabditis elegans affected in beta-glucuronidase activity. All of the mutations fall into one complementation group and identify a new gene, gus-1, which has been mapped on the right arm of linkage group I (LG I), 1.1 map units to the left of unc-54. The mutants have no visible phenotype, and their viabilities and fertilities are unaffected. Linked revertants of two of the mutations have been isolated. They restore enzyme activity to almost wild-type levels; the beta-glucuronidase that one of the revertants produces differs from that of the wild type. We propose that gus-1 is the structural locus for beta-glucuronidase.

Alleles↗
PubMed1995

Four novel mutations in mucopolysaccharidosis type VII including a unique base substitution in exon 10 of the beta-glucuronidase gene that creates a novel 5'-splice site.

Mucopolysaccharidosis type VII (MPS VII), or Sly syndrome, is a lysosomal storage disorder caused by a deficiency in the enzyme beta-glucuronidase. Various clinical phenotypes of this autosomal recessively inherited disease have been described. Recent isolation and characterization of human beta-glucuronidase cDNA and the genomic sequences facilitate analysis of molecular defects underlying the different phenotypes, and eight mutations in the beta-glucuronidase gene have been described. This report summarizes studies characterizing four new mutations in two Caucasian patients with a severe form of MPS VII. Three are point mutations, resulting in two missense and one nonsense change, and one is a 38 bp deletion. The first patient was a compound heterozygote having P148S and Y495C alleles. The second patient was a compound heterozygote of W507X and a 38 bp deletion at position 1642-1679 in exon 10(1642 delta 38nt). The 38 bp deletion was caused by a single base change mutation in exon 10 that generates a new, premature 5' splice site. Expression of mutant cDNAs encoding each of the four mutations showed that all four resulted in a severe reduction of beta-glucuronidase activity, indicating that these mutations are responsible for the reduced enzyme activity in patient cells. These four previously undescribed mutations provide further evidence for the broad molecular heterogeneity in Sly syndrome.

Base Sequence↗
PubMed1986

Effect of hyaluronidase, beta-glucuronidase and beta-N-acetylglucosaminidase inhibitors on sperm penetration of the mouse oocyte.

The role of hyaluronidase, beta-glucuronidase and beta-N-acetylglucosaminidase in the penetration by mouse spermatozoa through the layers surrounding the oocyte was investigated by in vitro techniques. Myocrisin, fenoprofen, phosphorulated hesperidin and PS53 (a hydroquinone-sulfonic acid-formaldehyde polymer) inhibited fertilization when incubated with capacitated spermatozoa before the treated spermatozoa were mixed with intact oocytes but not when the inhibitor-treated, capacitated spermatozoa were added to oocytes free of follicle cells. The antifertility activity did not appear to be due to an effect on sperm motility or on the oocytes. These 4 compounds are known hyaluronidase inhibitors and, of the acrosomal enzymes tested, only share inhibition of hyaluronidase. Kinetic studies indicated that myocrisin is a reversible inhibitor of mouse sperm hyaluronidase whereas the other three are irreversible inhibitors. Adding saccharolactone, a beta-glucuronidase inhibitor, or N-acetylglucosaminolactone and N-acetylgalactosaminolactone, beta-N-acetylglucosaminidase inhibitors, to capacitated spermatozoa under the same conditions as the hyaluronidase inhibitors did not decrease fertilization. This was the case even though the beta-glucuronidase or beta-N-acetylglucosaminidase activities of the spermatozoa were completely inhibited, at least at the time that the inhibitor-treated, capacitated spermatozoa were mixed with the oocytes. The hyaluronidase activity of mouse spermatozoa remained unaltered during the incubation period required for capacitation; however, prolonged incubation caused a significant decrease in hyaluronidase. Untreated mouse spermatozoa caused hydrolysis of hyaluronic acid more effectively than did sperm extracts obtained by detergent extraction. These results are consistent with the theory of an essential role of hyaluronidase in mouse fertilization. At least in this species, the enzyme appears to be specifically involved in sperm penetration through the follicle cell layer. The data do not support an essential role for beta-glucuronidase and beta-N-acetylglucosaminidase in the penetration by mouse spermatozoa through the oocyte's investments. In contrast to some other species, sperm capacitation in mice does not result in a loss of hyaluronidase although part of the enzyme activity is lost on prolonged incubation. Mouse spermatozoa appear to be able to digest substrate (hyaluronic acid) even though hyaluronidase is not released.

Acetylglucosaminidase↗
PubMed1977

Cutaneous beta-glucuronidase: cleavage of mycophenolic acid by preparations of mouse skin.

Mycophenolic acid, a new chemotherapeutic agent for the treatment of psoriasis, is known to be rapidly conjugated on absorption and to circulate largely in the form of its glucuronide conjugate. Since this metabolite does not readily penetrate intact cells and is cleaved by the enzyme beta-glucuronidase to yield free mycophenolic acid, the ability of preparations of mouse skin to cleave mycophenolic glucuronide was studied. The time course of mycophenolic acid liberation by such preparations and the dependence upon the amount of enzyme preparation were demonstrated. Preparations of mouse skin and mouse liver, kidney, spleen, lung, heart and small intestine were assayed for beta-glucuronidase activity using p-nitrophenyl-beta-D-glucuronide as substrate. Skin yielded preparations with higher beta-glucuronidase activity per/mg protein than any of the other organs tested. When expressed on the basis of beta-glucuronidase activity recovered per milligram of tissue DNA, skin, liver and kidney showed higher levels than the other organs tested.

Animals↗
PubMed1978

The release of beta glucuronidase from the white cells of patients with drug rashes when incubated in autologous plasma, with and without the addition of the causal drug.

In seven out of 16 patients with drug rashes, the leucocytes selectively released beta glucuronidase when incubated in autologous plasma, indicating the possible presence of immune complexes. When the white cells were incubated with the suspected drug in vitro, they tended to react in three different ways. In four out of 16 cases additional beta glucuronidase was released, perhaps due to the formation of immune complexes, in two out of the 16, beta glucuronidase release was suppressed, perhaps due to antigen excess, and in two cases LDH release was decreased while beta glucuronidase remained unaltered.

Blood↗
PubMed1986

Human biliary beta-glucuronidase: correlation of its activity with deconjugation of bilirubin in the bile.

Total and conjugated bilirubin contents of gall-bladder and hepatic biles before and after 24-h incubation at 37 degrees C and beta-glucuronidase activity of hepatic biles were determined in forty-eight patients divided equally into four groups: no stones or control (C), cholesterol stones (CS), black pigment stones (black PS), and brown pigment stones (brown PS). The percent conjugation of bilirubin is lower in gall-bladder biles and hepatic biles after incubation, particularly in black PS and brown PS, when compared with hepatic biles before incubation. Mean endogenous beta-glucuronidase activities at pH 5.2 were 12.0, 15.5, 44.5 and 147.7 nmol min-1 ml-1 for C, CS, black PS, and Brown PS, respectively, which correlated well with the degree of deconjugation of bilirubin in gall-bladder and hepatic biles and with the rate of deconjugation of hepatic bile incubated at 37 degrees C. Only four biles in brown PS exhibited bacterial enzyme activity. We concluded that though bacterial beta-glucuronidase might be responsible for deconjugation of bilirubin in some patients in brown PS, endogenous biliary beta-glucuronidase could play a key role in the pathogenesis of pigment cholelithiasis.

Adult↗
PubMedDate not supplied

The effects of acrylamide on beta-glucuronidase and acid phosphatase activities in rat sciatic nerve above and below a ligature.

The enzymes beta-glucuronidase and acid phosphatase have been assayed by histochemical and by fluorimetric methods above and below a tightly tied ligature on the rat sciatic nerve over the subsequent 10 days. These findings have been compared with similarly treated animals also given four daily doses of acrylamide (50 mg/kg). The following have been found: 1 during this time, acrylamide at this dose causes slight increases in beta-glucuronidase in untied sciatic nerves, detectable both histochemically and fluorimetrically; 2 below the ligature both enzyme activities were greatly increased and this was slightly reduced in the acrylamide-dosed animals; 3 there was a mild rise in beta-glucuronidase activity in the 1.0 cm above the ligature in undosed animals demonstrable both histochemically and fluorimetrically; 4 that in the acrylamide-dosed animals there was a marked rise in beta-glucuronidase activity both 1.0 cm and 2.0 cm above the ligature which was intensified at 7 days and at 10 days after dosing. This was demonstrated both histochemically and fluorimetrically. These results are discussed in the light of the known sheath cell and axonal responses to acrylamide intoxication.

Acid Phosphatase↗
PubMed1996

Exercise-induced changes in the activities of beta-glucuronidase and N-acetyl-beta-D-glucosaminidase in plasma and muscle of standardbred trotters.

The activities of lysosomal enzymes, such as beta-glucuronidase and N-acetyl-beta-D-glucosaminidase, have been shown to increase in muscle after endurance exercise. We examined whether measurable activities of lysosomal enzymes are present in equine plasma and whether the exercise-induced changes in the muscle are reflected in plasma. Six trained Standardbred trotters performed three exercise bouts with 1 h intervals and the same procedure was repeated 3 days later. Venous blood samples and muscle biopsies from the middle gluteal muscle were taken before and after exercise. The activities of beta-glucuronidase and N-acetyl-beta-D-glucosaminidase were measured both from plasma and muscle specimens. Cell infiltration into the muscle after exercise was evaluated by the DNA content and histochemically by haematoxylin stain. The activity of N-acetyl-beta-D-glucosaminidase in plasma was increased immediately after exercise, but had returned to the basal level at 4 h. N-acetyl-beta-D-glucosaminidase in muscle and beta-glucuronidase in muscle and plasma increased 2 days after exercise and returned to the basal level on day 3. A similar pattern was seen when the exercise protocol was repeated 3 days later, except that the activities continued to increase during the 3 days after exercise. The DNA content in muscle correlated with beta-glucuronidase in muscle and plasma and with the N-acetyl-beta-D-glucosaminidase in muscle indicating that the activities reflect the infiltration of phagocytes into the exercise-injured muscle. It can be concluded that the activities of the lysosomal enzymes in plasma increase after exercise and that the changes are mainly due to a simultaneous increase in the number of neutrophils. Therefore, plasma activities of the lysosomal enzymes are poor indicators of exercise-induced muscle damage.

Acetylglucosaminidase↗
PubMed1979

A regulatory locus for mouse beta-glucuronidase induction, Gur, controls messenger RNA activity.

A regulatory locus in a higher organism has been shown to control a specific messenger RNA activity. The Gur locus in mice regulates the production of kidney beta-glucuronidase messenger RNA activity after induction of the beta-glucuronidase structural gene, Gus, by testosterone. beta-Glucuronidase messenger RNA was assayed by its ability to direct the synthesis of catalytically active murine beta-glucuronidase in Xenopus oocytes.

Animals↗
PubMed1985

beta-Glucuronidase activities of intestinal bacteria determined both in vitro and in vivo in gnotobiotic rats.

The beta-glucuronidase activities of bacterial strains isolated from the rat intestinal tract were studied both in vitro in culture media and in vivo in the intestinal contents of gnotobiotic rats. Only 50 of 407 strains tested were found to be positive in vitro. They belonged to the three genera Clostridium, Peptostreptococcus, and Staphylococcus. The in vitro-negative strains were also negative in vivo. The beta-glucuronidase activities of the beta-glucuronidase activities of the positive strains were generally greater in vivo than in vitro. The highest in vivo activities were found in the intact bacterial cells and in the soluble fractions prepared from disrupted pellets. There was a discrepancy between the activities obtained from both conventional and gnotobiotic rats harboring selected positive strains, suggesting that the main beta-glucuronidase-positive strains have not yet been isolated from the intestines of conventional rats.

Animals↗
PubMed1987

Coagglutination and enzyme capture tests for detection of Escherichia coli beta-galactosidase, beta-glucuronidase, and glutamate decarboxylase.

Polyclonal antibodies to Escherichia coli beta-galactosidase, beta-glucuronidase, and glutamate decarboxylase were used in coagglutination tests for identification of these three enzymes in cell lysates. Enzyme capture assays were also developed for the detection of E. coli beta-galactosidase and beta-glucuronidase. The enzymes were released by using a gentle lysis procedure that did not interfere with antibody-enzyme interactions. All three enzymes were detected in 93% (51 of 55) of the E. coli strains tested by coagglutination; two of the three enzymes were identified in the remaining 7%. Of 42 non-E. coli tested by coagglutination, only four nonspecifically agglutinated either two or three of the anti-enzyme conjugates. Thirty-two (76%) non-E. coli isolates were negative by coagglutination for all three enzymes. The enzyme capture assay detected the presence of beta-galactosidase in seven of eight and beta-glucuronidase in all eight strains of E. coli tested. Some strains of beta-galactosidase-positive Citrobacter freundii and Enterobacter cloacae were also positive by the enzyme capture assay, indicating that the antibodies were not entirely specific for E. coli beta-galactosidase; however, five other gas-positive non-E. coli isolates were negative by the enzyme capture assay. The coagglutination tests and enzyme capture assays were rapid and sensitive methods for the detection of E. coli beta-galactosidase, beta-glucuronidase, and glutamate decarboxylase.

Agglutination Tests↗