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)

Sedimentation method has been used to study hen egg-white lysozyme binding to glucosylated (from T2 phage) and non-glucosylated (from calf thymus) DNA under conditions similar to physiological ones (pH 7,3--7,4, ionic strength 0.07--0.24). The results indicate that lysozyme binds cooperatively to both DNA's. Binding parameters have been obtained by applying the theory of one-dimensional adsorption of small molecules on a linear homopolymer. X-ray patterns of complexes with different protein content have been obtained.
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PMID:[DNA complexes with lysozyme]. 3 32

Earlier studies on fetal thymus suggested that certain of the large pyroninophilic cells found there might have a hemopoietic role, and it was decided to determine the nature of these cells using histochemical and immunohistochemical methods. Thymic tissue from aborted fetuses, stillbirths, and neonatal deaths was examined histochemically using methods for the detection of chloroacetate esterase, peroxidase, and pseudoperoxidase, and by staining techniques for mast cells and eosinophils. Tissue was also examined using the indirect immunoperoxidase method for the presence of hemoglobin A (HbA) and F (HbF), for lysozyme (muramidase) and immunoglobins alpha, mu, gamma, kappa, lambda. Positive staining to some degree was seen in cells in the connective tissue stroma using all methods, and the cells stained corresponded to one or another of the types of pyroninophilic cells present. The finding of large cells with positive chloroacetate esterase and antilysozyme indicates the presence of granulopoiesis. Similarly, the presence of large nucleated cells with pseudoperoxidase and anti-hemoglobin (A and F) staining indicates the presence of erythropoiesis. Plasma cells were present in small numbers.
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PMID:Evidence for significant hematopoiesis in the human thymus. 5 99

Monolayer and suspension cell cultures prepared from Hodgkin's disease tumors in the spleen were examined microscopically and by cytogenetics, tested for lymphocyte and monocyte cell surface properties, and assayed for enzymes by histochemical and spectrophotometric techniques. Hodgkin's disease monolayer cultures were composed of rapidly proliferating round and polygonal cells that were capable of propagation in vitro for an indefinite period of time. Abnormal aneuploid chromosomes were found in short-term Hodgkin's disease monolayers that had been passaged 16-20 times, and in established cell lines carried in culture longer than 3 yr and passaged more than 200 times. Cells fromHodgkin's disease monolayers contained lysozyme (muramidase), fluoride-resistant alpha naphthol acetate esterase, acid and alkaline phosphatase, and chymotrypsin-like activity. The monolayers did not exhibit specific cell surface markers or phagocytosis. Suspension cultures derived from Hodgkin's disease monolayers were composed of cells with aneuploid karyotypes and similar enzymes. The Hodgkin's disease suspension culture cells had surface receptors for complement and IgGFc, lacked surface or cytoplasmic immunoglobulin, and did not form Erosettes, react with an antithymocyte serum, nor exhibit phagocytosis. Normal monolayer culture cells, derived from adult spleen and human fetal spleen and thymus, were composed of spindle cells with a diploid number of chromosomes that could be carried for only a finite period of time in vitro. Normal cultured cells contained similar esterases and phosphatases, but were devoid of lysozyme and chymotrypsin-like activity. The morphologic, cytogenetic, cell surface, and enzymatic findings indicate that our Hodgkin's disease monolayer and suspension cultures are composed of cells with many properties suggesting an origin from monocytes (macrophages) rather than lymphocytes or fibroblasts. The presence of aneuploid karyotypes is consistent with a neoplastic origin and derivation from a malignant cell of Hodgkin's disease.
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PMID:Tissue culture studies in Hodgkin's disease: Morphologic, cytogenetic, cell surface, and enzymatic properties of cultures derived from splenic tumors. 6 93

Delayed footpad reaction (FPR) to lysozyme (Lys) in mice was induced without antibody responses by lipid-conjugated lysozyme (D.Lys). This FPR was suppressed by priming s.c. with a high dose (10 mg) of Lys 2 weeks previously (unresponsiveness). Spleen cells from the unresponsive mice suppressed antigen-specifically FPR in mice previously immunized with D.Lys, and also suppressed passive transfer of FPR by D.Lys-immune lymphoid cells into normal mice. The suppressive activity of the spleen cells was abolished by treatment with anti-phi anti-serum and complement. The suppressor cells occurred also in the thymus of unresponsive mice. Unresponsiveness was induced in mice immediately after priming with Lys and persisted at least up to 7 weeks after the induction. In contrast, suppressor cells appeared only 2 weeks after induction of unresponsiveness in both the spleen and the thymus but were no longer detectable 3-7 weeks later, although donor mice remained fully unresponsive. These results suggest that antigen-specific suppressor T cells are involved in the regulation of the expression of FPR only for a definite period of time in unresponsive mice.
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PMID:Regulatory role of suppressor T cells in the expression of delayed-type hypersensitivity in mice. I. Transient appearance of suppressor T cells for the expression of delayed footpad reaction induced with lipid-conjugated lysozyme. 9 72

Thymus cells from mice primed s.c. with a high dose (10 mg) of lysozyme (Lys) specifically suppressed delayed footpad reaction (FPR) in mice previously immuned with lipid-conjugated lysozyme (D.Lys), and also suppressed the transfer of FPR by D.Lys-immune spleen cells into normal mice. Furthermore, they inhibited antigen-stimulated DNA synthesis of D.Lys-immune spleen cells in vitro. If the suppressor thymus cells were cultured with Lys in vitro, they produced soluble factor which depressed the ability of D.Lys-immune spleen cells to transfer FPR. Both supernatant of culture without Lys and extract of suppressor thymus cells were inactive in supression of FPR. The suppressor factor was antigen-specific because its suppressive activity was absorbed with Lys but not with an unrelated antigen lactalbumin. The factor failed to depress the ability of D.Lys-immune spleen cells to transfer FPR when the spleen cells were depleted of glass-adherent cells. In addition, incubation of peritoneal exudate cells from normal mice with the factor rendered the cells suppressive for passive transfer of FPR. These results suggest that the suppressor factor depresses the effector function of T cells responsible for FPR possibly via macrophage.
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PMID:Regulatory role of suppressor T cells in the expression of delayed-type hypersensitivity in mice. II. Soluble factor from thymic suppressor cells stimulated with antigen in vitro and its possible interaction with macrophages. 9 73

The phosphate content of rat thymus histones was determined. As expected for a replicating tissue, histones 1 and 2B were more phosphorylated and had higher 32P uptakes than did histones from resting liver nuclei; the other histones all showed 32P uptake, but the phosphate content and uptake of histone 2A was about half that for liver histone 2A. When thymus nuclei were incubated in a slightly hypo-osmotic medium, non-histone proteins and phosphorylated histones were released into solution; this was enhanced if ATP was present in the medium. [gamma-32P]ATP was incorporated into non-histone proteins, including protein P1, and into the ADP-ribosylated form of histone 1; negligible 32P was incprporated into the other, bound, histones. Histones 1 and 2B added to the incubation medium were extensively, and histones 2A and 4 slightly, phosphorylated. Histones released by increasing the ionic strength of the medium were phosphorylated. Added lysozyme and cytochrome c were neither bound nor phosphorylated, but added non-histone protein P1 was phosphorylated, causing other histones to be released from the nuclei, especially histones 2A and 3. The released histones were phosphorylated. gamma-Irradiation decreased 32P uptake into the non-ADP-ribosylated histones 1 and 4; phosphorylation of histone 1 in vitro was unaffected. The importance of non-histone proteins, ATP availability and nuclear protein kinases to the control of histone phosphorylation in vivo is discussed.
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PMID:Phosphorylation of rat thymus histones, its control and the effects thereon of gamma-irradiation. 19 8

Immunostaining paraffin sections of appropriately fixed tissues with an antiserum to human urinary lysozyme as the primary step in an immunoglobulin-peroxidase bridge method has localized lysozyme in previously recognized sites such as Paneth cells, renal tubules, and lymph node macrophages in several species. In addition, lysozyme was demonstrated in the ciliary layer of the trachea, and type II pneumocytes, as well as cells of presumed mucoid nature in laryngotracheal glands. Large stellate cells in follicle centers in the lymph nodes and spleen and in the medulla of the thymus evidenced strong lysozyme reactivity. Granular pneumocytes disclosed immunoreactivity for lysozyme also at the ultrastructural level. Lysoplate assay demonstrated lysozyme in abundance in both the cellular pellet and acellular supernatant of rat alveolar wash fluid and in rat lung after repeated washing of alveoli. Hamster lung differed from the others in failing to immunostain for lysozyme and affording no evidence for content of lysozyme as determined by lysoplate assay. Sites stained with antiserum to human urinary lysozyme failed to stain with antiserum to egg white lysozyme. However, the pyloric glands, Golgi elements in intestinal epithelium, the surface of the colon, and the proximal straight renal tubule of the mouse stained exclusively with the antiserum to hen egg white lysozyme. Many sites staining with antiserum to urinary lysozyme in respiratory, renal, and lymphoid tissue lacked reactivity in control sections exposed to this antiserum after it was absorbed with purified urinary lysozyme. However, mucous acini in submandibular glands, although failing to stain with other control procedures, retained towared the absorbed antiserum, possibly through reacting with an antibody other than that for human urinary lysozyme. A number of cell types containing proteinaceous cytoplasmic granules stained in control sections exposed to normal serum in place of antilysozyme serum in the immunoglobulin-peroxidase bridge procedure and, thus, possessed selective, but nonimmunospecific affinity for immunoglobulin. Cell types that stained with antiserum to hen egg white lysozyme lost affinity for the antiserum after its absorption with egg white lysozyme but retained the affinity after absorption with urinary lysozyme.
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PMID:Immunocytochemical localization of lysozymes in respiratory and other tissues. 32 Mar 84

Lysozyme activity of macrophages and giant cells in various human granulomas were examined with immunoperoxidase bridge method in tissue sections. Various numbers of epithelioid cells and giant cells of epithelioid cell granulomas of tuberculosis, sarcoidosis and Crohn's disease exhibited intense granular cytoplasmic lysozyme activity. Foreign body granulomas induced with various substances showed negative or faintly positive lysozyme stain. Macrophages and giant cells of aspergillus granuloma associated with thymus hypoplasia and T-cell depression contained no lysozyme. The results suggest that cell-mediated immunology plays an important role for the lysozyme synthesis of macrophages in granuloma.
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PMID:Immunohistochemical observation of lysozyme in macrophages and giant cells in human granulomas. 36 52

During purification of E2R using oligo(dT)-cellulose chromatography, a receptor accessory factor (RAF) was identified in the cytosol of mouse kidney. This factor stimulates the binding of purified E2R to oligo(dT)-, oligo(dC)-, and oligo(dA)-cellulose as well as to DNA cellulose. It is a heat-stable, trypsin-resistant protein with an apparent molecular weight of between 10 and 30,000 daltons. Although structurally unrelated, similar stimulation of oligonucleotide binding was seen with calf thymus histones and, to a lesser extent, egg white lysozyme. Individual histones, especially H2a, H2B, and H3, also facilitate rebinding of purified E2R to oligo(dT)-cellulose, while H1 is less effective. Furthermore, histones stabilize the holoreceptor during sedimentation at 4 degrees and 12 degrees C. The N- and C-terminal half molecules of H2b were generated by cyanogen bromide-mediated cleavage and the N-terminal half was found to duplicate the effects of the parent molecule, both in binding and holoreceptor stabilization. These data suggest that the in vivo binding of E2R to DNA can be modulated by accessory proteins of cytosol and nuclear origin.
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PMID:Stimulation of oligonucleotide binding of estradiol receptor complexes by accessory proteins. 49 27

Using the immunoperoxidase method, major changes in the distribution of lysozyme (LZM) were found to occur during fetal development. At 10 weeks of gestation LZM was detected for the first time in the proximal tubules of the kidney. This generally coincides with the reported appearance of LZM in fetal blood and amniotic fluid. The enzyme was observed in lung macrophages and in mononuclear cells of the lamina propria of the small intestine in fetuses 12 and 16 weeks old, respectively. At about 18--20 weeks, LZM-positive mononuclear cells were detected in other tissues tested, such as liver, spleen and thymus. Paneth cells were found to be specifically stained at about 20 weeks of gestation. The timing of the appearance of LZM in the various tissues is discussed in relation to the functional maturation of each organ and the ontogeny of this enzyme in other species.
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PMID:Ontogeny of human lysozyme. Distribution in fetal tissues. 61 Jul 61


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