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)

In 25 patients (10 women and 15 men) aged 37 to 68 years activity of the following enzymes has been determined by the use of semiquantitative cytochemical methods: acid and alkaline phosphatase, beta-glucuronidase, N-acetyl-beta-glucosaminidase and myeloperoxidase. Additionally the content of glycogen and lipids has been determined in the cells studied. An increase of the myeloperoxidase and acid phosphatase activity and a decrease of the glycogen and the lipid content has been stated in neutrophils of the patients. Above alterations may reflect antitumor reactivity of neutrophils or nonspecific neutrophil response against inflammatory changes accompanying the tumor area.
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PMID:Enzymes of peripheral blood neutrophils in patients with cancer of the stomach. 631 12

We have found that pretreatment of human neutrophils with phenytoin (0.05 to 0.8 mM) results in concentration-dependent, reversible inhibition of both superoxide anion generation and release of lysosomal enzymes (myeloperoxidase, lysozyme, beta-glucuronidase) provoked by either the synthetic peptide, N-formyl-methionyl-leucyl-phenylalanine (FMLP) or the complement fragment C5a. In contrast, phenytoin did not inhibit either enzyme release or superoxide anion generation by neutrophils stimulated with phorbol myristate acetate or serum-opsonized zymosan particles. Phenytoin did not provoke leakage from neutrophils of the cytoplasmic enzyme, lactate dehydrogenase, and did not inhibit directed migration (chemotaxis) of neutrophils toward either FMLP or C5a. Specific binding of 3H-FMLP to neutrophil membrane receptors was not altered significantly by pretreatment of the cells with a wide range of concentrations of phenytoin. With flow microfluorometry and the fluorochrome, 3,3'-dipentyloxacarbocyanine, phenytoin was shown to prevent FMLP-induced changes in fluorescence intensity (i.e., apparent neutrophil membrane depolarization). These data indicate that various neutrophil functions may be regulated independently at other than the receptor level and that neutrophil chemotactic responses to FMLP and C5a do not appear to be dependent on membrane events registered by 3,3'-dipentyloxacarbocyanine.
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PMID:Selective inhibition by phenytoin of chemotactic factor - stimulated neutrophil functions. 631 77

Implanted foreign bodies are highly susceptible to pyogenic infections and represent a major problem in modern medicine. In an effort to understand the pathogenesis of these infections, we studied the phagocytic function in the vicinity of a foreign body by using a recently developed guinea pig model of Teflon tissue cages subcutaneously implanted (Zimmerli, W., F.A. Waldvogel, P. Vaudaux, and U.E. Nydegger, 1982, J. Infect. Dis., 146:487-497). Polymorphonuclear leukocytes (PMN) purified from tissue cage fluid had poor bactericidal activity against a catalase-positive microorganism. When compared with blood or exudate PMN, they exhibited a significant reduction in their ability to generate superoxide in response to a particulate or a soluble stimulus (72 and 57%, respectively, P less than 0.001). Not only their total contents in myeloperoxidase, beta-glucuronidase, lysozyme, and B12 binding protein were significantly reduced (by 62, 21, 47, and 63%, respectively, P less than 0.01), but also their capability for further secretion of residual B12 binding protein upon stimulation. Ingestion rates of endotoxin-coated opsonized oil particles were reduced by 25% (P less than 0.05). In an effort to reproduce these abnormalities in vitro, fresh peritoneal exudate PMN were incubated with Teflon fibers in the presence of plasma. Interaction of PMN with the fibers led to significant increases in hexose monophosphate shunt activity and exocytosis of secondary granules (P less than 0.01). PMN eluted after such interaction showed defective bactericidal activity, oxidative metabolism, and granular enzyme content similar to those observed in tissue cage PMN. The local injection of fresh blood PMN into tissue cages at the time of, or 3 h after, inoculation with 100 microorganisms (Staphylococcus aureus Wood 46) reduced the infection rate from 50 to 56 cages to 1 of 21 (P less than 0.001) and 3 of 8 cages (P less than 0.001), respectively. These results suggest that the in vivo as well as in vitro interaction of PMN with a nonphagocytosable foreign body induces a complex PMN defect, which may be partly responsible for the high susceptibility to infection of foreign bodies.
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PMID:Pathogenesis of foreign body infection. Evidence for a local granulocyte defect. 632 36

The degranulation and release of lysosomal (myeloperoxidase, beta-glucuronidase, lysozyme) and cytoplasmic (lactate dehydrogenase-LDH) enzymes from polymorphonuclear neutrophil granulocytes (PMG) during phagocytosis of inert latex particles or bacteria were studied. Degranulation was much faster and more pronounced by phagocytosis of bacteria than of inert particles. A high frequency of lysosome-lysosome as well as lysosome-phagosome fusions suggested that granular material was transported by lysosome- lysosome- phagosome fusions. During bacterial phagocytosis there was evidence of release of granular material into cytoplasm causing enzymatic disintegration. After 60 minutes cell lysis occurred in about 5 per cent of the cells during bacterial phagocytosis. There was non-specific release of LDH during phagocytosis of inert particles, probably due to erythro-phagocytosis. After 60 minutes the release during bacterial phagocytosis amounted to 20-30 per cent of the enzyme content of the cells. A nearly equal release of lysosomal and cytoplasmic enzymes gave support for the idea that cell lysis was the main mechanism of enzyme release.
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PMID:Degranulation and enzyme release during phagocytosis of inert particles and of bacteria by polymorphonuclear neutrophil granulocytes. 632 36

The heterogeneity of human neutrophil granules, particularly of azurophil granules, defined as peroxidase containing, was examined by measuring N-acetyl-beta-D-glucosaminidase in fractions of isopycnic sucrose gradients of such granules. Neutrophil granules were prepared from normal human blood, monodispersed in heparinized sucrose, and centrifuged by established methods. N-Acetyl-beta-D-glucosaminidase was previously shown to be exquisitely sensitive to small amounts of heparin; paradoxically, larger amounts restore activity. The inhibition is reversed with protamine. N-Acetyl-beta-D-glucosaminidase activity had its peak at density 1.20 gm/ml (band B) and a lesser peak at density 1.22 gm/ml (band A). Mean specific enzyme activity was 899 +/- 217 nmol p-nitrophenol released per minute per milligram protein in gradient fraction 12 (band B), and 507 +/- 149 nmol p-nitrophenol released per minute per milligram protein in fraction 8 (band A) (p less than 0.01), which correlated in part to the significantly higher protein content in band A. These specific activities are 31-fold and 17-fold greater, respectively, then mean neutrophil lysate specific activity of 28.8 +/- 7.0 nmol p-nitrophenol released per minute per milligram protein, indicating a considerable concentration of granule enzyme activity in these gradient bands. The gradient distribution of N-acetyl-beta-D-glucosaminidase is nearly identical to that of myeloperoxidase and beta-glucuronidase, thus providing another enzyme marking the existence of two populations of azurophil granules, separable by density. Of total gradient enzyme activity, the mean percentage distribution of N-acetyl-beta-D-glucosaminidase in the pellet was 0.3%. Because the mean percentage of total gradient activity in the pellet was on an order of magnitude higher for myeloperoxidase (4.7%), beta-glucuronidase (3.7%), lysozyme (3.9%), and protein (2.8%), our data suggest that N-acetyl-beta-D-glucosaminidase has a possibly unique site within or an affinity to one or both of the two populations of azurophilic granules that is distinct from that for myeloperoxidase and beta-glucuronidase.
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PMID:Human neutrophil N-acetyl-beta-D-glucosaminidase: granule localization. Further evidence for two azurophil granules. 633 Feb 50

The influence of taurine on neutrophil phagocytic and bactericidal capacities and lysosomal enzyme-releasing ability was evaluated in the present study using neutrophils obtained from casein-elicited rat peritoneal exudates. Taurine was dissolved in drinking water at a concentration of 0.3%, and the solution was given to rats for 1-21 days (460 mg/kg/day). Taurine concentration in the serum increased with the term of its administration, while in the neutrophils, it increased significantly after administration for 1 or 3 days. When administered for 7 or 10 days, however, no difference was noted from the control group, but then the concentration remarkably increased after 21 days of administration. The bactericidal capacity of the neutrophils against Escherichia coli was strengthened as their concentration of taurine increased; phagocytic capacity was also strengthened. The release of myeloperoxidase following phagocytosis of yeasts increased with administration, while the release of beta-glucuronidase, lysozyme and lactate dehydrogenase, which are induced by N-formylmethionyl-leucyl-phenylalanine, were inhibited. The hypotonic hemolysis of erythrocytes was also inhibited. Taurine decreased the fluorescence depolarization of diphenylhexatriene, indicating an increase in membrane fluidity. These results suggested that taurine strengthens both phagocytic and bactericidal capacities of neutrophils by increasing the fluidity of neutrophil membrane and membrane stability and thus plays an important role in the mechanism of host defense.
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PMID:[Role of taurine in neutrophil function]. 650 Apr 3

Rat peritoneal polymorphonuclear leukocytes accumulate radioactivity when incubated with 17 microM L[4,5-3H]leucine methyl ester; only low levels of accumulation are observed when the cells are incubated with equivalent amounts of labeled D-leucine methyl ester or the free amino acid, L-leucine. More than 98% of the intracellular radioactivity of cells incubated with leucine methyl ester is in the form of leucine. When cells that had been preincubated with L-leucine methyl ester were disrupted by sonication, 72% of the intracellular radioactivity could be trapped on glass fiber filters, indicating that the leucine had accumulated within a particulate intracellular compartment. Granule preparations obtained from the polymorphonuclear leukocytes accumulated leucine in the presence of leucine methyl ester in a manner similar to the intact cells. Separation by density gradient centrifugation of the granules obtained from cells preincubated with labeled leucine methyl ester revealed a nearly exact correspondence between the density distribution of accumulated radioactivity and that for beta-glucuronidase, an enzyme localized with the azurophilic subpopulation of polymorphonuclear leukocyte granules; there was no such correspondence with the activity of alkaline phosphatase, a marker for the specific granules. The results indicate that the azurophilic granules represent the intracellular site of leucine accumulation by the intact cells. This conclusion is supported by the effects of millimolar concentrations of amino acid methyl ester, which cause a dramatic loss of latency for the activities of the azurophilic granule enzymes beta-glucuronidase and myeloperoxidase but have no effect upon the latency of the specific granule enzyme alkaline phosphatase. Leucine accumulation by the intact cells is 80% inhibited by 0.1 mM chloroquine and 50% inhibited by 20 mM NH4Cl and methylamine, lysosomotropic agents that elevate the intralysosomal pH. These observations suggest that the azurophilic granules of these cells, generally considered to be primary lysosomes, are internally acidified.
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PMID:Accumulation of amino acids within intracellular lysosomes of rat polymorphonuclear leukocytes incubated with amino acid methyl esters. Evidence for the internal acidification of azurophilic granules. 668 51

The morphologic, cytochemical, and ultrastructural pathology of the blood and bone marrow of an infant with Mucopolysaccharidosis Type VII (MPS VII) is reported. The neutrophils, monocytes, basophils, and eosinophils contained prominent granulation of the Alder-Reilly type. The lymphocytes, plasma cells, osteoblasts, and macrophages contained cytoplasmic inclusions surrounded by clear vacuoles. Cytochemically, the granulocytes, monocytes, and lymphocytes were negative for beta-glucuronidase, negative or weakly metachromatic with toluidine blue, and positive for acid phosphatase. Macrophages were negative with toluidine blue. A normal staining pattern was present with myeloperoxidase and periodic acid-Schiff (PAS). Ultrastructural studies showed abnormal vacuoles in neutrophils, basophils, eosinophils, monocytes, lymphocytes, plasma cells, and macrophages. Occasional vacuoles contained Ruthenium Red positive material and confirmed the presence of acid mucopolysaccharide in these cells. This report confirms previously described abnormalities in peripheral blood cells in MPS VII, demonstrates additional abnormalities in bone marrow, and reports cytochemical reactions in leukocytes in MPS VII.
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PMID:Mucopolysaccharidosis type VII. A morphologic, cytochemical, and ultrastructural study of the blood and bone marrow. 681 36

A quantitative cytochemical study has been made, using scanning-integrating microdensitometry, of 1000 toxic granulation blood neutrophils from 20 infected patients, in comparison with 1250 normal blood neutrophils. Myeloid precursor cells in 10 normal marrows were also studied. Normal bone marrow granulocyte maturation was associated with a progressive decrease in azurophilic granule enzymes (myeloperoxidase, beta-glucuronidase, acid phosphatase, chloroacetate esterase), and also Alcian blue staining from acid mucosubstance, but an increase in the specific granule marker lactoferrin. Toxic granulation blood neutrophils showed minor changes in the enzyme content of their azurophilic and specific granules, consistent with cell immaturity, and an increase in acid mucosubstance in azurophilic granules. Abnormal maturation of azurophilic granules, with persistence of acid mucosubstance, is the likely explanation for the intense Romanowsky dye staining of the toxic granulation neutrophil.
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PMID:Quantitative cytochemistry of the toxic granulation blood neutrophil. 684 17

Polymorphonuclear leucocytes were isolated from pig blood relatively free from other cells and were characterised biochemically and morphologically and compared with human PMNLs. The activities of 16 enzymes of porcine and human PMNLs were measured and compared. Alkaline phosphatase, acid phosphatase, phosphodiesterase, gamma-glutamyl transpeptidase, NADH-cytochrome c oxidoreductase, malate dehydrogenase and acetylcholinesterase had higher specific activities in procine than in human cells. Alkaline phosphatase has an 87-fold higher specific activity in porcine than in human cells. beta-glucuronidase, lysozyme, beta-galactosidase, N-acetyl-glucosaminidase, beta-glucosidase, myeloperoxidase and catalase had higher specific activities in human than in porcine cells. beta-glucuronidase and myeloperoxidase showed over a 1000- and a 13-fold higher specific activity, respectively, in human than in porcine cells. Porcine PMNLs are readily available in large numbers and are recommended for studies of phagocytosis, chemotaxis and membrane biochemistry.
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PMID:Biochemical characterisation of porcine polymorphonuclear leucocytes: comparison with human polymorphonuclear leucocytes. 687 22


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