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)

The effect of various metals on uridine diphosphate (UDP)-glucuronyltransferase and beta-glucuronidase activities in rat liver microsomes was investigated. The presence of Mn2+, Cd2+, Zn2+, V5+, Ni2+, Co2+, Cu+ or Ca2+ (20 microM) in the enzyme reaction mixture did not cause a significant alteration of UDP-glucuronyltransferase activity in hepatic microsomes. Of these metals, Zn2+ and Cd2+ (20 microM) caused a remarkable increase in hepatic microsomal beta-glucuronidase activity. Appreciable effects of Zn2+ and Cd2+ on beta-glucuronidase activity were seen at 5.0 microM, and the effects were saturated at 50 microM. Ca2+ (5.0-50 microM) and/or the Ca2(+)-binding protein regucalcin (2.0 microM) did not have an appreciable effect on UDP-glucuronyltransferase and beta-glucuronidase activities in hepatic microsomes. Thus, Zn2+ and Cd2+ uniquely increased beta-glucuronidase activity. The Zn2(+)- and Cd2(+)-induced increase in beta-glucuronidase activity was completely reversed by the presence of an SH group-protecting reagent (dithiothreitol). The response of the microsomal enzyme to Zn2+ and Cd2+ (20 microM) was no longer seen after treatment with 0.2% Triton X-100 [polyoxyethylene(10)octylphenyl ether], indicating that the stimulation by these metals is dependent on membrane association. The present study suggests that, of various metals tested, Zn2+ and Cd2+ can uniquely increase hepatic microsomal beta-glucuronidase activity and that their effect is based on binding to membranous SH groups, beside the enzyme protein.
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PMID:Effects of Ca2+, Zn2+ and Cd2+ on uridine diphosphate-glucuronyltransferase and beta-glucuronidase activities in rat liver microsomes. 211 Aug 67

Human lymphocytes were isolated from defibrinated blood by Ficoll-Hypaque centrifugation with erythrocyte hypotonic lysis. Homogenates of mixed lymphocytes were subjected to analytical subcellular fractionation by sucrose gradient centrifugation in a Beaufay automatic zonal rotor. The principal organelles were characterized by their marker enzymes: cytosol (lactate dehydrogenase), plasma membrane (5'-nucleotidase), endoplasmic reticulum (neutral alpha-glucosidase), mitochondria (malate dehydrogenase), lysosomes (N-acetyl-beta-glucosaminidase), peroxisomes (catalase). gamma-Glutamyl transferase was exclusively localized to the plasma membrane. Leucine amino-peptidase, especially when assayed in the presence of Co2+, was also partially localized to the plasma membrane. Experiments with diazotized sulphanilic acid, a non-permeant enzyme inhibitor, showed that these plasma membrane enzymes are present on the cell surface. No detectable alkaline phosphatase was found in the lymphocytes. Acid phosphatase and beta-glucuronidase were localized to lysosomes and there was some evidence for lysosomal heterogeneity. Leucine amino peptidase, optimal at pH 8.0, showed a partial localization to intracellular vesicles, possibly lysosomes, especially when assayed in the presence of EDTA. These studies provide a technique for determining the intracellular distribution of hitherto unassigned lymphocyte constituents and serve as a basis for investigating the cell pathology of lymphocytic disorders.
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PMID:Enzyme analysis and subcellular fractionation of human peripheral blood lymphocytes with special reference to the localization of putative plasma membrane enzymes. 614 55

The morphological changes on lungs of thorax irradiated mice, receiving a single dose of fast neutron and 60 cobalt radiation were investigated. Lungs were studied by histological and histochemical methods 2 weeks up to 10 months. Harvest changes were found after a time of 4-8 weeks. With histochemical methods more detailed damages are seen in contrast to routine histology. Two weeks post irradiation disturbances of phospholipid synthesis in alveolar epithelium cells of type II (AEC II) are found. Impairment of capillary endothelial cells are indicated by decreased activity of adenosine triphosphatase. Increased activity of beta-glucuronidase is seen in damaged bronchial epithelium.
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PMID:[Light microscopic and histochemical findings on the mouse lung after neutron and 60 cobalt gamma-irradiation]. 689 42

The host inflammatory response to particulate wear debris has been implicated as a principal cause of osteolysis and aseptic loosening following total joint arthroplasty. While it has long been assumed that this inflammatory response is mediated solely by a chronic process, there has been evidence to suggest that an acute response to particulate debris may be important in initiating the chronic response. We studied the in vitro and in vivo acute inflammatory responses mediated by polymorphonuclear leukocytes (PMNs) to both retrieved particulate from a catastrophically failed uncemented metal-backed acetabular component and to commercially pure particulate (polyethylene, cobalt-chrome, and titanium). Isolated, nonactivated human PMNs in vitro exhibited both a dose- and time-dependent degranulation response to opsonized particulate debris, as evidenced by release of both specific (increased lysozyme activity) and azurophilic (increased beta-glucuronidase activity) granule contents. In the rat subcutaneous pouch model in vivo, PMNs were recruited within 3-6 h after exposure to particulate debris and were noted to phagocytize particulate and subsequently degranulate, as evidenced by increased beta-glucuronidase and PMN-specific myeloperoxidase (azurophilic granule enzymes) activities. This response peaked within the first 6 h and gradually declined by 24 h. The results of this study demonstrate the presence of an acute inflammatory response mediated by PMNs both in vitro and in vivo to particulate debris, which may be important in the sequence of events that lead to the macrophage-dominated chronic inflammatory process culminating in osteolysis and aseptic loosening of total joint arthroplasties.
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PMID:In vitro and in vivo activation of polymorphonuclear leukocytes in response to particulate debris. 1055 58

Ultrastructural cytochemical tests for several enzymes, proteins, carbohydrates, and nucleic acids were conducted on secretory granules o pound dorsal and subventral esophageal glands of preparasitic second-stage juveniles and the dorsal gland of adult females of Meloidogyne incognita. Secretory granules in the subventral glands of juveniles stained positive for acid phosphatase. Peroxidase, DNase, RNase, cellulase, and nucleic acids were not detected in these granules. Secretory granules in the dorsal gland of adult females stained positive for peroxidase (pH 7.6) in < 50% of the tests, Acid phosphatase, beta-glucuronidase, DNase, RNase, polyphenoloxidase, cellulase, and carbohydrates were not detected in dorsal gland granules in adult females. Positive staining with cobalt thiocyanate, a stain for amino groups of basic proteins, occurred in secretory granules in the dorsal gland, ribosomes, and chromatin in adult females. Ribosomes, nuclei, and secretory granules of the dorsal gland of adult females intensely stained when incubated in three reagents specific for nucleic acid.
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PMID:Ultrastructural Cytochemistry of Secretory Granules of Esophageal Glands of Meloidogyne incognita. 1929 Jan 95