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)

A study on the beta-glucuronidase activity in liver and spleen homogenates of mice infected with an Egyptian strain of Schistosoma mansoni and of non infected control animals was carried out for a follow up period of four months. A decreased enzyme activity was observed in the spleen up to the 40th day after infection. From the 60th day on, the enzyme level in both liver and spleen was found above that in the control. The possible causes for such changes in enzyme activity are discussed.
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PMID:beta-Glucuronidase activity in liver and spleen homogenates of mice experimentally infected with Schistosoma mansoni. 58 Nov 36

Triggering of eosinophil secretory and cytotoxic functions by stimulation of the IgG and IgE FcR is thought to have major importance in the pathophysiology of tissue eosinophilia. We studied the ability of human rIL-4 to regulate this triggering event in human eosinophils. At doses ranging from 0.1 to 10 pg/ml, IL-4 suppressed eosinophil secretion of beta-glucuronidase and arylsulfatase by up to 65% after stimulation with IgG-coated Sepharose beads. This effect required prolonged preincubation (16 h) of eosinophils with IL-4; no effect was detected after 1 h preincubation. Enzyme secretion stimulated by IgE-coated beads was not affected. Further, IL-4 (after 16 h preincubation), suppressed eosinophil antibody-dependent killing of schistosomula (Schistosoma mansoni) targets by 24 to 39% in four experiments (p less than 0.05). Flow microfluorimetry analysis showed that IL-4 reduced the expression of IgG FcR, but not IgE FcR, suggesting that this mechanism underlies the suppression of IgG-mediated secretion. Taken collectively, these results demonstrate a mechanism for T lymphocyte suppression of IgG-stimulated eosinophil functions via IL-4.
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PMID:Inhibition of IgG-triggered human eosinophil function by IL-4. 213 96

We have shown that IgG hydrolysed by Schistosoma mansoni schistosomula inhibited various macrophage functions, especially phagocytosis and anti-schistosome cytotoxicity. Here we show that a tripeptide, Thr289-Lys-Pro291, of the second constant domain of human immunoglobulin G (peptide 286-292) reproduced the inhibitory effect of a total hydrolysate. Indeed the beta-glucuronidase release from IgE-anti-IgE-stimulated rat and human macrophages decreased and its intracellular level did not rise after a prior incubation of the cells with Thr-Lys-Pro (500 nmol/ml). Moreover, the cell migration as well as the superoxide anion O2 generation were 50-80% reduced by the tripeptide. These results suggest that a single peptide set may be responsible for the decrease of the macrophage functions at the early stage of the parasite infection in the mammalian host. The pharmacologic properties of this tripeptide are under investigation.
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PMID:Characterization and synthesis of a macrophage inhibitory peptide from the second constant domain of human immunoglobulin G. 629 3

The in-vivo effect of the schistosomicidal drugs praziquantel and oltipraz on the activities of the liver lysosomal enzymes in Schistosoma mansoni-infected and non-infected mice was studied. The effect of S. mansoni infection and the administration of the schistosomicidal drugs on the activities of beta-glucuronidase, acid ribonuclease and alpha-naphthyl acetate esterases may be considered as indices for carcinogenicity. Drugs were given orally in subcurative doses, either in a single dose of 400 mg kg-1 for praziquantel or in five daily doses of 50 mg kg-1 oltipraz. The increase in enzymatic activities in infected animals was attributed to deranged metabolic function as a result of liver cell injury. Treatment of uninfected animals with either praziquantel or oltipraz significantly increased the activities of the three lysosomal enzymes. Praziquantel possesses reversible and less toxic effects on the liver than oltipraz. The role of these antischistosomal drugs cannot be ignored as a possible aetiological factor implicated in the process of carcinogenesis associated with schistosomiasis infection through modulation of the operating potential of the enzymes concerned with detoxification, protein and fat metabolism.
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PMID:An experimental study on the effect of praziquantel and oltipraz on some lysosomal enzymes. 842 71

We isolated a cDNA encoding a novel glucuronyltransferase from human placenta cDNA with the use of the degenerate reverse transcriptase-polymerase chain reaction method. Degenerate primers were designed based upon the amino acid sequence alignment of rat glucuronyltransferase (GlcAT-P) involved in the biosynthesis of the carbohydrate epitope HNK-1 with putative proteins in Caenorhabditis elegans and Schistosoma mansoni. The new cDNA sequence revealed an open reading frame coding for a protein of 335 amino acids with a type II transmembrane protein topology. The amino acid sequence displayed 43% identity to the rat GlcAT-P, and the highest sequence identity was found in the COOH-terminal catalytic domain. The expression of a soluble recombinant form of the protein in COS-1 cells produced an active glucuronyltransferase with marked specificity for a glycoserine Galbeta1-3Galbeta1-4Xylbeta1-O-Ser. In contrast, asialoorosomucoid, which contains the Galbeta1-4GlcNAc sequence and is a good acceptor substrate for the GlcAT-P, did not serve as an acceptor. The reaction product was sensitive to beta-glucuronidase digestion and co-chromatographed with authentic GlcAbeta1-3Galbeta1-3Galbeta1-4Xylbeta1-O-Ser in high-performance liquid chromatography, suggesting that the enzyme is a beta1, 3-glucuronyltransferase. These results indicate that this new member of the glucuronyltransferase gene family is the enzyme previously described as glucuronyltransferase I that forms the glycosaminoglycan-protein linkage region, GlcAbeta1-3Galbeta1-3Galbeta1-4Xylbeta1-O-Ser, of proteoglycans.
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PMID:Molecular cloning and expression of glucuronyltransferase I involved in the biosynthesis of the glycosaminoglycan-protein linkage region of proteoglycans. 950 57