Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.3.5 (5'-nucleotidase)
 3,167 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Monocytes of healthy, full-term newborns were isolated from cord blood, and functional and biochemical activities were quantitated. The yield of monocytes per milliliter of cord blood was 60% greater than that from the peripheral blood of healthy adults. Placental monocytes were initially less well spread than cells from adults, but no other morphological differences were noted. During 4 days of in vitro cultivation, placental monocytes secreted lysozyme at a constant rate, lost peroxidase activity, and increased 5'-nucleotidase activity 15- to 25-fold. Similar findings were obtained with monocytes from adults. Placental monocytes also displayed Fc and complement receptor activity. Ingestion and intracellular multiplication of Toxoplasma gondii were identical in normal placental and adult monocytes. Furthermore, toxoplasma multiplication was significantly inhibited by cells from both sources when the monocytes were preincubated with supernatants prepared from sensitized lymphocytes and toxoplasma antigen. Monocytes from newborns were competent cells in terms of the specific functions and activities we examined.
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PMID:Monocyte function in human neonates. 64 Jul 36

Stable cultures of mononuclear phagocytes from carrageenan-induced granulomas in mice have been established after enzymatic dispersion of these lesions. The cells can be maintained for up to 3 wk without division in serum-free media. The mononuclear phagocytes were identified by several criteria. The cells are adherent, phagocytic, contain lysosomal acid hydrolases at high specific activities, secrete lysozyme, and bind soluble aggregates of IgG. The activities of 5'-nucleotidase and leucine aminopeptidase in the cultured granuloma cells showed that they resembled macrophages from thioglycollate-stimulated mice but not unstimulated macrophages in these respects. Supernates from the cultured granuloma cells contain factor(s) which induce the proliferation of thymocytes; the release of such factors by the cells is stimulated by lipopolysaccharide.
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PMID:Mononuclear phagocytes from carrageenan-induce granulomas. Isolation, cultivation, and characterization. 67 Aug 87

Subcellular fractionation studies in resting human neutrophils indicated a bimodal distribution for cytochrome b. A major peak of cytochrome b co-sedimented with gelatinase under different experimental conditions. This localization was partially overlapped with specific granules (using lysozyme and lactoferrin as specific granule markers), but clearly resolved from azurophilic granules, plasma membrane, mitochondria, as well as from a novel alkaline phosphatase-rich intracellular organelle. A minor localization of cytochrome b was found in fractions enriched in both the plasma membrane marker 5'-nucleotidase and alkaline phosphatase. A significant portion of ubiquinone cell content co-fractionated with the gelatinase-containing granules. After phorbol myristate acetate (PMA)-cell stimulation, cytochrome b was mobilized to fractions showing respiratory burst activity and enriched in 5'-nucleotidase activity. This mobilization paralleled secretion of gelatinase and lysozyme to the extracellular medium. Furthermore, neutrophil stimulation with fluoride in the absence of cytochalasin B induced release of gelatinase and generation of superoxide anion with only minimal release of lysozyme. Preincubation of cells with the anion channel blocker 4,4'-diisothiocyanostilbene-2,2'-disulfonic acid (DIDS) prevented lysozyme release, but had only a minor effect on the release of gelatinase and did not inhibit the superoxide anion generation elicited by N-formyl-methionyl-leucyl-phenylalanine or PMA. These results suggest a main location of cytochrome b in mobilizable gelatinase-containing granules, which can constitute a subpopulation of specific granules. Furthermore, these findings show that the gelatinase-containing granule is functionally involved in the respiratory burst in neutrophils and that membrane fusion between plasma membrane and the gelatinase-containing granule occurs during activation of cells.
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PMID:Cytochrome b co-fractionates with gelatinase-containing granules in human neutrophils. 165 2

The assignment of cytochrome b-558 as a component of the O2- (H2O2) -generating enzyme in guinea-pig alveolar macrophages was investigated. Guinea pig alveolar macrophages contained 76 pmol cytochrome b-558/mg protein, a value very similar to that of neutrophils. The rate of myristic acid-stimulated O2- generation by alveolar macrophages, calculated per cytochrome b-558, was only one-fourth that of neutrophils. An analysis of Percoll density gradient centrifugation profiles showed that the H2O2-generating activity of myristic acid-activated alveolar macrophages was concentrated in a single peak which was consistently associated with 5'-nucleotidase activity, a plasma membrane marker enzyme. A little H2O2-generating activity was seen with unactivated alveolar macrophages. Furthermore, the cytochrome b-558 of both myristic acid-activated and unactivated alveolar macrophages was also predominantly associated with 5'-nucleotidase activity and was found in trace amounts in a peak containing lysozyme activity, a marker of lysosome granules. Only about 6% of the cytochrome b-558 in plasma membranes from myristic acid-activated guinea-pig alveolar macrophages was anaerobically reduced by 0.5 mM NADPH, while under the same conditions about 30% of the heme protein of myristic acid-activated neutrophils was reduced. These results suggest two conclusions: firstly, that in both activated and unactivated alveolar macrophages, cytochrome b-558 is located in the plasma membrane, and the translocation of cytochrome b-558 does not occur during the activation of NADPH oxidase; and secondly, that a smaller part of cytochrome b-558 is associated with the activated NADPH oxidase of guinea pig alveolar macrophages compared with neutrophils.
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PMID:Presence of cytochrome b-558 in guinea-pig alveolar macrophages-subcellular localization and relationship with NADPH oxidase. 283 23

The effect of blastolysin, a glycopeptide of the cell walls of L. bulgaricus, on the resistance of mice to infections caused by S. typhimurium and B. pertussis, lysozyme levels in the blood serum and 5'-nucleotidase activity of peritoneal macrophages was studied. The changes in the nonspecific resistance of mice due to the effect of blastolysin depended on the administration route and the type of the developing infection. It activated the enzymatic activity of the peritoneal macrophages and changed the lysozyme levels in the blood serum of mice. The optimal protective effect of blastolysin was achieved on intramuscular injection in a dose of 100 micrograms.
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PMID:[Change in the natural immunity of mice after administration of blastolysin, a glycopeptide from the Lactobacillus bulgaricus cell wall]. 299 70

The influence of extracts from oak bark, St. John's-wort leaves and pine buds on natural immunity characteristics of mice has been studied. The injection of these extracts into mice has been found to enhance their resistance to infection with Staphylococcus aureus and Bordetella pertussis virulent cultures, to decrease the enzymatic activity of 5'-nucleotidase in the peritoneal exudate macrophages of mice and to increase the level of lysozyme in their blood. The action of these extracts has proved to depend on their dosage and the time of observation.
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PMID:[Action of plant extracts on the natural immunity indices of animals]. 301 9

NADPH oxidase, a complex enzyme system in the cell membrane responsible for the bactericidal function of polymorphonuclear leukocytes through the production of superoxide anion, was facilely released by mild treatment with a press. At the pressure where almost all NADPH oxidase activity was released, releases of the activities of lactate dehydrogenase, 5'-nucleotidase, lysozyme, and N-acetyl-beta-glucosaminidase, and of the amount of total protein were negligible. This method can be useful for the elucidation of NADPH oxidase.
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PMID:Facile release of NADPH oxidase from polymorphonuclear leukocyte membrane by mild pressure treatment. 381 61

An iso-osmotic Percoll density gradient was applied to determine the subcellular localization of the O2- generating enzyme, NADPH oxidase, in guinea pig polymorphonuclear leukocytes (PMN). [14C]Myristate (MA) was employed as a metabolic stimulant in order to clarify whether the myristate binding site on PMN membrane was identical with the O2- generating site. The distribution pattern of the O2- generating activity of MA-activated PMN was compared with that of unactivated PMN in parallel experiments to find fractions showing an enhanced O2- generating activity (i.e., above the background values due to O2-generation by other electron-transport systems). We observed very high O2- generating activity concentrated in a single peak with MA-activated PMN but little activity was seen with unactivated PMN in the Percoll density gradient. The O2- generating activity of MA-activated PMN was consistently associated with 5'-nucleotidase activity as a membrane marker enzyme, but was not associated with lysosomal marker enzymes such as myeloper-oxidase and lysozyme. O2- generating and 5'-nucleotidase activities in the peak fraction of MA-activated PMN were increased to about six and four times those of whole cells in terms of specific activity, respectively. These results indicate that the O2- generating enzyme is located on PMN plasma membrane. Furthermore, [14C]myristate-binding activity was mainly found in the peak fraction containing O2 - generating enzyme. This suggests that [14C]myristate binds to plasma membrane, and the O2 - generating enzyme may thus be activated.
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PMID:Subcellular localization of O2- generating enzyme in guinea pig polymorphonuclear leukocytes; fractionation of subcellular particles by using a Percoll density gradient. 627 84

The localization of the Pseudomonas aeruginosa lectins (PA-I and PA-II) was studied using methods of osmotic shock, freezing and thawing and spheroplast formation. Very slight release of the two lectins occurred when P. aeruginosa was exposed to magnesium-osmotic shock or was frozen and thawed. Under these conditions, release of the periplasmic 5'-nucleotidase occurred, whereas no release of cytoplasmic glucose-6-phosphate dehydrogenase activity was detected. Formation of spheroplasts from P. aeruginosa by gradual removal of the bacterial envelopes revealed low lectin activity in the treatment fluids. Osmotic shock treatment of the lysozyme treated mureinoplasts resulted in low release of glucose-6-phosphate dehydrogenase and the two lectins (10-13%) and a considerable activity (38.4%) of 5'-nucleotidase. The presence of the lectins on the outer and the cytoplasmic membranes enabled intact cells and spheroplasts of P. aeruginosa to agglutinate papain-treated human erythrocytes. These results indicate that the two lectins are located mainly in the cytoplasm with small fractions on the cytoplasmic and outer membranes and in the periplasmic space.
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PMID:The intracellular localization of Pseudomonas aeruginosa lectins. 631 95

The inducible cholinesterase of Pseudomonas aeruginosa strain K (ATCC 25102) degraded propionylcholine, acetylthiocholine, acetylcholine and acetyl-beta-methylcholine at a high rate and butyrylcholine and succinylcholine at very low rates. The localization of the enzyme in the periplasmic space was indicated by a similar rate of acetylcholine degradation by intact cells or their extracts, by release of cholinesterase together with alkaline phosphatase into the culture medium during cell growth in a low phosphate-containing medium, by liberation of cholinesterase and alkaline phosphatase during lysozyme-induced conversion of cells to spheroplasts and by freezing and thawing. Threatment of cells with diazo-7-amino-1,3-naphthalenedisulphonic acid, which inactivates surface-located enzymes, abolished most of the cholinesterase and 5'-nucleotidase activities.
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PMID:Localization of cholinesterase in Pseudomonas aeruginosa strain K. 677 68


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