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:3.2.1.17 (lysozyme)
21,489 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The antibacterial activity of a myeloperoxidase (MPO)-glucose oxidase system was found to be greatly increased by granulocyte elastase, present in azurophil granules of human neutrophils. The MPO-H2O3-mediated killing of both Escherichia coli and Staphylococcus aureus was potentiated by granuocyte elastase at an acid pH, whereas at pH 7.4 only killing of E. coli was potentiated. The potentiating effect of elastase was not dependent on the enzymatic properties of the protein since it was not abolished by heating, which destroys the enzymatic activity. A peptide chloromethyl ketone elastase inhibitor abolished both elastolytic activity and the pctentiating effects on MPO-H2-O2-mediated bacterial killing. The antibacterial activity of chymotrypsin-like cationic protein of human neutrophils was also potentiated by elastase. Other degradative enzymes isolated from human granulocytes, e.g., collagenase and lysozyme, did not potentiate MPO-H2O2-mediated or cationic protein-dependent bacterial killing. The present study indicates that a neutrophil constitutent, elastase, which is not microbicidal by itself, can initiate sublethal changes that render some microorganisms more susceptible to the action of microbicidal agents like MPO and chymotrypsin-like cationic protein.
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PMID:Microbicidal mechanisms of human granulocytes: synergistic effects of granulocyte elastase and myeloperoxidase or chymotrypsin-like cationic protein. 1 11

To test our hypothesis that neutrophil elastase plays a role in airway hypersecretion associated with the allergic late-phase response, using an isolated tracheal segment system in vivo and measuring lysozyme activity in the perfusate of the lumen as a marker of submucosal gland secretion over 8 h, we studied the response of five allergic dogs to ragweed. The dogs were exposed on separate occasions to specific allergen, to allergen vehicle, and to allergen in the presence of a selective neutrophil elastase inhibitor, ICI 200,355. Allergen exposure caused a marked increase in lysozyme secretion that was significantly increased at 4, 6, and 8 h compared with controls and ICI 200,355-treated dogs. Neutrophil elastase appeared in the perfusate after allergen exposure and was positively correlated with lysozyme secretion at 8 h. These findings suggest that neutrophil elastase plays an important role as a secretagogue in the allergic late-phase response.
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PMID:Role of neutrophil elastase in allergen-induced lysozyme secretion in the dog trachea. 139 99

The neutrophil enzyme elastase is a potent secretagogue of airway secretory cells, and elastase is present in high concentrations in sputum of patients with hypersecretion (e.g., cystic fibrosis, bronchiectasis). Interleukin-8 (IL-8), a recently discovered cytokine with potent neutrophil chemotactic properties in vitro, is also found in the sputum of these patients. We used an isolated tracheal segment in dogs in vivo to study the effect of IL-8 in causing neutrophil accumulation, elastase release, and secretion (by measuring lysozyme concentrations) in the luminal superfusate. IL-8 caused a potent time-dependent neutrophil accumulation at between 3 and 6 h. The effect was significant at 10(-9) and maximum at 10(-8) M. No increase in free elastase, cathepsin G, or lysozyme was detected in the superfusate. Thus, in contrast to previous studies showing that ragweed antigen causes the accumulation of neutrophil elastase which in turn causes lysozyme secretion, IL-8 causes neutrophil accumulation without granule secretion (or subsequent secretagogue activity). The findings were confirmed with dog and human neutrophils in vitro.
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PMID:Interleukin-8 induces neutrophil accumulation but not protease secretion in the canine trachea. 147 6

We have developed a method for electrotransfer of strongly basic proteins (lysozyme, pI 11; mucus proteinase inhibitor, pI greater than 10; bovine pancreas trypsin inhibitor; pI 10.5; human leukocyte elastase, pI greater than 9) from nondenaturing acid gels (pH 4.5) to nitrocellulose sheets. Buffers were those used in a discontinuous system for transfer from sodium dodecyl sulfate (SDS)-containing polyacrylamide gels with one modification in the cathode buffer which contained 0.1% SDS. This method was compared to electrotransfer performed in 0.7% acetic acid. The basic proteins studied, which were positively charged in the gel, formed with SDS negative complexes which migrated toward the anode and were efficiently transferred to the nitrocellulose. Moreover, their biological properties were preserved: inhibitory activity, enzyme activity, and antigenicity. This method is advantageous because it is simple, is sensitive, and can be applied to various biological fluids to detect inhibitors, enzymes, and other proteins which have a basic character, after electrophoretic separation under their native forms.
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PMID:Electrotransfer of basic proteins from nondenaturing polyacrylamide acid gels to nitrocellulose: detection of enzymatic and inhibitory activities and retention of protein antigenicity. 169 33

The antigen which has alpha 2-globulin mobility was identified immunochemically in leukolysate and pus extract. This antigen was localized in polymorphonuclear leukocytes by the immunofluorescence technique in the blood of healthy donors. The alpha 2-globulin of granulocytes (alpha 2GG) is not identical to lactoferrin, lysozyme, granulocyte elastase, fibronectin, fetal hemoglobin, amyloid P-component of the serum. The molecular mass of alpha 2GG is equal to 50 +/- 8 Kd. in the pus extract. The biological role of alpha 2GG is unknown.
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PMID:[Immunochemical identification and physico-chemical characteristics of specific alpha 2 globulin of human granulocytes]. 169 38

Using immunochemical analysis with standard antisera, leukocyte thermostable alpha-glycoprotein (LT alpha G) was shown to be distinct from lactoferrin, lysozyme, and fibronectin. The determination of peroxidase and nonspecific elastase in immune precipitates of LT alpha G gave negative results. Affinity sorption of LT alpha G onto the pus protein component was revealed. Purified LT alpha G had amidolytic activity in response to a substrate for elastase (p-nitroanilide succinyl-trialanyl). The ability of LT alpha G to cause the hydrolysis of substrates for thrombin, kallikrein, plasmin was investigated. The identity of LT alpha G and granulocyte elastase is suggested.
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PMID:[Thermostable leukocyte alpha-glycoprotein: immunochemical study and enzyme activity research]. 310 19

A small series of granulocytic sarcomas (GS) or 'chloromas' has been studied by means of conventional histology and immunohistochemistry. The latter was found to be most useful in the diagnosis and characterization of these neoplasms, which are rare in Great Britain. Polytypic antisera to leukocyte elastase and cathepsin G have proved to be most useful, giving intense staining in all cases. These two markers are more specific than muramidase (lysozyme) and alpha 1-antitrypsin, since, unlike the latter two, they do not stain histiocytic cells. The results of staining with two monoclonal antisera, AGF 4.48 and AGF 4.36, are also described. In addition, the clinicopathological details of the seven cases are summarized and the literature is briefly surveyed.
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PMID:An immunohistochemical and clinicopathological study of granulocytic sarcoma ('chloroma'). 352 33

The effect of gamma versus ethylene oxide sterilization of different dialyzers (polyacrylonitrile, cuprophan) and blood lines on plasma levels of granulocyte elastase and of lysozyme during hemodialysis was investigated in 17 chronically uremic patients. Plasma levels of granulocyte elastase increased during hemodialysis but significantly less in the presence of polyacrylonitrile compared with cuprophan membranes. In contrast, enhanced lysozyme plasma levels decreased during dialysis using the polyacrylonitrile dialyzer to values of healthy controls and remained unchanged using the cuprophan dialyzer. Both effects were not influenced by the way of sterilization. We conclude that granulocyte activation during hemodialysis occurs independently of the sterilization procedure of dialyzers and blood lines in patients showing no clinical signs of hypersensitivity.
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PMID:Effect of gamma radiation versus ethylene oxide sterilization of dialyzers and blood lines on plasma levels of granulocyte elastase in hemodialyzed patients. 385 7

Plasma levels of granulocyte elastase in complex with alpha 1-proteinase inhibitor during hemodialysis were investigated in 15 patients (37.4 +/- 3.2 years) undergoing maintenance hemodialysis (47.0 +/- 12.9 months) with dialyzers made from cellulose hydrate, cuprophan, polymethylmethacrylate, ethylene-vinyl alcohol copolymer, and polyacrylonitrile. Cellulose hydrate membrane caused a maximal increase of the plasma levels of granulocyte elastase in complex with alpha 1-proteinase inhibitor (E-alpha 1PI: 1,659.0 +/- 256.8 ng/ml). Patients dialyzed with polyacrylonitrile dialyzers failed to exhibit comparable plasma levels of granulocyte elastase (E-alpha 1PI: 237.8 +/- 22.9 ng/ml). During hemodialysis plasma E-alpha 1PI values rose to a peak 643.0 +/- 174.7 ng/ml in patients on polymethylmethacrylate dialyzers, to 557.5 +/- 120.0 ng/ml on cuprophan dialyzers, but to only 381.9 +/- 54.0 ng/ml on ethylene-vinyl alcohol copolymer dialyzers. Plasma lysozyme levels decreased significantly in the presence of polyacrylonitrile and polymethylmethacrylate membranes. We conclude that the degree of PMNs stimulation depends on the nature of the dialyzer membrane material. The following membranes induce a reaction of increasing intensity: polyacrylonitrile, ethylene-vinyl alcohol copolymer, cuprophan, polymethylmethacrylate, and cellulose hydrate.
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PMID:Plasma levels of granulocyte elastase during hemodialysis: effects of different dialyzer membranes. 387 6

An antiserum to human cathepsin G has been raised in sheep and its reactivity with human tissues has been tested. The indirect immunoperoxidase staining sequence was employed and was applied to routinely processed paraffin sections. Mature granulocytes, especially those of the neutrophil variety, were intensely and consistently stained. Activity was not observed in other cell or tissue types. Many of the cells of acute and chronic myeloid leukemia were strongly stained, in contrast to those of acute lymphoblastic or chronic lymphocytic leukemias. The results of the technique are compared with those described with staining for muramidase (lysozyme), alpha 1-antitrypsin, leukocyte elastase, and naphthol-AS-D-chloroacetate esterase, and with certain monoclonal antisera directed against granulocyte determinants.
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PMID:Immunohistochemical localization of cathepsin G in human tissues. 391 78


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