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)

A series of biochemical and morphological studies has focused on the properties and origins of lipid laden foam cells in experimentally induced atherosclerosis in rabbits. Lipids inclusions present in these cells occupy half or more of the cytoplasmic volume and are of two kinds: cytoplasmic lipid droplets composed predominantly of cholesteryl esters and lysosomes in which substantial quantities of free cholesterol have accumulated. The foam cells exhibit some properties of macrophages but not others. They possess high levels of acid hydrolases and catalase and Fc membrane receptors can be detected on their surface. Only about one third of the foam cells, however, exhibit C3 receptors and few if any of the cells appear to contain or secrete lysozyme.
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PMID:Characterization of foam cells in experimental atherosclerosis. 693 40

The alveolar macrophage belongs to the "Mononuclear Phagocytic System". The medullary promonocyte is its stem-cell. It has a kidneyshaped nucleus, a developed vesicular Golgi apparatus, numerous mitochondriae, lysosomes, phagosomes, and a rough or smooth ergastoplasm. It can survive several weeks in vitro, when cultivated on a porous membrane in contact with a nutrient medium and incubated in a gaseous phase (5 per cent carbon dioxide in water saturated air). Mitotic activity is questionable. Oxygen consumption is high during endocytosis. Metabolic energy is derived from direct oxidative glucose breakdown. Its anti-infectious property is based on phagocytosis as well as on cytoplasmic germicidal or lytic systems (hydrogen peroxide, catalase, free oxygen radicals, hydrogen ion, lysozyme and other lysosomial hydrolases). This function is stimulated by T lymphocyte and by endocytosis of digestible material. In vitro, the alveolar macrophage is capable of inhibiting intra-cellular development of Candida albicans, Klebsiella pneumoniae, Listeria monocytogenes, Staphlylococcus albus and Staphylococcus aureus.
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PMID:[The alveolar macrophage and its anti-infectious function (author's transl)]. 700 32

Incorporation of [3H]thymidine ([3H]TdR) into tonsil lymphocytes was inhibited by native Staphylococcus epidermidis while Staphylococcus aureus Cowan I caused stimulation. The inhibitory effect of S. epidermidis was abolished by formalin treatment but not by heat killing. A toxic agent was released from S. epidermidis on gentle water extraction without lysing the bacteria. The extract contained protein and other UV-absorbing material, but did not exhibit haemolytic, lysozyme, catalase or protease activity. The heat-resistant, formalin-sensitive inhibitor present in the aqueous extract of S. epidermidis inhibited [3H]TdR incorporation of lymphocytes in a dose-dependent manner and decreased the viability of lymphocytes.
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PMID:Cytotoxic material released from Staphylococcus epidermidis. I. Effects on [3H]thymidine incorporation of human lymphocytes. 709 Aug 57

Each of 11 tumors tested produced a factor that markedly suppressed the ability of macrophages to release H2O2 or O.2- in response to phorbol myristate acetate or zymosan. Four of seven normal cell types produced a similar activity, which was 3.5-7 times lower in titer than that in tumor cell-conditioned medium (TCM), and which was much more rapidly reversible in its effects. TCM caused 50% inhibition of H2O2 release when it was present in the medium for 48 h at a concentration of 13%, or when 100% TCM was present in the medium for 18 h. The H2O2-releasing capacity of macrophages incubated in TCM only returned to control levels by 6 d after its removal. TCM prevented augmentation of H2O2-releasing capacity by lymphokines. The titer of suppressive activity in TCM depended on both the concentration of tumor cells and the duration of their incubation. TCM did not augment the activity of catalase, myeloperoxidase, glutathione peroxidase, or glutathione reductase or the content of glutathione within macrophages, suggesting that decreased synthesis rather than increased catabolism was responsible for reduced secretion of H2O2. Suppression of the release of H2O2 or O.2- by TCM appeared to be a relatively specific effect, in that TCM increased macrophage spreading and adherence to glass while exerting little influence on rates of phagocytosis, synthesis of protein, or secretion of lysozyme, plasminogen activator, or arachidonic acid and its metabolites. Thus, tumor cells and some normal cells can secrete a factor that selectively deactivates macrophage oxidative metabolism.
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PMID:Suppression of macrophage oxidative metabolism by products of malignant and nonmalignant cells. 715 14

During phagocytosis, neutrophils generate reactive oxygen metabolites and release lysosomal enzymes into the extracellular medium. We have investigated the possibility that these enzyme are inactivated by the oxygen compounds. Phagocytosing neutrophils from 12 patients with chronic granulomatous disease, which do not generate these oxygen metabolites, released two to three times more activity of lysozyme and beta-glucuronidase than did normal neutrophils. This difference proved to be due to a decrease of approximately 20% of the total activity of these enzymes in normal neutrophils, but not in neutrophils of patients with chronic granulomatous disease. This inactivation of enzymes took place during phagocytosis of opsonized zymosan particles as well as during stimulation of normal cells with phorbol myristate acetate. The inactivation was not due to formation of inhibitors. The lysosomal enzymes were not activated when the neutrophils were stimulated under anaerobic conditions. Addition of catalase, superoxide dismutase, or albumin gave no protection against the oxidative damage; reduced glutathione gave partial protection. The oxidative inactivation was more pronounced in the presence of azide. Measurement of the activity and the amount of protein of acid alpha-glucosidase in the cells showed that the specific activity of this enzyme decreased by approximately 50% during 30 min of phagocytosis. This indicates that the inactivation of the lysosomal enzymes takes place in the phagolysosomes, before the enzymes have leaked into the extracellular medium.
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PMID:Phagocytosing human neutrophils inactivate their own granular enzymes. 722 38

A total of 57 gram-positive, catalase-positive cocci, considered etiological agents of clinical and subclinical bovine mastitis, were tested for glucose and mannitol fermentation, coagulase and thermonuclease production, sensitivity to lysostaphin, gelatin hydrolysis, lysozyme, phosphatase and egg yolk factor production, hemolytic properties, antibiotic sensitivity, susceptibility to human and bovine phages, and enterotoxin production. All 57 strains were identified as staphylococci. A good correlation was found between 3+ and 4+ coagulase reactions, thermonuclease production, and high sensitivity to lysostaphin. Neither mannitol fermentation nor production of other enzymes appeared to be a specific property of bovine Staphylococcus aureus strains. beta- and delta-hemolysins were more frequently found than alpha-hemolysin. Nearly 40% of the strains were penicillin resistant. Strains were lysed by phage 42E from the human phage set more frequently than by phage 42D, whereas with the bovine set, strains were more sensitive to specific bovine phages. Three strains produced enterotoxin C, and one strain produced enterotoxin D.
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PMID:Characterization of staphylococci isolated from mastitic cows in Spain. 738 55

The water-insoluble proteins from aged human lens are known to contain protein-bound chromophores that act as UVA senisitizers. The irradiation of a sonication-solubilized, water-insoluble fraction from human lenses (55-75 years) with UVA light (1.5 kJ/cm2, gamma > 338nm) caused an oxygen-dependent photolysis of tryptophan, not seen when either alpha-crystallin or lysozyme were irradiated. The suggested requirement for active oxygen species was consistent with a linear increase in hydrogen peroxide formation, which was also observed. A final concentration of 55 microM H2O2 was attained, with no H2O2 being detected in either dark-incubated controls or in irradiated samples of native proteins. The UVA-dependent H2O2 formation was increased 50% by superoxide dismutase (SOD) and abolished by catalase, arguing for the initial generation of superoxide anion. A linear photolysis of histidine and tryptophan was also seen; however, the addition of SOD or SOD and catalase had no effect on the photolytic destruction of either amino acid. Superoxide dismutase increased the oxidation of protein SH groups implicating H2O2, but SOD and catalase caused a decrease in SH oxidation only at later time periods. The direct addition of H2O2 to a water-insoluble sonicate supernatant fraction caused only a slight oxidation of SH groups, but this was increased four- to eight-fold when the protein was denatured in 4.0 M guanidine hydrochloride. Overall, the data suggest a UVA-dependent oxidation of protein SH groups via H2O2 generated within the large protein aggregates of the water-insoluble fraction. These data also provide a mechanism for oxidation of the sulfur-containing amino acids in vivo--a process that is known to accompany the formation of age-onset cataracts.
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PMID:The generation of hydrogen peroxide by the UVA irradiation of human lens proteins. 763 74

Several bacteriocin-producing Leuconostoc strains have been isolated from meat and identified as Leuconostoc gelidum UAL 187, Leuconostoc paramesenteroides-La7a, Leuconostoc carnosum-Ta11a and Leuconostoc carnosum-La54a. All strains produce bacteriocins that are active against Listeria monocytogenes and other lactic acid bacteria of concern in meat spoilage. All of the bacteriocins studied are heat stable in acidic environments and are inactivated by a range of proteolytic enzymes but not by catalase or lysozyme. Most are detected early in the growth cycle and are produced at refrigeration temperatures and in a pH range of 4.0-7.0. Leucocin A-UAL187, produced by Leuconostoc gelidium UAL 187, is a small peptide (MW 3930) translated as a 61 amino acid prepeptide consisting of a 24 amino acid leader region and 37 amino acid active bacteriocin that is secreted. A probe designed from a region of the leucocin gene has been used to locate the bacteriocin genes in the other strains (La7a, La54a and Ta11a). Strong hybridization signals were detected from 8.9 MDa, 32 MDa and 8.9 MDa plasmids in strains La7a, La54a and Ta11a, respectively. The bacteriocin structural gene from Leuconostoc carnosum-Ta11a (leucocin B-Ta11a) has been cloned and sequenced and the bacteriocin shows 100% homology to leucocin A-UAL187; however, the prepeptide differs in six residues. The mature extracellular bacteriocin from strain UAL 187 was purified and characterized by precipitation, gel filtration, hydrophobic interaction chromatography followed by RP-HPLC and amino-terminal sequencing, whilst those of the other strains are in the process of being purified and characterized using similar techniques.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Bacteriocins of leuconostocs isolated from meat. 770 31

Leuconostoc (Lc.) carnosum Ta11a, isolated from vacuum-packaged processed meats, produced a bacteriocin designated leucocin B-Ta11a. The crude bacteriocin was heat stable and sensitive to proteolytic enzymes, but not to catalase, lysozyme, or chloroform. It was active against Listeria monocytogenes and several lactic acid bacteria. Leucocin B-Ta11a was optimally produced at 25 degrees C in MRS broth at an initial pH of 6.0 or 6.5. An 8.9-MDa plasmid in Leuconostoc carnosum Ta11a hybridized to a 36-mer oligonucleotide probe (JF-1) that was homologous to leucocin A-UAL187. A 4.9-kb Sau3A fragment from a partial digest of the 8.9-MDa plasmid was cloned into pUC118. The 8.1-kb recombinant plasmid (pJF8.1) was used for sequencing and revealed the presence of two open reading frames (ORFs). ORF1 codes for a protein of 61 amino acids comprising a 37-amino-acid bacteriocin that was determined to be the leucocin B-Ta11a structural gene by virtue of its homology to leucocin A-UAL 187 (Hastings et al. 1991. J. Bacteriol 173:7491-7500). The 24-amino-acid N-terminal extension, however, differs from that of leucocin A-UAL187 by seven residues. The predicted protein of the ORF2 has 113 amino acids and is identical with the amino acid sequence of the cognate ORF of the leucocin A-UAL 187 operon.
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PMID:Characterization of leucocin B-Ta11a: a bacteriocin from Leuconostoc carnosum Ta11a isolated from meat. 776 96

Seventy-four Gram-positive, catalase-positive coccal strains were isolated from fresh beef stored under carbon dioxide (< 500 ppm O2) or vacuum for up to 15 weeks at 0, 2 or 4 degrees C. Isolates were identified using biochemical tests listed in several published protocols and the API Staph-Ident System. No isolates were identified as Staphylococcus aureus. Twenty-nine isolates were identified as Staphylococcus saprophyticus (five distinct groups), 24 isolates were identified as Staphylococcus gallinarum and 21 isolates were identified as Micrococcus varians. The staphylococcal isolates were coagulase-negative, non-hemolytic and novobiocin resistant. They produced acid from several carbohydrates under aerobic conditions, hydrolysed gelatin but not collagen, showed lipolytic activity and grew in 15% NaCl. The Micrococcus varians isolates also were salt-tolerant, produced acid only from glucose, fructose and galactose (two strains), and were resistant to lysozyme (1600 micrograms/ml). Lactic acid was the major end product of aerobic glucose metabolism. All S. saprophyticus and M. varians isolates tested contained cell wall fatty acids with chain length > or = C20:0.
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PMID:Identification of psychrotrophic Micrococcaceae spp. isolated from fresh beef stored under carbon dioxide or vacuum. 784 79


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