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 degranulation and release of lysosomal (myeloperoxidase, beta-glucuronidase, lysozyme) and cytoplasmic (lactate dehydrogenase-LDH) enzymes from polymorphonuclear neutrophil granulocytes (PMG) during phagocytosis of inert latex particles or bacteria were studied. Degranulation was much faster and more pronounced by phagocytosis of bacteria than of inert particles. A high frequency of lysosome-lysosome as well as lysosome-phagosome fusions suggested that granular material was transported by lysosome- lysosome- phagosome fusions. During bacterial phagocytosis there was evidence of release of granular material into cytoplasm causing enzymatic disintegration. After 60 minutes cell lysis occurred in about 5 per cent of the cells during bacterial phagocytosis. There was non-specific release of LDH during phagocytosis of inert particles, probably due to erythro-phagocytosis. After 60 minutes the release during bacterial phagocytosis amounted to 20-30 per cent of the enzyme content of the cells. A nearly equal release of lysosomal and cytoplasmic enzymes gave support for the idea that cell lysis was the main mechanism of enzyme release.
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PMID:Degranulation and enzyme release during phagocytosis of inert particles and of bacteria by polymorphonuclear neutrophil granulocytes. 632 36

When exposed to zymosan or latex particles or heat-inactivated staphylococci, freshly prepared human blood monocytes and granulocytes rapidly released a large fraction of their lysozyme content. Within 24 hours the total lysozyme activity in the monocyte suspensions tripled, while it doubled in the granulocyte suspensions, indicating synthesis of the enzyme following release. The monocytes in particular seemed to release and synthesize lysozyme without any other stimulus than contact with lymphocytes and the tube walls. Potassium caseinate in solution did not influence the lysozyme release. Myeloperoxidase and beta-glucuronidase, which in the granulocytes are kept in lysosomal fractions separate from most of the lysozyme, were neither released nor synthesized to a significant degree. Moreover, the minute amount of lactate dehydrogenase released indicated that the lysozyme release was not the result of cell lysis. Accordingly, the monocytes, which are not already stimulated by adherence to nonphagocytosable surfaces, are capable of selective enzyme release similar to that of the granulocytes.
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PMID:In vitro release of lysozyme from monocytes and granulocytes. 632 67

The peritoneal macrophages of mice treated with lysozyme were studied by cytochemical assay. In single and repeated doses of 0.5-5 mg/kg lysozyme induced an increase in macrophage metabolism. This was evident from an increased activity of succinate dehydrogenase, NADP X N-DH and the enzymes catalyzing glycolysis typical of these cells (lactate dehydrogenase and alpha-glycerophosphate). The changes in the activity of the enzymatic systems were most pronounced in minute and less mature macrophages after repeated administrations of the drugs. In a dose of 50 mg/kg lysozyme somewhat decreased the activity of a number of the enzymes. In the doses optimal for the macrophage activity lysozyme had a low effect on the infection resistance and slightly increased the cephotaxim efficiency in experimental staphylococcal infection. This may be mainly due to the immunomodulating effect of lysozyme and its low effect on the large macrophages having the bactericidal effect.
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PMID:[Experimental effect of lysozyme on macrophage metabolism and resistance to infection]. 633 Dec 92

Immunochemical techniques with enzymes as the antigen have grown in frequency during the last few years. These techniques have allowed evaluation of enzymes in the presence of endogenous inhibitors. Among those enzymes measured by immunochemical techniques and which have found diagnostic application, mention will be made of alkaline phosphatase (with particular reference to the intestinal, placental, and Regan isoenzymes), lactate dehydrogenase (in which renewed interest has developed due to techniques for specifically measuring the LD-1 isoenzyme), aspartate aminotransferase (of which the cytosolic and mitochondrial forms can now be independently measured by immunochemical techniques), acid phosphatase (for which a specific immunochemical assay for the prostatic enzyme has been widely introduced in diagnostic laboratories), and creatine kinase (for which a variety of immunochemical techniques to measure the M- and B-subunits are now part of standard laboratory assays). Other enzymes which will be discussed in this review include phosphohexose isomerase, amylase, ribonuclease, and lysozyme (muramidase). Finally, the use of enzymes, particularly asparaginase, in the chemotherapy of cancer will be outlined.
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PMID:Immunoassay of enzymes--an overview. 634 26

Prior to administration, leukocyte transfusions are commonly irradiated with up to 5,000 R to eliminate lymphocytes and thereby prevent graft-versus-host disease in the recipient. It has been widely believed that phagocytes are resistant to this irradiation. In a recent report, we noted that phagocyte oxidative metabolism was compromised during preparation of white cells for transfusion. As part of our effort to examine the basis for this inhibition of phagocyte function during white cell preparation, we assessed the effects of irradiation on the long-lived monocytes that have been shown to persist at inflammatory foci posttransfusion. Human monocytes were irradiated for up to 3 min, receiving 2,500-5,000 R. This irradiation damaged human monocytes, significantly decreasing their in vitro survival for the first 3 wk of culture (p less than 0.02, irradiated versus control survival), and growth as assessed by two-dimensional cell size measurements during the first 2 wk of culture (p less than 0.01, irradiated versus control growth). Despite smaller cell size, total cell protein was significantly increased over time in irradiated cultures (p less than 0.001, irradiated versus control total protein per cell). Extracellular release of lysozyme and beta-glucuronidase per cell was not affected by irradiation, but extracellular lactate dehydrogenase (LDH) release was significantly increased after irradiation (p less than 0.001, irradiated versus control LDH release). Irradiated monocytes killed Listeria monocytogenes at a slower rate than the nonirradiated controls (p less than 0.05, irradiated versus control rate of killing). Thus, the data indicate that irradiation in doses used to prevent graft-versus-host disease in leukocyte transfusion recipients has a deleterious effect on in vitro human monocyte survival and function.
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PMID:Radiation effects on cultured human monocytes and on monocyte-derived macrophages. 642 52

The influence of taurine on neutrophil phagocytic and bactericidal capacities and lysosomal enzyme-releasing ability was evaluated in the present study using neutrophils obtained from casein-elicited rat peritoneal exudates. Taurine was dissolved in drinking water at a concentration of 0.3%, and the solution was given to rats for 1-21 days (460 mg/kg/day). Taurine concentration in the serum increased with the term of its administration, while in the neutrophils, it increased significantly after administration for 1 or 3 days. When administered for 7 or 10 days, however, no difference was noted from the control group, but then the concentration remarkably increased after 21 days of administration. The bactericidal capacity of the neutrophils against Escherichia coli was strengthened as their concentration of taurine increased; phagocytic capacity was also strengthened. The release of myeloperoxidase following phagocytosis of yeasts increased with administration, while the release of beta-glucuronidase, lysozyme and lactate dehydrogenase, which are induced by N-formylmethionyl-leucyl-phenylalanine, were inhibited. The hypotonic hemolysis of erythrocytes was also inhibited. Taurine decreased the fluorescence depolarization of diphenylhexatriene, indicating an increase in membrane fluidity. These results suggested that taurine strengthens both phagocytic and bactericidal capacities of neutrophils by increasing the fluidity of neutrophil membrane and membrane stability and thus plays an important role in the mechanism of host defense.
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PMID:[Role of taurine in neutrophil function]. 650 Apr 3

The present study was designed to find useful markers for detection of renal damage due to gentamicin (GM). Following the administration of 80 mg/kg GM, there were significant increases in urinary protein contents and alkaline phosphatase, N-acetyl-beta-glucosaminidase, lactate dehydrogenase, gamma-glutamyl transpeptidase and lysozyme activities. Alterations of these parameters had a peak at the 7th or 10th day and values restored to near normal levels by the 15th day. Light microscopic observations of the kidney on the 10th day showed mainly the necrosis of proximal tubular epithelial cells in the renal outer cortex, and there was regeneration of epithelial cells on the 15th day. In addition, when 1 mg/kg HgCl2 was given to rats, there were increases in urinary enzyme activities and protein contents, and BUN. The kidney of rats that received HgCl2 showed the necrosis of tubular epithelial cells in the renal inner cortex. It is considered from these results that determination of the activities of various urinary enzymes may be useful markers to detect tubular damage induced by GM.
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PMID:[Studies on the nephrotoxicity of aminoglycoside antibiotics and protection from these effects. (1). Nephrotoxicity of gentamicin and mercuric chloride]. 651 81

Effects of gentamicin (GM) alone and in combination with latamoxef (LMOX), an oxacefem antibiotic, were studied in rat kidney in order to determine the effect of combinations of nephrotoxic drugs. Groups of 7 male Sprague-Dawley rats, weighing approx. 230 g, were given daily s.c. doses of GM (80 mg/kg) or 80 mg/kg GM plus LMOX (500, 1000 or 2000 mg/kg) for 15 days. Treatment with GM alone resulted in marked increases in urinary lactate dehydrogenase, N-acetyl-beta-glucosaminidase and lysozyme activities, urinary protein contents and blood urea nitrogen contents, which peaked on the 10th day. The combination of GM plus LMOX significantly suppressed the increases in these biochemical parameters with GM alone. In this case, the suppressions were roughly dependent on the dose of LMOX. Although GM alone caused pronounced histological changes in proximal tubules between the 7th and 15th days, the combination with LMOX apparently protected against these changes. These results indicate that the combination with LMOX obviously protects the kidney from the nephrotoxicity of GM.
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PMID:[Studies on the nephrotoxicity of aminoglycoside antibiotics and protection from these effects. (2). Protective effect of latamoxef against gentamicin nephrotoxicity]. 651 82

Plasma and intracellular levels of lactate dehydrogenase (LDH), phosphohexose isomerase (PHI) and lysozyme activities were investigated in 20 patients with acute myelocytic leukemia (AML), 18 patients with acute lymphatic leukemia (ALL) and 10 patients with chronic myelocytic leukemia in blast transformation (CML/BT). Though the plasma levels of LDH and PHI in all patients with acute leukemia were elevated as compared to control persons there was no distinctive pattern which could be of use in the classification of acute leukemia. On the other hand the intracellular levels of these enzymes could be of value in classifying acute leukemia. The leukemic lymphoblasts were characterized by low levels of PHI and lysozyme as compared to leukemic myeloblasts or to normal lymphocytes (p less than 0.01). The LDH/PHI ratio is also significantly higher in leukemic lymphoblasts than in leukemic myeloblasts or in normal lymphocytes (p always less than 0.01). These characteristics might also be made use of in identifying the blasts of CML/BT als "lymphoid" or "myeloid" in corresponding cases.
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PMID:Plasma and intracellular levels of lactate dehydrogenase, phosphohexose isomerase and lysozyme activity in acute leukemia. 658 21

Human tear fluid has plasminogen activator activity. The type of plasminogen activator activity in unstimulated and stimulated tears was determined, using antibodies that specifically neutralize tissue plasminogen activator or urokinase. All plasminogen activator activity was tissue plasminogen activator-related in both types of tears. Correlations between activities of beta-hexosaminidase, lysozyme and lactate dehydrogenase with tissue plasminogen activator activity indicate that the contribution to plasminogen activator activity of conjunctival and corneal epithelium is more important in unstimulated tears than stimulated tears. In stimulated tears the tissue plasminogen activator activity originates mainly from the lacrimal gland. It is suggested that a constant concentration of plasminogen activator is released from the lacrimal gland and that this concentration is independent of the secretion rate of tear fluid and that the release from the conjunctiva is due to desquamation of cells.
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PMID:Immunological characterization and possible origin of plasminogen activator in human tear fluid. 668 45


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