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)

1. Polysaccharide in a heparin-producing mouse mastocytoma was pulse-labelled in vivo with [35S] sulphate, and after various periods of time was isolated from subcellular fractions. Such fractions were recovered from tissue homogenates by consecutive centrifugations at 1000g for 10min, 20000g for 20min and 100000g for 1h. Initially the 35S-labelled polysaccharide formed occurred principally in the second centrifugal fraction (20000g precipitate), with small amounts in the first (granular) and third (microsomal) fractions. Analysis for glycosyltransferase activity confirmed that glycosaminoglycans were formed chiefly in particles sedimenting at 20000g. Molecules of this newly synthesized polysaccharide were considerably larger than those of commercially available heparin, as judged from gel chromatography. 2. Within the first hour after injection of [35S]sulphate, most of the labelled polysaccharide was redistributed from the second to the first centrifugal fraction. During, and possibly also after, this shift, the macromolecular polysaccharide was degraded, ultimately to the size of commercial heparin. The degradation process appeared complete 6h after injection of [35S]sulphate. 3. Particulate subcellular fractions were incubated with macromolecular [35S]heparin and the products were analysed by gel chromatography. Significant degradation of the substrate occurred only with the second centrifugal fraction. Further characterization of this fraction, by density-gradient centrifugation in iso-osmotic colloidal silica, revealed a single visible band of particles, at approximately the same density at lysosomes. This band contained all the beta-glucuronidase, 35S-labelled endogenous polysacchride and heparin-degrading enzyme present in the second fraction.
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PMID:Metabolism of macromolecular heparin in mouse neoplastic mast cells. 82 71

It was reported that neurotropin (NSP), an extract isolated from the inflamed skins of rabbits inoculated with vaccinia virus, activates murine T cell functions participating in cell-mediated immunity. The present study was undertaken to examine the effect of NSP on plastic dish-adherent macrophages (M phi) from ddY mice in vitro. Total activities of beta-glucuronidase and N-acetyl-beta-D-glucosaminidase in resident peritoneal M phi was slightly enhanced when the M phi were cultured with NSP (10-1000 micrograms/ml) for 48 and 96 hr, but no enhancement was noted in 24 hr culture. Intracellular activity of lactate dehydrogenase (LDH) was also strongly enhanced in a dose-dependent manner by culturing with NSP for 48 and 96 hr. The enhanced LDH activity in the M phi cultured with NSP for 96 hr was completely inhibited by cycloheximide, an inhibitor of protein synthesis. In addition, consumption of glucose in the culture media by the M phi was also enhanced by culturing with NSP for 96 hr. Intracellular activity of LDH and glucose consumption of plastic dish-nonadherent cells from normal mouse peritoneal cells, however, was not enhanced by NSP in 96 hr culture. In regard to allogeneic M phi-mediated cytostatic activity to P815-X2 mastocytoma, NSP had no effect on cytostatic activities of the resident and thioglycollate-induced M phi, although NSP by itself dose-dependently inhibited the growth of P815-X2 mastocytoma without affecting cell viability. These results suggest that NSP biochemically activates mouse peritoneal M phi in vitro, but the M phi activated by NSP can not inhibit the growth of P815-X2 mastocytoma.
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PMID:[Immunopharmacological actions of neurotropin (4). Effect of neurotropin on mouse peritoneal macrophages]. 644 Aug 35

The lipoxygenation of arachidonic acid in basophils, mastocytoma cells, and other leukocytes generates the unstable intermediate 5-hydroperoxy-eicostaetraenoic acid, which is converted in part to a series of complex hydroxy-eicosatetraenoic acids (HETEs) with additional polar substituents and 3 conjugated double bonds. One of the products, 5,12-di-HETE, is chemotactic for human neutrophils in vitro at a concentration as low as 3 ng/ml and evokes a maximal neutrophil chemotactic response at 30 ng/ml, as compared to 1000 ng/ml for 5-HETE and 10,000 to 20,000 ng/ml for 11-HETE and 12-HETE. In contrast, other products in the same series, such as the slow reacting substance 5-hydroxy-6-glutathionyl-eicosatetraenoic acid (leukotriene C), and the platelet-derived 8,9,12-trihydroxy-eicosatrienoic acid and 8,11,12-trihydroxy-eicosatrienoic acid exhibited only marginal neutrophil chemotactic activity. Only 5,12-di-HETE released significant quantities of beta-glucuronidase and lysozyme from the neutrophils, but the maximal level of enzyme release was far less than that for the chemotactic fragment of C5 and the formyl-methionyl peptides.
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PMID:The human PMN leukocyte chemotactic activity of complex hydroxy-eicosatetraenoic acids (HETEs). 741 Aug 54