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

---

Query: EC:3.2.1.17 (lysozyme)
21,489 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Twelve cases of pure acute monocytic leukemia in adults were studied. They were selected on the basis of the morphology of the blast cells on Romanowsky-stained smears of blood and bone marrow, as well as positivity of the cells for the naphthol ASD acetate esterase reaction specifically inhibited by sodium fluoride. There was no sex predominance. Neoplastic involvement of the skin and/or gingiva was very frequent. The leukemic proliferation in blood and bone marrow consisted of monoblasts, promonocytes and monocytes. The peroxidase reaction was negative or only faintly positive. Serum and urinary lysozyme levels were increased. The blast cells retained their ability to stimulate, in vitro, colony formation by normal bone marrow cells used as targets. All of these characteristics permit specific identification of this type of acute leukemia. The prognosis is grim: only five of 12 patients achieved complete remission, and four of these five had relapses in less than 14 months; the median survival was five months.
...
PMID:Pure acute monocytic leukemia. A study of 12 cases. 30 66

Human milk was subjected to heat treatments of graded severity and examined for its content of immunoglobulins, lactoferrin, lysozyme, vitamin B12-and folate-binder proteins, and lactoperoxidase. Holder pasteurization (62.5degrees C 30 minutes) reduced the IgA titer by 20%, and destroyed the small content of IgM and most of the lactoferrin. Lysozyme was stable to this treatment, but with an increase in temperature there was progressive destruction, to near 100% at 100degrees C. The same was broadly true of the capacity of milk to bind folic acid and potect it against bacterial uptake; with vitamin B12 the binder was more labile at 75degrees C than at 100degrees C. The milk contained no detectable lactoperoxidase.
...
PMID:Influence of the heat treatment of human milk on some of its protective constituents. 31 82

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.
...
PMID:Immunocytochemical localization of lysozymes in respiratory and other tissues. 32 Mar 84

Phorbol myristate acetate (PMA, 2 to 100 ng/ml) and ionophore A23187 (10(-7) to 10(-6) M) cause human neutrophils to release up to 50% of the granule-associated enzyme lysozyme extracellularly without release of beta-glucuronidase or the cytoplasmic enzyme LDH. When azurophil and specific granules are separated from neutrophil lysates by sucrose density centrifugation, it is found that lysozyme release from neutrophils exposed to PMA or to A23187 reflects a selective disappearance of the small, peroxidase-negative (specific) granules from the cells. These studies demonstrate that neutrophils can mobilize the specific and azurophil granules independently. These studies also demonstrate that under certain conditions the specific granules of human neutrophils behave like the storage granules of secretory cells. Finally, these studies show that techniques of separating neutrophil granules according to their sedimentation characteristics successfully divide these granules into populations that are distinct not only by cytochemical and morphologic criteria but also according to their availability for mobilization and extracellular release. (APM J Pathol 87:273-284, 1977).
...
PMID:The differential mobilization of human neutrophil granules. Effects of phorbol myristate acetate and ionophore A23187. 32 7

An immunocytochemical unlabelled antibody method using rabbit antihuman lysozyme, antirabbit immunoglobulin, and soluble rabbit antihorseradish peroxidase/horseradish peroxidase complexes was used to study the fine structural distribution of lysozyme in human bronchial glands. None was identified in mucous cells but there was heavy staining of the serous cell granules. The serous cell granules were not stained uniformly, suggesting the presence of other secretory products but lysozyme secretion appears to be a major function of these cells. The pathological implications of this are discussed.
...
PMID:Ultrastructural immunocytochemical localisation of lysozyme in human bronchial glands. 32 82

Mechanisms were studied that might explain the attachment and damage to Candida albicans pseudohyphae by neutrophils in the absence of serum. Attachment of neutrophils to pseudo hyphae was inhibited by Candida mannans (1-10 mg/ml), but not by mannose, dextran, chitin, conconavalin A, or highly charged polyamino acids. Contact was also inhibited by pretreatment of Candida before incubation with neutrophils with chymotrypsin, but not trypsin or several inhibitors of proteases. Similar results were obtained with pretreatment of neutrophils, except that trypsin was inhibitory. When pseudohyphae were killed with ultraviolet light, proteinpolysaccharide complexes of mol wt <10,000 were released which appeared to bind to the surfaces of neutrophils and inhibit contact between neutrophils and Candida, as well as other fungi. Damage to Candida by neutrophils was inhibited by agents known to act on neutrophil oxidative microbicidal mechanisms, including sodium cyanide, sodium azide, catalase, superoxide dismutase, and 1, 4 diazobicyclo (2, 2, 2) octane, a singlet oxygen quencher. Neutrophils from a patient with chronic granulomatous disease did not damage Candida at all. However, the hydroxyl radical scavengers mannitol and benzoate were not inhibitory. Cationic proteins and lactoferrin also did not appear to play a major role in this system. Low concentrations of lysozyme which did not damage Candida in isotonic buffer solutions damaged pseudohyphae in distilled water. Isolated neutrophil granules damaged pseudohyphae only with added hydrogen peroxide and halide, and damage occurred only with granule fractions known to contain myeloperoxidase. These findings suggest that neutrophils recognized a molecule on the Candida surface which has a chymotrypsin sensitive protein component, and which may be liberated from the cell surface upon death of organism. The neutrophil receptors for Candida appear to be sensitive to trypsin and chymotrypsin. Damage to Candida by neutrophils occurred primarily by oxidative mechanisms, including the production of superoxide and hydrogen peroxide interacting with myeloperoxidase and halide, as well as singlet oxygen, but did not appear to involve hydroxyl radical. Lysozyme might have an accessory role, under some conditions.
...
PMID:Mechanisms of attachment of neutrophils to Candida albicans pseudohyphae in the absence of serum, and of subsequent damage to pseudohyphae by microbicidal processes of neutrophils in vitro. 34 Apr 71

The antimicrobial activity of various proteins and other substances in milk and colostrum is discussed. These factors include antibodies, complement, lactoferrin and transferrin, lactoperoxidase and lysozyme. The possible importance of these factors in protecting the newborn infant against infectious diseases is discussed.
...
PMID:[Antimicrobial factors in milk and colostrum: their importance for the newborn infant (author's transl)]. 34 62

Polymorphonuclear leukocytes (PMNs) are one of the main sources of enzymes responsible for tissue damage in inflammatory processes. These enzymes are stored in two types of cytoplasmic granules. Azurophil granules contain lysosomal hydrolases, neutral serine proteinases, and bactericidal elements (myeloperoxidase and lysozyme). Specific granules contain collagenase, lysozyme and lactoferrin but lack lysosomal hydrolases. PMNs store all four classes of tissue proteinases, carboxyl, thiol and serine proteinases in the azurophil granules, and metallo proteinases in the specific granules. Three serine proteinases have been identified, elastase, cathepsin G and a third enzyme, which together account for a large proportion of the protein of the azurophil granules. In the course of phagocytic events, all these enzymes are released extracellularly. The neutral proteinases degrade proteoglycans and collagen. In vitro, they stimulate B-lymphocytes, which suggests that they may have immuno-potentiating activity when they are released at sites of chronic inflammation.
...
PMID:The polymorphonuclear leukocyte. 34 82

The bactericidal action that results from lactoperoxidase-catalyzed oxidation of iodide or thiocyanate was studied, using Escherichia coli as the test organism. The susceptibility of intact cells to bactericidal action was compared with that of cells with altered cell envelopes. Exposure to ethylenediaminetetraacetic acid, to lysozyme and ethylenediaminetetraacetic acid, or to osmotic shock were used to alter the cell envelope. Bactericidal action was greatly increased when the cells were exposed to the lactoperoxidase-peroxide-iodide system at low temperatures, low cell density, or after alteration of the cell envelope. When thiocyanate was substituted for iodide, bactericidal activity was observed only at low cell density or after osmotic shock. Low temperature and low cell density lowered the rate of destruction of peroxide by the bacteria. Therefore, competition for peroxide between the bacteria and lactoperoxidase may influence the extent of bactericidal action. Alteration of the cell envelope had only a small effect on the rate of destruction of peroxide. Instead, the increased susceptibility of these altered cells suggested that bactericidal action required permeation of a reagent through the cell envelope. In addition to altering the cell envelope, these procedures partly depleted cells of oxidizable substrates and sulfhydryl components. Adding an oxidizable substrate did not decrease the susceptibility of the altered cells. On the other hand, mild reducing agents such as sulfhydryl compounds did partly reverse bactericidal action when added after exposure of cells to the peroxidase systems. These studies indicate that alteration of the metabolism, structure, or composition of bacterial cells can greatly increase their susceptibility to peroxidase bactericidal action.
...
PMID:Susceptibility of Escherichia coli to bactericidal action of lactoperoxidase, peroxide, and iodide or thiocyanate. 34 97

Conjugation of lysozyme with horse radish peroxidase by means of glutaraldehyde results in a complex which retains the activities of both enzymes. The incubation of peptidoglycan with lysozyme-peroxidase followed by the reaction with 3,3'-diaminobenzidine and H2O2 results in a strong labelling of both sides. In contrast, after treatment with peroxidase alone no reaction was observed. Thus, the specific binding of lysozyme-peroxidase can be used for the electron microscopic localization of this component in the bacterial cell wall. Isolated peptidoglycane as well as trypsinized cell walls of group A and C streptococci were labelled both on the inner and the outer surface. The surface of intact cells of group A- and C-streptococci was labelled only sparsely. In contrast, by means of the indirect immunoferritin technique strong labelling of intact cells was effected with specific anti-peptidoglycan antibodies. The specificity of these antibodies are mainly directed to the peptide side chains. From this we suggest that in the cell wall of group A and C streptococci the lysozyme-sensitive part of the peptidoglycan is not so superficially localized as the peptides.
...
PMID:The use of lysozyme-peroxidase-conjugates for the electron microscopic detection of peptidoglycan in the cell wall of streptococci. 35 34


<< Previous 1 2 3 4 5 6 7 8 9 10 Next >>

---