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)

The mechanism of laryngotracheitis virus-induced dissolution of chick nasal turbinate cartilage was studied by lysosomal enzyme histochemistry. Five-day-old chicks were infected by intranasal instillation, and changes in lysosomal enzyme distribution were followed at daily intervals through the tissue regeneration stage, Day 28. In the mucosa the lysosomes were activated beginning on Day 1, and glycerol acid phosphatase and a diffuse form of beta-glucuronidase were released concomitant with tissue cell destruction. In the chondrocytes (where glycerol acid phosphatase was absent), beginning on Day 2, particulate (lysosomal) beta-glucuronidase decreased as diffuse beta-glucuronidase increased and extended out into the matrix. The cartilage lost its metachromatic staining properties and became soft and pliable. Regeneration of the mucosa started on Day 6 and gradual reappearance of metachromatic staining of the cartilage began on Day 8 with considerable recovery of original turbinate structure by Day 12. A lysosomal membrane labilizer, vitamin A, exacerbated the cartilage pathology, whereas a stabilizer, cortisone, retarded it.
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PMID:Virus-induced lysosomal enzyme dissolution of nasal turbinate cartilage. 19 85

"Capacitase," a product combining beta-amylase and beta-glucuronidase, was compatible with survival of bull spermatozoa frozen in whole milk-glycerol extender at final concentrations per ml of 0, 5, 10, and 20 mug of beta-amylase combined with 0, 75, 150, and 300 units of beta-glucuronidase, respectively. Bull semen was frozen in whole milk-glycerol extender containing the three lower concentrations of enzymes tested in the previous trial and used to inseminate 9057 first-service cows within 4 mo of freezing. The 60- to 90-day percent nonreturns were 74.6, 75.6, and 75.0. The same treatments plus a fourth one containing 10 mug of catalase per ml were fertility tested in another trial. Insemination of 16,842 cows resulted in 75.6, 74.1, 74.6, and 74.2% nonreturns. In this trial semen was held immersed in liquid nitrogen and distributed for immediate use each mo for 6 mo. There was no change in fertility during 6 mo of continuous storage at --196 C. Under the conditions tested neither catalase nor beta-amylase with beta-glucuronidase enhanced fertility of frozen bull semen.
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PMID:Fertility of bull semen frozen with beta-amylase, beta-glucuronidase, and catalase. 99 19

Kinetic studies of the histochemical and histoenzymatic behavior of rabbit pancreatic parenchymas were performed 5, 30 and 90 days after Wirsung duct ligation. In control pancreas, some enzyme activities (EA) were more prominent in Langerhans islets [glucose-6-phosphatase, glucose-6-phosphate dehydrogenase (DH), isocitrate DH, glycerol-3-phosphate DH, NADPH DH], others were strongly marked in acini and ducts (alkaline phosphatase, beta-glucuronidase, acid esterase aryl-sulfatase). Histochemical and enzyme abnormalities observed in experimental rabbits reflect the post-ligation degenerative and reactive processes in both exocrine and endocrine pancreas: (1) the decrease in Krebs cycle and pentose pathway linked EA and the increased lysosomal and acid phosphatase EA reflect early (day 5) degeneration and necrosis of islets and acini (day 30); (2) proliferative processes in developed ductal epithelia are shown by an increase in both glycolytic and lysosomal EA (days 30 and 90); (3) connective tissue neogenesis and interstitial fibrosis occurred as shown by activated beta-glucuronidase, aryl-sulfatase, alkaline phosphatase and increased ribonucleoproteins and glycoaminoglycans contents (day 30); (4) on day 90, the neoformed cell clusters presenting glucose-6-phosphatase positivity (B-cell marker) are seen in the pancreas remnant. At the same time, blood insulin level increases correlated with a decrease of hyperglycemia.
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PMID:Cell features in pancreas of prediabetic and diabetic rabbits after Wirsung duct ligation. Histochemical and histoenzymatic studies. 233 24

The effect of dimethylsulfoxide (DMSO) on the level of prostaglandins (PGE and PGF2 alpha), the intensity of peroxide oxidation of lipids (POL), activity of beta-glucuronidase (BGU) prior to and 5 and 24 hours after application made to the patients' hands was studied by a double blind method in 20 patients with genuine rheumatoid arthritis (RA) against the background of therapy with nonsteroid antiphlogistic preparations. Of 20 patients 10 received one-hour application of a 50 per cent DMSO gel, 10 patients received placebo (glycerol instead of DMSO). The authors revealed a significant suppression of PS production against the background of an increased level of POL in four patients who had been given DMSO. The activity of BGU increased five hours after application of DMSO and in 24 hours returned to the initial levels. Changes in the levels of inflammation mediators proved to be statistically insignificant in the group of patients given placebo. Thus, one-hour application of DMSO produced a substantial effect on the system of mediators and their interrelationship in patients with RA.
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PMID:[Effect of 1-hour administration of dimethyl sulfoxide on the levels of prostaglandins, products of lipid peroxidation and beta-glucuronidase activity in the blood of patients with rheumatoid arthritis]. 260 62

The effects of two co-carcinogenic phorbol esters (phorbol myristate acetate (PMA) and phorbol dibutyrate (PDBu] and a synthetic diacylglycerol (OAG, 1-oleoyl-2-acetyl-glycerol), which all stimulate protein kinase C, were compared with two inactive phorbol compounds (4 alpha-phorbol and 4 alpha-phorbol didecanoate (4 alpha-PDD)) on three functional properties of stimulated human polymorphonuclear leukocytes (PMNs): release of granular enzymes lysozyme and beta-glucuronidase, chemokinesis, and changes in cytoplasmic free calcium [Ca2+]i. PMA, PDBu and the diacylglycerol, OAG, all caused a dose-dependent and slow (max by 15 min) release of small amounts of lysozyme with much less beta-glucuronidase and no release of cytoplasmic lactate dehydrogenase. Release was unaffected by removal of extracellular Ca2+. PMA, PDBu and OAG inhibited random movement of the cells, did not cause chemokinesis and induced a slow reduction in the basal [Ca2+]i, as measured by the quin-2 method. PMA, PDBu and OAG increased the capacity of five independently-acting stimulants (N-formyl-Met-Leu-Phe, leukotriene B4, C5a des-Arg, platelet activating factor and A23187) to cause release of lysozyme and beta-glucuronidase but strongly inhibited PMN chemokinesis induced by the same five agents and reduced the stimulant-induced increases in [Ca2+]i. PMA was always more potent than PDBu and much more potent than OAG in eliciting these stimulatory or inhibitory effects on human PMNs. In all tests, 4 alpha-phorbol and 4 alpha-PDD were inactive. The results confirm that stimulation of the diacylglycerol/protein kinase C system in human PMN, either by active phorbol esters or the synthetic diacylglycerol, causes bidirectional effects on human PMN function. In particular, activation of the C-kinase causes inhibition of stimulated neutrophil motility, whereas the secretory functions of the cells are enhanced.
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PMID:Divergent effects of co-carcinogenic phorbol esters and a synthetic diacylglycerol on human neutrophil chemokinesis and granular enzyme secretion. 347 47

Recently, some knowledge of metabolic pathways, rather than individual enzyme activities of M. leprae, is becoming available. Ultimately this may be useful in devising culture media for M. leprae. Knowledge restricted to individual reactions may be misleading. For instance, the detection of GlcNacase and beta-glucuronidase and the subcellular localization of hyaluronic acid led to attempts to cultivate M. leprae on hyaluronic-acid based medium. Subsequent investigations suggested that there was no pathway for the breakdown of hyaluronic acid in M. leprae. The biochemical pathways for breaking down glucose and glycerol seem to be complete, and thus similar to many bacteria, but there is an unusually high level of one enzyme, 6-phosphogluconate dehydrogenase (6PGDH). Although 6-phosphogluconate is oxidized by M. leprae, and this is an unusual activity, reflecting very high levels of 6PGDH, glycerol may be a preferable energy source (on the basis of rates of oxidation by suspensions) for M. leprae in attempts to cultivate the bacterium. The utilization of 6-phosphogluconate might be important for other aspects of M. leprae metabolism not yet investigated (e.g., pentose metabolism) or it may be an adaption, not needed in vitro, to its existence in host macrophages. Alternatively, its oxidation may be a way of rapidly generating NADPH at critical times for the bacterium. Other unusual activities which have been reported are the presence of an enzyme characteristic of chemoautotrophism , completely surprising in view of the biology of M. leprae. This report needs to be confirmed--some aspects, in fact, have failed to be confirmed. o-Diphenoloxidase activity is unique, among mycobacteria, to M. leprae, but there is still doubt over whether or not it is an enzymatic activity and its function is unknown. A transpeptidase which may be involved in cell wall synthesis, recently demonstrated in M. leprae, is a typical mycobacterial enzyme. It is now known that iron could be supplied to M. leprae in potential media in the form of ferriexochelin from M. neoaurum . Two "deletions" in the metabolic processes of M. leprae have been observed. Catalase appears to be absent in M. leprae; its addition to media stimulates the growth of some organisms since peroxides form in the bacteriological media . Purine synthesis de novo occurred at a very low rate compared with purine scavenging. Whether this is an adaption to growth in vivo is not known.(ABSTRACT TRUNCATED AT 400 WORDS)
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PMID:Metabolism in Mycobacterium leprae: its relation to other research on M. leprae and to aspects of metabolism in other mycobacteria and intracellular parasites. 614 38

At 10 microM, 1-0-oleoyl-, 1-0-palmitoyl-, and 1-0-myristoyl-2-0-acetyl-glycerol weakly stimulated neutrophils to release lysozyme, an enzyme in secondary granules, but had no such effect on the release of a primary granule enzyme, beta-glucuronidase. The glycerides (1-10 microM) had a second effect on both granule populations: they enhanced the degranulating potencies of leukotriene B4, platelet-activating factor, a formylated oligopeptide, and C5a by 10- to 30-fold. In contrast, they were much less effective in enhancing responses to ionophore A23187 and partially inhibited responses to phorbol myristate acetate. The diether analogue, 1-0-hexadecyl-2-0-ethylglycerol was inactive in these regards. We suggest that diacylglycerols are a novel class of bioactive products mobilized from phosphoglycerides in stimulated neutrophils; as co-products of this mobilization, platelet-activating factor and leukotriene B4 may interact with diacylglycerols to promote cell function.
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PMID:Diacylglycerols enhance human neutrophil degranulation responses: relevancy to a multiple mediator hypothesis of cell function. 643 20

Promoter analysis was performed on the Rhizopus niveus 3-phosphoglycerate kinase 2-encoding gene (pgk2), one of the two pgk genes (pgk1 and pgk2) from this filamentous fungus sequenced so far. Deletion mutants of the promoter region were fused to the Escherichia coli uidA gene (which codes for beta-glucuronidase; GUS), and introduced into R. niveus to measure the intracellular GUS activities of the transformants. Deletion of the sequence between nt -174 to -133 (numbers indicate the position from the putative translation start codon) caused a significant decrease in the ratio of the GUS activity of the transformant cultured in glucose medium compared to that in glycerol medium. In this region, a 21-nt sequence which is well conserved between pgk1 and pgk2 is present. When it was inserted into the promoter region of the uninducible gene encoding RNase Rh of R. niveus, ligated in front of uidA and introduced into R. niveus, the GUS activity of the transformant was greatly induced by glucose, but less by glycerol. We therefore suggest that the 21-nt sequence is a glucose-inducible transcriptional activator of R. niveus. This is the first report on a transcriptional activator in zygomycetes.
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PMID:Analysis of the 3-phosphoglycerate kinase 2 promoter in Rhizopus niveus. 782 18

Two 3-phosphoglycerate kinase genes (pgk1 and pgk2) were cloned from Rhizopus niveus. It was deduced that both pgk genes have two introns. They have open reading frames of 1,355 bp and 1,356 bp, and code for proteins of 417 and 416 amino acids, respectively. The first introns of both genes are located at similar positions as those of pgk genes from other fungi based on the deduced amino-acid sequences of PGK proteins. The position of their second introns was similar to that of the seventh intron of the human pgk gene. The deduced amino-acid sequences of PGK proteins show high identity (64.8-72.2%) to those of PGKs of other filamentous fungi. When the promoters of each of the pgk genes were fused to the E. coli beta-glucuronidase (GUS) gene and introduced into R. niveus, significant GUS activities were detected in the cell lysates of the transformants, suggesting that GUS protein was expressed under the control of both pgk gene promoters in R. niveus. GUS activity was induced by glucose but not by glycerol, indicating that expression of R. niveus pgk genes was regulated by the carbon source.
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PMID:Cloning and characterization of two 3-phosphoglycerate kinase genes of Rhizopus niveus and heterologous gene expression using their promoters. 808 4

We studied the degranulation reaction of electropermeabilized human neutrophils induced by 1,2-didecanoyl-3-sn-phosphatidic acid (PA10). PA10 dose-dependently induced the release of beta-glucuronidase, an enzyme of azurophil granules, but did not induce the release of lactoferrin, a protein of specific granules. The enzyme release by PA10 absolutely required Ca2+, ATP, and Mg2+ and the concentrations for the half-maximal response were 2.5 microM, 60 microM, and 0.25 mM, respectively. Although Ca2+ alone at concentrations higher than 10 microM induced the release of both beta-glucuronidase and lactoferrin, the extents of the release were far less than that of the beta-glucuronidase release by PA10. Phorbol myristate acetate (PMA) and 1-oleoyl-2-acetyl-sn-glycerol induced the release of lactoferrin alone at concentrations of Ca2+ below 0.5 microM while they induced the release of both beta-glucuronidase and lactoferrin at higher Ca2+ concentrations, indicating that the degranulation induced by PA10 is not mediated by diacylglycerol which might be formed from PA. The degranulation reactions induced by PA10 and PMA were dose-dependently inhibited by staurosporine and calphostin C, protein kinase C inhibitors, although no direct activation of protein kinase C by PA10 was observed. The extent of the beta-glucuronidase release by PA10 was not enhanced by the addition of PMA. Propranolol, which inhibits protein kinase C as well as phosphatidic acid phosphohydrolase, strongly inhibited the degranulation reactions induced by PA10 and PMA. Ethanol, a metabolic modulator of phospholipase D, and cyclic AMP did not affect the degranulation reactions by PMA and PA10.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Phosphatidic acid induces the release of beta-glucuronidase but not lactoferrin from electropermeabilized human neutrophils. 820 72


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