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 effects of timolol maleate on the secretion and composition of human saliva were studied in vivo. Eight healthy volunteers received orally 10 mg timolol maleate. Stimulated parotid saliva samples, resting whole saliva samples, and blood samples were collected immediately before and four times after the drug intake at intervals of 1 h. The levels of total protein, lysozyme, IgA, IgG and IgM, salivary peroxidase, myeloperoxidase, lactoferrin, amylase, thiocyanate (SCN-), and hypothiocyanite (OSCN-) were analyzed from saliva samples. Drug levels were measured both from parotid saliva and blood samples. Results were compared to the analyses of the samples collected in a similar way but without administration of any drugs. Decreased levels of total protein, lactoferrin, amylase, and salivary peroxidase were observed in parotid saliva after a single oral dose of timolol maleate. No such decrease was found in lysozyme, myeloperoxidase, SCN-, OSCN-, or immunoglobulins. Salivary flow rate was not significantly changed after drug intake. The results suggest that the beta-blocking drug may cause qualitative changes in the composition of saliva by inhibiting the synthesis and/or release of acinar proteins.
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PMID:Effects of a beta-blocking agent, timolol maleate, on saliva in healthy volunteers. 245 Dec 71

In this study, a combination of the diaminobenzidine staining procedure for myeloperoxidase and the immunogold labeling technique was successfully used to show that lysozyme is indeed found in both the primary and secondary type granules of human neutrophils. Following the systematic selection of processing conditions by light microscopic peroxidase anti-peroxidase cytochemistry, on slide preparations, consistent gold labeling was obtained over both types of granules. The combination of myeloperoxidase and immunogold cytochemical procedures permitted the lysozyme-labeling pattern of the small-sized granules to be studied in isolation, thereby confirming the existence of lysozyme in secondary granules. In addition, myeloperoxidase was observed in the large-sized, lysozyme-positive, granules by both cytochemical and immunocytochemical methods, thereby confirming that these labeled structures were primary granules. Morphometrical analysis confirmed that there was a significant difference in mean size between the lysozyme-positive, myeloperoxidase-positive, granules and the lysozyme-positive, myeloperoxidase-negative, granules. The former were significantly larger in size than the latter. In conclusion, although the localization of lysozyme in human neutrophils by the immunogold technique is confirmatory, the combination of enzyme cytochemistry and immunocytochemistry is a novel technical approach that permits the lysozyme-labeling patterns of granule types to be studied in isolation. This double labeling technique is relatively straightforward and, as such, consistent immunostaining can be routinely obtained using intact cells.
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PMID:Combination of diaminobenzidine staining and immunogold labeling: a novel technical approach to identify lysozyme in human neutrophil cells. 247 12

The specificity of the basic bactericidal/permeability increasing protein (BPI) of polymorphonuclear leukocytes (PMN) for gram-negative bacteria is attributable to its strong attraction for the negatively charged envelope LPS. The antibacterial activity of PMN homogenates or extracts toward Escherichia coli corresponds to their BPI content and is blocked by anti-BPI IgG, suggesting that BPI action is unaffected by the presence of other PMN proteins. To test if BPI is preferentially bound to E. coli when other antibacterial proteins are present, we have measured binding in buffered (pH 7.5) balanced salts solution of [125I] human BPI to E. coli J5 in the presence and absence of other human PMN granule proteins. BPI binding is saturable with an apparent K = 23 nM and 2.2 million binding sites/cell. While binding of [125I] human BPI is competitively inhibited by human or rabbit BPI, it is only weakly inhibited by myeloperoxidase, lysozyme, or cathepsin G. In contrast, myeloperoxidase binding to E. coli is strongly inhibited by BPI. Moreover, incubation of E. coli with crude extracts of PMN or CML spleen results in near quantitative binding of BPI, identified by silver staining and immunoblotting after SDS-PAGE of the washed E. coli pellet, without recognizable binding of other leukocyte proteins (greater than 98% of added total protein is recovered in supernatant). After addition of 200 mM MgCl2, approximately 80% of bound BPI is released as fully active and pure protein (as judged by SDS-PAGE and HPLC). Thus the selective and reversible binding of BPI in crude PMN extracts to target bacteria provides a one-step "affinity" purification procedure.
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PMID:Preferential binding of the neutrophil cytoplasmic granule-derived bactericidal/permeability increasing protein to target bacteria. Implications and use as a means of purification. 253 11

In this study immuno-electron microscopy was used to assay, semi-quantitatively, the granule contents of elastase, lactoferrin, lysozyme and myeloperoxidase in human peripheral blood neutrophils from 13 chronic myeloid leukaemia patients in the chronic phase of the disease and from normal non-smoking donors. The fixation conditions that adequately preserved the antibody binding capacities of these antigens and reasonably preserved the ultrastructure of the neutrophils were selected by light-microscopic immunoperoxidase cytochemistry on cytospin smears. Immunogold cytochemistry on LR White resin sections localised elastase and myeloperoxidase to the primary granules, lactoferrin to the secondary granules and lysozyme to both types of granule. When applicable, peroxidase cytochemistry was combined with immunogold staining making it easier to distinguish the primary from the secondary granules. A comparison of the immunolabelling density values obtained for the leukaemic and normal states revealed no significant abnormalities in the immunoreactivity patterns for any of these neutrophil granule antigens in the leukaemic patients. All 13 patients gave normal immunostaining reactivities for these neutrophil granule proteins. Consequently the distribution patterns of these proteins, as shown in this study, cannot be used as indices in distinguishing chronic myeloid leukaemic neutrophils from normal neutrophils.
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PMID:Analysis of human neutrophil granule protein composition in chronic myeloid leukaemia by immuno-electron microscopy. 255 61

Blood neutrophils, when exposed to appropriate stimuli, aggregate, degranulate and generate superoxide anion. Curcumin, a non-steroidal antiinflammatory agent, modulated these functions, depending upon the kind of stimulus used. It inhibited monkey neutrophil aggregation induced by chemotactic peptide fmlp and zymosan activated plasma (ZAP) but did not affect that induced by serum treated zymosan (STZ) and arachidonic acid (AA). Generation of O2- radical was inhibited by curcumin, when cells were stimulated by AA, STZ and fmlp. Curcumin inhibited the release of myeloperoxidase, an azurophilic granule marker enzyme. Release of lysozyme was less susceptible to inhibition by curcumin. The results suggest that curcumin interferes with neutrophil responses to various physiological stimuli and a part of its antiinflammatory action is mediated via inhibition of neutrophil function. Inhibition of neutrophil function by curcumin appears to be mediated via calcium dependent mechanisms.
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PMID:Inhibition of neutrophil response by curcumin. 255 3

The heterogeneity in human neutrophil granules was examined by the ultrastructural localization of a series of antigens which have been previously identified with neutrophil granules by either physical separation or biochemical/biological techniques. All samples were prepared by cryofixation and molecular distillation drying (LifeCell Process), a two-step physical method that achieves cryofixation by metal mirror freezing and drying by the controlled, incremental heating of cryofixed samples in an ultrahigh vacuum. After drying, the samples were either exposed to vapor-phase osmium followed by embedment in Spurr resin, or they were exposed to formaldehyde vapor followed by embedment in Araldite resin. An indirect streptavidincolloidal gold procedure was used for immunoelectron microscopy on ultrathin sections. Subcellular ultrastructural morphology of neutrophils prepared by this method was good compared to standard electron microscopic techniques and superior compared to comparable, published electron microscopic cryomethods applied to neutrophils. Immunogold localization of myeloperoxidase, cathepsin G, lysozyme, lactoferrin, beta 2-microglobulin, and CD-15 antigens showed high intensity and specificity of labeling in the intracellular granules. Patterns of labeling varied from antigen to antigen, demonstrating granule heterogeneity both within and among neutrophils. This methodology is useful in the exploration and definition of granule heterogeneity and function.
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PMID:Human neutrophil granule heterogeneity: immunolocalization studies using cryofixed, dried and embedded specimens. 261 53

A 21-year-old man was admitted to our hospital because of anorexia and general malaise in July, 1988. On admission, the white blood cell count of 18,600/microliters with 72% leukemic cells. The bone marrow aspirate showed 76.8% immature monocytes, 10% mature and immature eosinophils. Leukemic cells were 66.6% myeloperoxidase positive cells, and 20.6% naphthylbutyrate esterase positive cells. The lysozyme activity in urine was high. Cytogenetic analysis revealed the presence of 46 XY inv (16) (p13 q22). Under the diagnosis of acute myelomonocytic leukemia with eosinophilia (M4Eo) associated with inv (16) (p13 q22), one course of DCMP induction therapy was performed. After complete remission, the bone marrow aspirate showed disappearance of inv (16) (p13 q22), and associated with decreased residual leukemic cells.
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PMID:[Acute myelomonocytic leukemia with inv (16) (p13 q22) disappeared abnormal karyotype during complete remission]. 262

Because early childhood is an important period for the colonization of bacteria in the primary dentition, it is possible that antimicrobial factors in saliva may modify these early events. In this study we have followed longitudinally 33 children from predentate to dentate phase and analyzed whole saliva for such salivary factors as lysozyme, lactoferrin, salivary peroxidase, myeloperoxidase, thiocyanate, hypothiocyanite, total IgA, IgG, IgM, and total protein. Children's saliva samples were compared with those from an adult reference group whose samples were collected and analyzed in an identical way. It was observed that salivary thiocyanate and IgG increased and salivary peroxidase decreased significantly from predentate to dentate phase. The other parameters remained unchanged. Children in predentate phase already had reached adult levels of hypothiocyanite and IgM, whereas all the other components were found in significantly lower amounts in children's saliva than in adult saliva. Salivary myeloperoxidase assay is interfered by the thiocyanate ions, and the observed increase in salivary "myeloperoxidase" activity may be due to the simultaneous increase in salivary thiocyanate.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Antimicrobial factors in whole saliva of human infants: a longitudinal study. 262 37

Sphingoid long-chain bases (sphinganine and sphingosine) have recently been shown to inhibit protein kinase C both in vitro [Y. Hannun et al. (1986) J. Biol. Chem. 261, 12604-12609] and in intact human neutrophils, in which they block activation of the superoxide-generating respiratory burst [E. Wilson et al. (1986) J. Biol. Chem. 261, 12616-12623]. In the present study we have used sphingosine to investigate the pathways for agonist-induced secretion of neutrophil granule contents. Induction of secretion of the specific granule component lactoferrin by a variety of agonists [phorbol 12-myristate-13-acetate (PMA), formyl-methionyl-leucyl-phenylalanine (fMLP), and calcium ionophore A23187] was completely inhibited by sphingosine with an ED50 of 6 to 10 microM. PMA-induced secretion of lysozyme (present in both the azurophilic and specific granules) was completely blocked with an ED50 of 10 microM, whereas fMLP-induced secretion was only about 50% inhibited. Secretion of the azurophilic granule proteins beta-glucuronidase and myeloperoxidase was activated by fMLP and A23187, but not by PMA, and was not affected by sphingosine. The use of A23187 in the presence of sphingosine allowed differentiation between calcium activation of protein kinase C-dependent versus-independent pathways. The effect of sphingosine was not mediated by neutralizing intracellular acidic compartments, since treatment of neutrophils with inhibitory concentrations of sphingosine did not significantly alter the uptake of labeled methylamine. We conclude that at least two mechanisms participate in the regulation of specific and azurophilic granule secretion, respectively: a protein kinase C-dependent pathway and a calcium-dependent pathway which does not involve protein kinase C.
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PMID:Protein kinase C inhibition by sphingoid long-chain bases: effects on secretion in human neutrophils. 282 97

Neutrophil-mediated antibody-dependent cellular cytotoxicity (ADCC) against Raji target cells and neutrophil degranulation during the ADCC process were evaluated in the presence and in the absence of different agents able to interfere with the neutrophil release of granule components (anion channel blockers, colchicine, isoproterenol, dimethylxanthine, cAMP). When used at concentrations incapable of preventing the target cell recognition by neutrophils, the majority of these agents inhibited both the ADCC and the release of myeloperoxidase (MPO, primary granule marker) and lysozyme (LZM, primary and secondary granule marker). The inhibition of the ADCC correlated strictly with the inhibition of the MPO release. Thus, the results are consistent with the hypothesis that neutrophil primary granules play a major role in the cytolytic process.
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PMID:Relationship between antibody-dependent tumour cell lysis and primary granule exocytosis by human neutrophils. 282 22


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