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)

Glucan is a potent reticuloendothelial stimulant whose immunobiological activity is mediated, in part, by an increase in the number and function of macrophages. In studying the role of glucan as a mediator of antibacterial activity, we attempted to ascertain the ability of glucan to modify the mortality of mice with experimentally induced Gram-positive bacteremia, and to enhance antibacterial defenses in rats as denoted by serum lysozyme and phagocytic activity. After intravenous administration of glucan, serum lysozyme concentrations were increased approximately sevenfold over control concentrations. The increase in serum lysozyme appeared to parallel the glucan-induced increase in phagocytosis and induced hyperplasia of macrophages. Prior treatment of mice with glucan significantly enhanced their survival when they were challenged systemically with Staphylococcus aureus. These studies indicate that glucan confers an enhanced state of host defense against bacterial infections.
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PMID:Increased resistance to Staphylococcus aureus infection and enhancement in serum lysozyme activity by glucan. 62 41

Site-directed mutagenesis experiments designed to identify the active site of Bacillus licheniformis endo-beta-1,3-1,4-D-glucan 4-glucanohydrolase (beta-glucanase) have been performed. Putative catalytic residues were chosen on the basis of sequence similarity analysis to viral and eukaryotic lysozymes. Four mutant enzymes were expressed and purified from recombinant E. coli and their kinetics analysed with barley beta-glucan. Replacement of Glu134 by Gln produced a mutant (E134Q) that retains less than 0.3% of the wild-type activity. The other mutants, D133N, E160Q and D179N, are active but show different kinetic parameters relative to wild-type indicative of their participation in substrate binding and transition-state complex stabilization. Glu134 is essential for activity; it is comprised in a region of high sequence similarity to the active site of T4 lysozyme and matches the position of the general acid catalyst. These results strongly support a lysozyme-like mechanism for this family of Bacillus beta-glucan hydrolases with Glu134 being the essential acid catalyst.
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PMID:Essential catalytic role of Glu134 in endo-beta-1,3-1,4-D-glucan 4-glucanohydrolase from B. licheniformis as determined by site-directed mutagenesis. 135 72

A series of experiments was conducted to examine the effect of glucan on the reticuloendothelial system (RES) and on the development of 90Sr-induced osteosarcomas and malignant lymphomas in CBA/S mice. Glucan demonstrated a strong RES-stimulating effect, as evidenced by a dose-related increase in lysozyme levels in the plasma and an enlargement of the liver and spleen. Weekly injections of glucan between 150 and 250 days after exposure to 90Sr suppressed the actuarial appearance of the fibroblastic type of osteosarcomas and stimulated the emergence of malignant lymphomas. Glucan itself had no tumorigenic effect in mice not exposed to 90Sr.
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PMID:Effects of glucan on the reticuloendothelial system and on the development of tumors in 90Sr-exposed mice. 163 83

The effects of pentoxifylline (Trental) on human neutrophil CR3 up-modulation, degranulation, and superoxide production were studied. We used the chemotactic peptide fMLP and the phorbol ester PMA as soluble stimuli, and beta-glucan particles as a CR3-specific solid phase stimulus of neutrophil superoxide production. Since neutrophils have adenosine A2 receptors, we compared effects of pentoxifylline to effects of adenosine, and we also looked at the effect of cytochalasin B, which breaks up actin filaments. Pentoxifylline inhibited both CR3 up-modulation and degranulation of myeloperoxidase and lysozyme. Pentoxifylline is a more potent inhibitor of fMLP- compared to PMA-induced degranulation, and is especially potent against superoxide production. While pentoxifylline is less potent than adenosine in its inhibition of fMLP-induced superoxide production, it is more potent in its inhibition of PMA- and beta-glucan particle-stimulated superoxide production. Cytochalasin B, which enhances degranulation and fMLP-stimulated superoxide production, was found to inhibit beta-glucan particle-stimulated superoxide production. These findings are consistent with the hypothesis that pentoxifylline can affect both the cytoskeletal architecture of unstimulated neutrophils and the activation and responses of neutrophils which involve actin polymerization and receptor-cytoskeletal interactions.
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PMID:Stimulus-specific effects of pentoxifylline on neutrophil CR3 expression, degranulation, and superoxide production. 215 76

The cel-3 gene cloned from Fibrobacter succinogenes into Escherichia coli coded for the enzyme EG3, which exhibited both endoglucanase and cellobiosidase activities. The gene had an open reading frame of 1,974 base pairs, coding for a protein of 73.4 kilodaltons (kDa). However, the enzyme purified from the osmotic shock fluid of E. coli was 43 kDa. The amino terminus of the 43-kDa protein matched amino acid residue 266 of the protein coded for by the open reading frame, indicating proteolysis in E. coli. In addition to the 43-kDa protein, Western immunoblotting revealed a 94-kDa membranous form of the enzyme in E. coli and a single protein of 118 kDa in F. succinogenes. Thus, the purified protein appears to be a proteolytic degradation product of a native protein which was 94 kDa in E. coli and 118 kDa in F. succinogenes. The discrepancy between the molecular weight expected on the basis of the DNA sequence and the in vivo form may be due to anomalous migration during electrophoresis, to glycosylation of the native enzyme, or to fatty acyl substitution at the N terminus. One of two putative signal peptide cleavage sites bore a strong resemblance to known lipoprotein leader sequences. The purified 43-kDa peptide exhibited a high Km (53 mg/ml) for carboxymethyl cellulose but a low Km (3 to 4 mg/ml) for lichenan and barley beta-glucan. The enzyme hydrolyzed amorphous cellulose, and cellobiose and cellotriose were the major products of hydrolysis. Cellotriose, but not cellobiose, was cleaved by the enzyme. EG3 exhibited significant amino acid sequence homology with endoglucanase CelC from Clostridium thermocellum, and as with both CelA and CelC of C. thermocellum, it had a putative active site which could be aligned with the active site of hen egg white lysozyme at the highly conserved amino acid residues Asn-44 and Asp-52.
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PMID:Structure of the cel-3 gene from Fibrobacter succinogenes S85 and characteristics of the encoded gene product, endoglucanase 3. 267 79

High-molecular-weight polymers of alpha-1,6-linked D-glucans are insoluble in alcohol solutions. Whole, but not parotid, saliva prevented the precipitation of D-glucans by 80% (vol/vol) ethanol, showing that the whole saliva contained a factor which complexed with the glucan to render it alcohol soluble. The glucan-binding factor was retained on a column of Sephacryl S-200 which had been preequilibrated with 80% ethanol. The factor was then eluted with water. Passive hemagglutination assays revealed that the glucan-binding factor could sensitize erythrocytes to agglutination with anti-poly(glycerolphosphate), suggesting that the active glucan-binding component with lipoteichoic acid. The glucan-solubilizing factor was resistant to heat (100 degrees C), proteases, sialidase, lysozyme, lactoperoxidase, trichloroacetic acid, and Triton X-100. When sucrose was added to saliva, a suspension of Streptococcus cricetus AHT, or a suspension of Streptococcus sanguis 10556, relatively large amounts of glucan-binding factor were released in a soluble form. In addition, penicillin G caused the release of the glucan-solubilizing component from a suspension of S. cricetus AHT. It is suggested that whole saliva contains a component, tentatively identified as lipoteichoic acid, which can complex with glucans in a relatively hydrophobic solvent. This type of complex formation may be important in the adhesion of oral streptococci to saliva-coated surfaces.
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PMID:Glucan-binding factor in saliva. 316 92

Glucan, an immunostimulant, was evaluated for its ability to modify a staphylococcal mammary challenge in ewes. Glucan was administered subcutaneously to ewes prior to lactation or during lactation, and all ewes, including a control group, were subsequently challenged intramammarily with Staphylococcus haemolyticus 40 days after the mean lambing date. The glucan treatment was shown to modify the staphylococcal mammary infection as the milk bacterial counts from all of the glucan-treated groups were significantly reduced compared to controls. For the glucan-treated groups, the highest mean somatic cell counts were recorded 1 day post-challenge, while for the control group, the mean cell count rose more gradually to peak by 3 days post-challenge. Glucan did not increase serum lysozyme levels or blood neutrophil bactericidal activity. However, there was a negative correlation between the bactericidal activity of blood neutrophils collected from the glucan-treated ewes prior to challenge and their mean milk bacterial counts post-challenge. Glucan was observed to stimulate ovine mammary macrophages in vitro, while the addition of zymosan or opsonised killed Staphylococcus aureus to macrophage cultures had no effect. These studies indicate that, in sheep, glucan can enhance some elements of the immune system against staphylococcal infections.
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PMID:Protective effect of glucan against experimentally induced staphylococcal mastitis in ewes. 335 93

Lavaged and in situ rat alveolar macrophages were compared with respect to lysozyme content and size in order to assess the extent to which macrophages from pulmonary lavages reflect the in situ cell population. This relationship was studied in normal rats and in rats with pulmonary granulomas induced by glucan stimulation (10 mg/kg given intravenously on Days 5, 3, and 1 before being killed). Alveolar macrophages in pulmonary lavages and histologic sections were stained for lysozyme by the immunoperoxidase method using rabbit antiserum to rat lysozyme. Enzyme content and cell size were measured with a conventional scanning cytospectrophotometer and an automated image analysis system (LEYTAS). Scanning cytospectrophotometry measurements showed that 26% of in situ alveolar macrophages from glucan-treated rats contained more lysozyme than did control cells and that 31% possessed larger areas. Fewer large alveolar macrophages containing increased amounts of lysozyme were detected in lavages of glucan-treated rats. Frequency histograms of lysozyme content and cell size were similar for lavaged and in situ macrophages from control rats. Measurements with LEYTAS confirmed the results. These experiments demonstrate that alveolar macrophages obtained by lavage are representative of their in situ counterparts in normal but not in glucan-treated rats.
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PMID:Comparison of lavaged and intrapulmonary alveolar macrophages in respect to lysozyme content and size in the rat. 670 73

Following the administration of Di Luzio particulate glucan, Corynebacterium parvum, pyran (maleic anhydride vinyl ether 6), and lipopolysaccharide (Shigella) to inbred C57BL/6J mice, dose, route, and time-dependent studies were undertaken on antitumor activity and serum lysozyme levels to explore the possible relevance of serum lysozyme as a useful index of antitumor activity. Antitumor activity was assessed by measurement of the extent of loss of iv injected 125I-labeled 5-iodo-2'-deoxyuridine-labeled B16 tumor cells. Increases in serum lysozyme levels were dose-, route-, and time-dependent and varied greatly from one agent to another. The peak levels of antitumor activity were similar for all agents but were also critically dose- and time-dependent. Correlations of serum lysozyme levels and antitumor activity were inexact. The doses for peak lysozyme level increases were higher than those for peak antitumor activity. Antitumor activity peaked earlier and lasted longer than serum lysozyme level increases.
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PMID:Dose, route, and time dependence of serum lysozyme and antitumor activity following administration of glucan, Corynebacterium parvum, pyran, or lipopolysaccharide to mice. 694 57

A prepared polysaccharide from the cell wall of yeast, M-Glucan, has previously been demonstrated to have immunostimulatory effects in salmonids as observed by enhanced in vivo non-specific disease resistance in Atlantic salmon, Salmo salar L., and increased in vitro bactericidal activity of rainbow trout, Oncorhynchus mykiss (Walbaum), macrophages. In the present study M-Glucan was injected intraperitoneally into Atlantic salmon and the effect on core components in the non-specific part of the immune system was observed. The hydrogen peroxide (H2O2) production of isolated head kidney macrophages from glucan-injected fish was measured 3 and 6 weeks after M-Glucan treatment and was increased at both time-points upon phorbol myristate acetate-(PMA) triggering. Without PMA triggering the difference was only significant 3 weeks after glucan injection when compared to a control group injected with saline. In a phagocytic assay with macrophages and Vibrio salmonicida the initial uptake of bacteria was elevated at both 3 and 6 weeks after glucan treatment. There was no significant difference when uptake of another fish pathogenic bacteria, Renibacterium salmoninarum, was studied. Treatment of Atlantic salmon with M-Glucan also resulted in enhanced serum lysozyme activity in week 3 of the experimental period. The results indicate that M-Glucan elevates the activity of the non-specific part of the immune system and the use of M-Glucan as an immunostimulant is discussed.
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PMID:Effect of injected yeast glucan on the activity of macrophages in Atlantic salmon, Salmo salar L., as evaluated by in vitro hydrogen peroxide production and phagocytic capacity. 783 49


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