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)

Three urinary lysosomal enzymes, beta-glucuronidase (beta-Gluc), beta-galactosidase (beta-Gal) and N-acetyl-beta-D-glucosaminidase (NAG), were measured in twenty-one renal allograft recipients to evaluate their role in the diagnosis and prediction of rejection episodes, and in the prediction of eventual graft outcome. A fluorometric assay using methylumbelliferone substrates was used to measure the three enzymes in morning urine samples and enzyme activity was defined in terms of urine creatinine concentration. Urinary NAG levels increased significantly in 13/16 first rejection episodes and 4/4 instances of acute tubular necrosis and graft infarction. In 5 of the 16 first rejection episodes the NAG was predictive of the rejection. NAG was not useful in diagnosing second or subsequent rejections and beta-Gluc and beta-Gal were of little value in assessing any component of renal transplant pathology. As a prognostic index of eventual graft outcome, the peak urinary NAG was particularly encouraging. It correlated strongly with deterioration in graft function as time passed such that only 2/10 patients with peak NAG greater than 1400 Units had normal serum creatinines at 6 months post transplantation. Conversely 4/4 patients with peak NAG levels less than 700 Units had normal serum creatinine at that time. In our series the measurement of urinary NAG was a useful adjunct to the diagnosis of first rejections but appears to be more valuable in predicting graft outcome.
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PMID:Urinary lysosomal enzyme excretion after renal allotransplantation. 10 10

The LAC4 gene encoding the beta-galactosidase (beta Gal) of the yeast, Kluyveromyces lactis, was cloned on a 7.2-kb fragment by complementation of a lacZ-deficient Escherichia coli strain. The nucleotide sequence of the structural gene, with 42 bp and 583 bp of the 5'- and 3'-flanking sequences, respectively, was determined. The deduced amino acid (aa) sequence of the K. lactis beta Gal predicts a 1025-aa polypeptide with a calculated M(r) of 117618 and reveals extended sequence homologies with all the published prokaryotic beta Gal sequences. This suggests that the eukaryotic beta Gal is closely related, evolutionarily and structurally, to the prokaryotic beta Gal's. In addition, sequence similarities were observed between the highly conserved N-terminal two-thirds of the beta Gal and the entire length of the beta-glucuronidase (beta Glu) polypeptides, which suggests that beta Glu is clearly related, structurally and evolutionarily, to the N-terminal two-thirds of the beta Gal. The structural analysis of the beta Gal alignment, performed by mean secondary structure prediction, revealed that most of the invariant residues are located in turn or loop structures. The location of the invariant residues is discussed with respect to their accessibility and their possible involvement in the catalytic process.
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PMID:Sequence of the Kluyveromyces lactis beta-galactosidase: comparison with prokaryotic enzymes and secondary structure analysis. 151 85

We are attempting to develop methods for the sequencing of glycosaminoglycans from their reducing end. Here we describe a procedure for the analysis of dermatan sulphate from pig skin. The glycosaminoglycan is released from its parent proteoglycan by exhaustive proteolysis by using both endo- and exo-peptidases. The amino group of the residual serine residue is conjugated with a p-hydroxyphenyl group, which in turn is iodinated with 125I (the Bolton-Hunter reagent, BHR). The ion-exchange-purified end-labelled dermatan sulphate is then degraded partially or completely by various enzymic or chemical means to yield fragments extending from the labelled serine residue to the point of cleavage. The various products are separated by gradient PAGE, detected by autoradiography and quantified by videodensitometry. Complete digestion with chondroitin ABC lyase affords the labelled fragment delta HexA-GalNAc(-SO4)-GlcA-Gal-Gal-Xyl-Ser(-BHR). The structure was confirmed by sequential degradation from the non-reducing end by chondroitin AC lyase, HgCl2, and beta-galactosidase. Periodate oxidation cleaves most of the Xyl even without treatment with alkaline phosphatase, showing that Xyl is not substituted with phosphate. Results from partial and selective periodate oxidation indicate that most of the non-sulphated IdoA residues are located towards the non-reducing end. Partial or complete digestions with testicular hyaluronidase (in the presence of an excess of beta-glucuronidase) or chondroitin AC lyase identify the positions of GlcA residues. The results confirm that HexA next to Gal is always GlcA. Moreover, GlcA is common in the first three disaccharide repeats. Results with testicular hyaluronidase indicate that the distribution of clustered GlcA-GalNAc repeats is periodic and peaks at positions 1-3, 8-9 and around 25. Although there must be chains that contain IdoA in nearly all of the available positions, regions that have not been fully processed during biosynthesis are markedly non-random.
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PMID:A method for the sequence analysis of dermatan sulphate. 216 67

The two major components of the acidic glycolipid fraction from the pupae of Calliphora vicina were isolated using high-performance liquid chromatography. The acidic moiety was identified as glucuronic acid by beta-glucuronidase cleavage and gas chromatographic analysis as the pentafluoropropionyl derivative. The structures of the carbohydrate moiety were elucidated by peracetylation, methylation, exoglycosidase cleavage, fast-atom-bombardment mass spectrometric and 1H-nuclear magnetic resonance spectroscopic analysis. The only difference between the two hexasaccharide variants was the presence, in one of them, of a between the two hexasaccharide variants was the presence, in one of them, of a phosphoethanolamine (AeP) sidechain on the third sugar of the sequence, i.e. N-acetylglucosamine. The composition of the ceramide moiety was dominated by a C20:0 fatty acid (arachidic acid) and a C14:1 sphingoid base (tetradecasphing-4-enine). The chemical structures of the two insect acidic glycosphingolipids were determined to be: GlcA(beta 1-3)Gal-(beta 1-3)GalNAc(beta 1-4)GlcNAc(beta 1-3)Man (beta 1-4)Glc(beta 1-1)Cer; GlcA(beta 1-3)Gal(beta 1-3)GalNAc(beta 1-4)[2AeP-6]-GlcNAc(beta 1-3) Man(beta 1-4)Glc(beta 1-1)Cer. Such glucuronic-acid-containing insect glycosphingolipids have been given the generic name arthrosides, with the implied synonymity to the gangliosides.
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PMID:Glycosphingolipids in insects. Chemical structures of two variants of a glucuronic-acid-containing ceramide hexasaccharide from a pupae of Calliphora vicina (Insecta: Diptera), distinguished by a N-acetylglucosamine-bound phosphoethanolamine sidechain. 238 87

To elucidate the function of the reticuloendothelial system of liver in hepatic injury, we investigated the effect of endotoxins on superoxide anion (O-2) generating capacity and lysosomal enzyme activities of Kupffer cells isolated from rats treated with galactosamine (Gal N), with Gal N supplemented with polymyxin B (Polymyxin B-Gal N), with lipopolysaccharide (LPS) and from control rats. After collagenase digestion of the liver and centrifugation over metrizamide gradient, Kupffer cells were prepared by the dish adherence procedure. O-2 production by the cells was examined as chemiluminescence during phagocytosis of latex particles and beta-glucuronidase activities were analyzed. High titers of endotoxemia were detected in LPS and Gal N rats by limulus test, while a low endotoxemia titer was found in Polymyxin B-Gal N rats. Hepatocyte damage was found in Gal N rats, but little was recognized in LPS and Polymyxin B-Gal N rats. In the latter groups, Kupffer cells, activated by endotoxins, showed the enhancement of chemiluminescence and a release of lysosomal enzyme. Though lysosomal enzyme was released from Kupffer cells in Gal N rats, chemiluminescence was slightly suppressed in spite of the high titer of endotoxemia. These results appear to be related to the consumption of O-2 during liver injury. The functional state of Kupffer cells was thus changed by the grade of endotoxemia and hepatic injury.
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PMID:Superoxide anion generating capacity and lysosomal enzyme activities of Kupffer cells in galactosamine induced hepatitis. 301 77

Activity changes of thiamine pyrophosphatase (TPPase), acid phosphatase (aP), non-specific esterase (nE), acid beta-galactosidase (a beta Gal), beta-glucuronidase (beta-Gluc), and beta-D-N-acetylglucosaminidase (NAG) in follicles during atresia were investigated in the ovaries of mice, rats, Mongolian gerbils, hamsters, guines pigs, rabbits, cats, and pigs. Changes of hydrolase activity were highly enzyme dependent, species-specific and mostly confined to the granulosa. Decrease of TPPase activity and increase of lysosomal enzyme activities during atresia appeared to be true for all mammals. The start of activity changes in the time course of atresia depended on the occurrence of the enzyme in the growing granulosa. Continuous increase of lysosomal enzyme activity appeared in follicles where these enzymes could also be found in the growing granulosa. In contrast, when lysosomal enzyme activity was low or could not be detected in the growing granulosa, increased enzyme activity could only be observed at a time when degenerative processes have already progressed considerably. This distribution pattern suggests that hydrolytic enzymes in the granulosa cells as well as hydrolases of invading macrophages participate in this degenerative process. In some mammals, enzyme activity changes appeared in the cumulus oophorus for the first time in advanced stages of degeneration. In some mammals enzyme activity changes were dependent on the developmental stage of the follicle. This stage dependency argues for an interrelationship between activation of lysosomal enzymes and androgen metabolism.
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PMID:Hydrolase cytochemistry during follicular atresia in mammals. 313 20

An i.p. injection of benzo(a)pyrene (BP; 10 mg/kg) into rats led to the progressive release of hepatic, beta-glucuronidase (beta-Gluc), beta-galactosidase (beta-Gal) and beta-N-acetylglucosaminidase (beta-Glm). This occurred prior to the appearance of altered cells or cell populations from which malignant transformations may gradually develop. The in vitro studies on the latency of beta-Gluc, Beta-Gal and beta-Glm in the lysosome-enriched rat liver suspension treated with BP showed that concentrations of 10(-7) M, 10(-6) M and 10(-5) M significantly decrease latency of all three lysosomal enzymes, the effect being time-dependent. These concentrations of BP did not alter the activities of beta-Gluc, b-Gal and beta-Glm in vitro. No significant alterations were observed in total enzyme activities, following in vivo and in vitro BP administration. BP exerts its effect on rat liver lysosomes by modifying the structural properties of the lysolemma, and may represent an early precarcinogenic change.
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PMID:The effects of benzo(a)pyrene on rat liver lysosomes. 680 1

Isozyme patterns for five acid hydrolases, acid phosphatase (AP), aryl-sulfate (AS), beta-glucuronidase (beta-Glu), N-acetylglucosaminidase (NAG) and beta-galactosidase (beta-Gal), were studied in isolated lysosomes from ethylnitrosourea (ENU)-induced gliomas and compared with normal and newborn rat brains. With polyacrylamide gel electrophoresis (PAGE), AP was separated into three bands, acidic (A), intermediate (B) and basic (C). In tumors and newborn brains there was a decrease in A and C but a significant increase in B. For NAG the acidic form was elevated by 9-19% in tumors, while newborn brains showed a 19% decrease. Even though the band intensities of beta-Glu in tumors and newborn brains were increased, the relative distribution remained similar to normal brain. With isoelectric focusing, five hydrolases were separated into four to five distinct forms. In ENU-induced gliomas the intensities of all peaks were considerably increased, but in most cases the number of isozymes remained the same. In tumors the isoelectric points were shifted towards the acidic side and smaller peaks in the basic regions merged into more acidic peaks. This effect was especially evident for AP and Gal. In the cases of AS, beta-Glu and NAG, consistently more activity was associated with acidic peaks than with the basic ones. Our data indicates that there is a significant increase in acidic forms of some of the lysosomal hydrolases studied in ENU-induced brain tumors.
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PMID:Lysosomal isozyme patterns in ethylnitrosourea-induced brain tumors. 681 Dec 78

125I-Labeled L-fucose-albumin complex and rat preputial beta-glucuronidase are rapidly cleared from plasma after intravenous infusion. L-Fucose-albumin retards the plasma clearance of beta-glucuronidase whereas D-fucose-albumin is inactive. In vitro, 125I-labeled L-fucose-albumin is taken up into rat or rabbit alveolar macrophages by receptor-mediated pinocytosis. Uptake (37 degrees C) is time-dependent, is saturable with increasing ligand concentration (Kuptake = 4.4 X 10(-8) M), and requires Ca2+. 125I-labeled D-fucose-albumin is poorly taken up. Binding (4 degrees C) is saturable and Ca2+ dependent. Binding and uptake are fully inhibited by yeast mannan. A series of neoglycoproteins, including L-fucose-albumin, were tested as inhibitors of uptake of 125I-labeled beta-glucuronidase into macrophages. The following order of potency was observed: L-Fuc = D-Man greater than GlcNAc approximately D-Glc greater than D-Xyl much greater than than D-Gal = L-Ara = D-Fuc. L-Fucose-terminated oligosaccharides coupled to bovine serum albumin also block 125I-labeled beta-glucuronidase uptake into macrophages.
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PMID:L-Fucose-terminated glycoconjugates are recognized by pinocytosis receptors on macrophages. 694 Jan 20

The nucleotide (nt) sequence of a 2.57-kb Sau3A fragment carrying the Rhizobium meliloti beta-galactosidase (beta Gal)-encoding gene (RmlacZ) was determined. An open reading frame (ORF) of 2.26 kb was identified which encoded a 755-amino-acid (aa) polypeptide with a calculated molecular mass of 84,141 Da, in fair agreement with the value of 88 kDa determined by SDS-PAGE. The deduced N-terminal aa sequence was confirmed by direct sequencing of electrophoretically purified R. meliloti beta Gal. The size of the native R. meliloti beta Gal was approx. 174 kDa. Similarities were found between the aa sequence of the R. meliloti beta Gal and those from Clostridium thermosulfurogenes EM1 and Agrobacterium radiobacter, as well as human beta-glucuronidase (beta Glu). Comparisons with beta Gal from Escherichia coli, Klebsiella pneumoniae, Lactobacillus bulgaricus and Kluyveromyces lactis found only weak similarities; however, the putative active site residues appear to be conserved. The RmlacZ sequence is flanked by two partially sequenced ORFs, which show aa sequence and organisational similarities to the previously reported lac operon in A. radiobacter.
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PMID:Nucleotide and deduced amino acid sequences of Rhizobium meliloti 102F34 lacZ gene: comparison with prokaryotic beta-galactosidases and human beta-glucuronidase. 816 82


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