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)

Eosinophils from the blood of normal individuals were purified by centrifugation over discontinuous Percoll gradients. Eosinophil suspensions were obtained with a mean purity of 96% and a mean recovery of 64% (n = 19). When incubated with phorbol-myristate acetate, eosinophils consumed twice as much oxygen as did neutrophils from the same donors. With serum-treated zymosan, 70% and 100% of the maximal oxidative response (i.e. the response to phorbol-myristate acetate) was obtained with eosinophils and neutrophils, respectively. The calcium ionophore A23187 is a weak stimulus that triggered only 2.5% of the eosinophil and 10% of the neutrophil oxidative capacity. The response of both cell types to formyl-methionyl-leucyl-phenylalanine (fMLP) was rapid, with a maximum after 3 min. The magnitude of this eosinophil reaction was half that of neutrophils. Although the activities of the granule enzymes beta-glucuronidase and arylsulphatase were 2.5 and 6 times higher in eosinophils than in neutrophils, respectively, the exocytosis of these enzymes in response to various stimuli was lower in eosinophils. The high yield of eosinophils from our separation method enabled us to prepare eosinoplasts by centrifugation of eosinophils over discontinuous Ficoll gradients that contained cytochalasin B. Eosinoplasts are plasma membrane vesicles derived from eosinophils, filled with cytoplasm but devoid of granules and nucleus. The eosinoplasts contained 30% of the cytoplasm and plasma membrane present in intact eosinophils. Eosinoplasts still possessed a functionally intact oxidase enzyme that could be stimulated with various stimuli. Therefore, eosinoplasts may provide a valuable tool to study separately the role of the oxidase products and that of the granule contents in eosinophil functions.
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PMID:Purification of eosinophils from normal human blood, preparation of eosinoplasts and characterization of their functional response to various stimuli. 381 66

Human platelet factor 4 (PF4) and a substituent dodecapeptide designated PF4(59-70) elicited human neutrophil and monocyte chemotaxis with a similar concentration-dependence and maximal responses equal to that attained by chemotactic fragments of C5 (C5fr). At maximally chemotactic concentrations, PF4(59-70) stimulated the secretion by neutrophils of approximately 40% and 60% of the respective quantities of beta-glucuronidase and beta-glucosaminidase released by 10(-6) M N-formyl-methionyl-leucyl-phenylalanine (fMLP). In contrast to the deactivation of chemotaxis achieved by preincubation of neutrophils with other chemotactic factors, prior exposure to 10(-6)M PF4(59-70) for 2 min, or 20 min at 37 degrees, enhanced by 1.5- to 2-fold the chemotactic responses of neutrophils evoked by optimal concentrations of fMLP, C5fr, leukotriene B4, and PF4(59-70). Concentrations of PF4(59-70) which enhanced neutrophil chemotaxis inhibited the rate of receptor-mediated internalization of [3H]fMLP at 37 degrees and 18 degrees, but at 0 degrees failed to alter the binding affinity or the number of receptors for [3H]fMLP. Preincubation of neutrophils at 37 degrees with concentrations of PF4(59-70) which enhanced neutrophil chemotaxis also did not affect the subsequent binding of [3H]fMLP at 0 degrees. The inhibition by PF4(59-70) of the receptor-mediated internalization of [3H]fMLP was not mimicked by other positively charged compounds. The specific inhibition of receptor-mediated internalization of fMLP may explain the enhanced chemotactic responsiveness of neutrophils preincubated with PF4(59-70).
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PMID:Inhibition of human neutrophil receptor-mediated uptake of N-formyl-met-leu-phe by platelet factor 4 (59-70). 383 92

The appearance of the adult respiratory distress syndrome (ARDS) during the course of acute illness is believed to result, in part, from intrapulmonary neutrophil sequestration and degranulation induced by circulating inflammatory mediators. To evaluate the role of complement-neutrophil interactions in the pathogenesis of ARDS in man, 34 patients suffering from intra-abdominal sepsis (seven), multisystem trauma (15), or acute pancreatitis (12) were serially studied with regard to neutrophil migratory responses to C5a and F-Met-Leu-Phe, lysosomal content of beta-glucuronidase and lysozyme, and simultaneously obtained plasma levels of immunoreactive C3adesArg and C5adesArg. Nineteen patients developed ARDS. In these patients, plasma C3adesArg levels obtained within 72 hours of admission to the hospital were elevated to 305 +/- 35 ng/ml compared with 145 +/- 16 ng/ml for patients who did not develop ARDS (p less than 0.0005). C5adesArg levels were not elevated in either group. In vitro studies showed that neutrophils from normal persons were able to clear all of the C5a/C5adesArg generated in up to 5% zymosan-activated serum, while no clearance of C3adesArg was identified. Patient migratory responses could be divided into three groups based on their initial (less than 72 hour) samples: (1) hyperresponsive to both N = formyl-methionyl-leucyl-phenylalanine (FMLP) and C5a, (2) specifically deactivated to C5a, and (3) deactivated to both C5a and FMLP. Patients in the latter two groups developed ARDS. Enzyme content of neutrophils from patients who developed ARDS showed a substantial fall in beta-glucuronidase and lysozyme levels. The finding of elevated plasma C3a levels and deactivation of migratory response to C5a support the contention that complement activation had occurred in these patients and that their neutrophils had been exposed to C5a/C5adesArg in vivo. The finding of nonspecific migratory dysfunction associated with lysozymal enzyme loss, a circumstance not reproducible in vitro by C5a exposure, suggests that other stimuli produced degranulation of neutrophils made hyperresponsive by prior exposure to C5a.
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PMID:Complement activation and clearance in acute illness and injury: evidence for C5a as a cell-directed mediator of the adult respiratory distress syndrome in man. 400 15

The effects of the co-carcinogenic phorbol ester, phorbol myristate acetate (PMA), on N-formyl-Met-Leu-Phe (FMLP)-induced human polymorphonuclear leukocyte chemokinesis and release of granular lysozyme and beta-glucuronidase were compared with those of the inactive phorbol didecanoate (PDD). Release of the enzymes was enhanced by PMA but was unaffected by PDD which also had no effect on chemokinesis. In contrast, FMLP-induced chemokinesis was completely suppressed by PMA in a dose-dependent fashion (ID50 = 3.5 nM). PMA also inhibited the FMLP-induced increase in cytoplasmic calcium level, measured by the fluorescent indicator quin-2. These and other results suggest that although the diacylglycerol/protein kinase C system is involved in the positive regulation of certain neutrophil functions (degranulation and superoxide generation), if it is very powerfully stimulated, as with PMA, it has inhibitory actions on other neutrophil properties such as motility.
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PMID:Phorbol myristate acetate enhances human polymorphonuclear neutrophil release of granular enzymes but inhibits chemokinesis. 406 81

A simple test for the detection of bacterial enzymes has been developed using paper strip impregnated with different chromogenic substrates. The test was applied to 145 strains belonging to various species of the family Enterobacteriaceae. Positive reactions were revealed after four hours of incubation at 35 degrees C by the formation of a yellow colour indicating released nitrophenol or nitranilide where a loopful of bacteria had been placed. The results of the multistrips test were in agreement with those obtained by previously described methods for the detection of beta-galactosidase, beta-xylosidase, beta-glucuronidase, gamma-glutamyltransferase, and phenylalanine ammonialyase. The suitability of the test for rapid determination of the enzyme profile in enterobacteria is discussed.
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PMID:A rapid multistrips tests for determination of the enzyme profile in enterobacteria. 406 13

Previous reports have suggested that histamine modulates neutrophil chemotaxis, but this has not been observed by all laboratories. We have re-addressed this controversial point and demonstrate that histamine and H1- and H2-receptor-specific agonists cause limited inhibition of chemotaxis while stimulating chemokinesis. Furthermore, using the chemoattractant N-formyl-methionyl-leucyl-phenylalanine (f-met-leu-phe) as a stimulus, we demonstrate that histamine and H1/H2 agonists inhibit f-met-leu-phe-stimulated changes in membrane potential (monitored with the cyanine dye dipentyloxacarbocyanine), superoxide anion production (cytochrome c reduction), hydrogen peroxide formation (scopoletin fluorescence), and degranulation of granule contents (lysozyme and beta-glucuronidase) in a dose-dependent manner but have no effect on neutrophil functions stimulated by the secretagogues phorbol myristate acetate or A23187. All inhibitory effects of histamine and the H1/H2 agonists are reversed in a competitive manner by the H2 antagonist cimetidine. In addition, structure-activity studies using H1 and H2 receptor agonists and antagonists indicate that a single site with specificity for both H1 and H2 analogue structures modulates the various f-met-leu-phe-stimulated functions studied. Kinetic studies demonstrate that the inhibitory effects of histamine on neutrophil function are only observed when histamine is added before f-met-leu-phe and that inhibition occurs within 10 to 20 sec of histamine addition, does not persist after its removal, and is reversed by addition of cimetidine 10 to 20 sec before stimulation with f-met-leu-phe. Although the inhibitory effects of histamine are exerted early in the sequence of PMN activation by f-met-leu-phe, histamine does not affect the binding or internalization of f-met-leu-[3H]phe. The ability of histamine to modify the variety of neutrophil responses demonstrated in this report suggests an important and direct role for histamine in the regulation of inflammatory reactions in acute allergic settings or other disease states in which histamine release may occur.
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PMID:Histamine modulation of human neutrophil oxidative metabolism, locomotion, degranulation, and membrane potential changes. 613 22

The degranulation response of human neutrophils to the calcium ionophore A23187, serum opsonized zymosan (ZC), aggregated gamma-globulin (A gamma G), C5a, formyl-methionyl-leucyl-phenylalanine (FMLP), and PMA has been studied as a reaction time course in order to compare the release kinetics of the separate granule types. Cell suspensions were treated with submaximal doses of stimuli for various time intervals, and the isolated supernatants were assayed for granule constituents. Lactoferrin (LF), a unique specific (secondary) granule protein, was measured by radioimmune assay, and the azurophil (primary) granule components, myeloperoxidase (MPO) and beta-glucuronidase (beta-glu), by enzymatic activity. A sequential pattern of first LF release followed by MPO and beta-glu was demonstrated with each of the stimuli examined, with or without cytochalasin B pretreatment. These kinetic studies demonstrate that the extracellular release of the specific and azurophil granules occur sequentially in human neutrophils with both soluble and particulate stimuli. These findings support the concept that the two granule types are subject to separate controlling factors.
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PMID:The sequential release of granule constitutents from human neutrophils. 615 6

A human neutrophil protease, initially termed neutral peptide-generating protease, has been shown to cleave angiotensin II directly from angiotensinogen and has been identified as leukocyte cathepsin G. When purified neutrophils were disrupted by nitrogen cavitation and fractionated by differential centrifugation, 44 and 24% of the angiotensin II-generating activity was in the lysosomal and undisrupted cell fractions, respectively. Cytochalasin B-treated human neutrophils stimulated with N-formyl-L-methionyl-L-leucyl-L-phenylalanine released beta-glucuronidase, lysozyme, and angiotensin II-generating protease in a dose-dependent fashion, consistent with localization of this protease to the neutrophil granule. Individually purified angiotensin II-generating protease and cathepsin G had similar proteolytic and esterolytic activity for angiotensinogen and N-benzoyl-L-tyrosine ethyl ester on a weight basis, exhibited identical mobilities by SDS-gradient polyacrylamide gel electrophoresis and pH 4.3 disc-gel electrophoresis, and gave precipitin lines of antigenic identity on Ouchterlony analysis with goat antibody to the angiotensin II-generating protease. Thus, the angiotensin II-generating protease of human neutrophils has been identified as cathepsin G on the basis of subcellular localization, substrate specificity, physicochemical characteristics, and antigenic identity.
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PMID:Identification of a human neutrophil angiotension II-generating protease as cathepsin G. 617 48

N-Formylmethionyl-leucyl-phenylalanine (FMLP) is a synthetic chemotactic peptide which induced beta-glucuronidase and lysozyme release from human neutrophils treated with cytochalasin B. FMLP-releasing effects were rapid and dose dependent. Unlike other secretagogues of neutrophils (e.g., zymosan and immune complexes), FMLP secretory activity was not modulated by acetylcholine, which by itself did not release lysosomal enzymes from human neutrophils. Isolated rat mast cells did not respond to FMLP, which has been demonstrated to release histamine from human neutrophils. Two markers of rat mast cell secretory granules, histamine and beta-glucuronidase, were assayed, but the results were negative for both. In the same experimental conditions, 48/80 released histamine and the enzyme: the ratio of the net percentage release of beta-glucuronidase to the net percentage release of histamine was congruent 0.4.
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PMID:N-Formylmethionyl-leucyl-phenylalanine: Different releasing effects on human neutrophils and rat mast cells. 619 52

The short transient increase of the intracellular cAMP concentration during the first minute following stimulation, exocytosis from specific and azurophil granules, random and directional locomotion were assessed following stimulation of human and equine neutrophils with f-Met-Leu-Phe, C5ades Arg, standard gamma globulin (SGG) and the ionophore A23187. Different leucocyte-activating agents elicited distinct patterns of responses. The results showed that: Chemotactic factors produced exocytosis of small amounts of vitamin B12-binding proteins but not beta-glucuronidase, in the absence of cytochalasin B. Chemotaxis, the appearance of the transient cAMP peak and exocytosis from specific granules in response to cytotaxins were strictly correlated in the absence of cytochalasin B but not if exocytosis was measured in the presence of cytochalasin B. Thus comparison of exocytosis measured in the presence of cytochalasin B with other functions may be misleading. The non-chemotactic agents tested (SGG, A23187) produced secretion but no cAMP peak within 1 minute after stimulation, indicating that the cAMP peak is no obligatory event for triggering exocytosis in general. The ionophore A23187 alone at a concentration of 10(-6) M produced exocytosis from specific granules only, increased motility of cells in suspension and a marked increment of neutrophil adhesion to glass and after a lag period a sustained increase in cAMP. SGG elicited release of both vitamin B12-binding proteins and beta-glucuronidase.
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PMID:Relationship between the transient cAMP increase, exocytosis from specific and azurophil granules and chemotaxis in neutrophil granulocytes. 619 57


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