muramidase and Lung-Diseases--Obstructive

muramidase has been researched along with Lung-Diseases--Obstructive* in 10 studies

Reviews

1 review(s) available for muramidase and Lung-Diseases--Obstructive

ArticleYear
[Current concepts on the biochemistry of bronchial secretions in normal conditions and in diseases of the bronchopulmonary system].
    Problemy tuberkuleza, 1985, Issue:5

    Topics: alpha 1-Antitrypsin; Blood Proteins; Bronchi; Humans; Immunoglobulin A, Secretory; Immunoglobulin E; Immunoglobulin G; Immunoglobulin M; L-Lactate Dehydrogenase; Lipids; Lung Diseases, Obstructive; Malate Dehydrogenase; Mucins; Muramidase; Peptide Hydrolases; Protease Inhibitors; Pseudomonas Infections; Serotonin

1985

Other Studies

9 other study(ies) available for muramidase and Lung-Diseases--Obstructive

ArticleYear
A possible role for lysozyme in determining acute exacerbation in chronic bronchitis.
    Clinical and experimental immunology, 1995, Volume: 102, Issue:2

    The aggregation of non-serotypable Haemophilus influenzae (NTHI) by whole saliva from patients with chronic obstructive lung disease (COLD) was investigated. Significant differences were observed between salivary aggregating activity of a control and COLD population (P < 0.001). Saliva from patients less prone to acute exacerbations had a greater capacity to aggregate bacteria compared with saliva from patients with a predilection to infection. The mechanism of saliva-mediated aggregation of NTHI was investigated and shown to be related to lysozyme content. Lysozyme activity in saliva was measured by the turbidimetric technique and results showed that patients with chronic bronchitis had increased levels of salivary lysozyme, with a subpopulation within the non-infection-prone group having greater amounts. A significant difference was observed in salivary lysozyme between controls and non-infection-prone (P < 0.005) and infection-prone (P < 0.05) patients, respectively: the non-infection-prone patients having significantly (P < 0.005) more than the infection-prone patients. There was significant correlation (r = 0.742, P < 0.001) between salivary aggregation of NTHI and lysozyme activity. Chromatographically purified human lysozyme had a similar aggregation profile to that of saliva. There was no difference in serum and saliva lactoferrin concentrations between groups, but there was a significant increase (P < 0.05) in serum lysozyme concentration in the non-infection-prone group. This study suggests that the level of salivary lysozyme derived from macrophages may play an important role in determining resistance or susceptibility to acute bronchitis.

    Topics: Acute Disease; Adult; Aged; Bronchitis; Chronic Disease; Communicable Diseases; Female; Haemophilus influenzae; Humans; Inflammation; Lactoferrin; Lung Diseases, Obstructive; Macrophages; Male; Middle Aged; Monocytes; Muramidase; Neutrophils; Saliva; Salivation

1995
[Bronchoalveolar lavage--a diagnostic method in chronic nonspecific bronchopulmonary diseases in childhood? 2. Studies of cellular and humoral parameters in BAL irrigation fluid].
    Zeitschrift fur Erkrankungen der Atmungsorgane, 1991, Volume: 176, Issue:1

    With a view of the pathogenesis of chronic bronchopulmonary diseases the interrelations between infections and evolving defense system are of interest, they are perhaps detectable by means of diagnostic bronchoalveolar lavage. We carried out cytodifferentiation, investigated adenosine deaminase activities and interleukin 1 formation of macrophages, determined immunoglobulin concentrations (secretory IgA), lysozyme, alpha 2-macroglobulin, alpha 1-antitrypsin, albumin. Because the cytodifferentiation yields insight into topical inflammatory reactions, shows diagnostic useful informations in single cases and because it is simple to carry out we can recommend it for each bronchological examination. There were no results specific for any disease group for parameters mentioned above.

    Topics: Adenosine Deaminase; Adolescent; alpha 1-Antitrypsin; Bronchoalveolar Lavage Fluid; Child; Child, Preschool; Female; Humans; Immunoglobulin A; Immunoglobulin G; Immunologic Deficiency Syndromes; Infant; Interleukin-1; Leukocyte Count; Lung Diseases, Obstructive; Macrophages; Male; Muramidase; Respiratory Tract Infections; Serum Albumin

1991
In vitro restructuring effect of human airway immunoglobulins A and lysozyme on airway secretions.
    European journal of respiratory diseases. Supplement, 1987, Volume: 153

    The in vitro effects of different pure proteins: IgA, IgM and human airway lysozyme (HAL) on rheological and transport properties of airway secretions from patients with chronic bronchitis, were studied. The proteins were added to the reconstituted sputum samples in concentrations within the range present in sputa (IgA: 4% HAL: 1% and IgM: 0.5%). A significant (p less than 0.05) positive increase in apparent viscosity and in elastic modulus was observed after adding IgA or HAL. This suggests that these two secretory proteins contribute to the viscoelastic properties of airway secretions and may act as restructuring molecules. After protein overload of the sputum samples, opposite changes in mucociliary transport rate were observed according to whether the initial values of protein concentration and rheology were abnormally low or high. These results suggest that, as for mucus rheology, there is an intermediate range of IgA and HAL optimal for mucociliary transport rate.

    Topics: Elasticity; Humans; Immunoglobulin A; Lung Diseases, Obstructive; Muramidase; Osmolar Concentration; Proteins; Respiratory System; Rheology; Viscosity

1987
[Prognosis of the course of nonspecific lung diseases and possibilities of their immuno-correction].
    Sovetskaia meditsina, 1986, Issue:6

    Topics: Humans; Immunotherapy; Leukocyte Count; Lung Diseases, Obstructive; Muramidase; Periodicity; T-Lymphocytes

1986
Inhibitor activity against elastolytic enzymes in the bronchial area. A contribution to the pathogenesis of chronic airway obstruction.
    Zeitschrift fur Erkrankungen der Atmungsorgane, 1985, Volume: 165, Issue:1

    In the bronchial mucus of patients with long-term airway obstruction free elastolytic activities are observed. These originate from leucocytes with polymorphous nuclei and may cause the digestion of lung tissue and thus an emphysematous lung metaplasia. It is known that the supersensitivity of bronchial musculature increases due to the influence of proteolytic ferments. For the inhibition of elastolytic enzymes, specific, acid-proof, low-molecular inhibitory substances are available. We were able to measure three of them in bronchial mucus against different substrates; i.e. against substrates for trypsin, pancreas elastase and leucocyte elastase. Our results show that the free inhibitor preparation decreases if free elastolytic activity in bronchial mucus is measured and is no longer available if the concentration decreases. It was also found that the concentration of secretory IGA decreases if the elastolytic activity increases. Thus, it is possible that the secretory IGA molecule is attacked by proteolytic enzymes. It is known that in case of chronic obstructive airway diseases lysozyme is released from leucocytes with polymorphous nuclei; in case of silicosis, from macrophages as well. In this study, the lysozyme concentration served as measurement for cell decomposition. The observation showed that in spite of the same lysozyme levels the elastolytic activity in patients can be very different. It is in strong connection with the available inhibitor capacity. Regarding the clinical evaluation can be concluded that some patients show a lack of secretory inhibitors. On a long-term basis, this lack can lead to the formation of emphysemata.

    Topics: Anti-Bacterial Agents; Bronchi; Cortisone; Humans; Lung Diseases, Obstructive; Mucus; Muramidase; Neutrophils; Pancreatic Elastase; Prognosis; Sputum

1985
Lysozyme and lactoferrin in sputum from patients with chronic obstructive lung disease.
    European journal of respiratory diseases, 1984, Volume: 65, Issue:7

    The two basic proteins lysozyme and lactoferrin have been isolated from solubilized mucoid sputum from patients with chronic bronchitis in one step by cation exchange chromatography. In sputa from 13 patients with chronic bronchitis their mean concentrations were 0.4 g/l and 0.7 g/l, respectively, representing 6.6% and 11.5% of the total amount of solubilized protein. Lysozyme and the acid mucin glycoproteins of sputum formed aggregates at low ionic strength, probably as a result of electrostatic interactions between the two. Although only aggregates were formed and not a viscoelastic fluid or a gel, these interactions may contribute to the viscoelastic properties of native sputum.

    Topics: Chromatography, Ion Exchange; Humans; Lactoferrin; Lactoglobulins; Lung Diseases, Obstructive; Mucins; Muramidase; Sputum; Viscosity

1984
[Quantification of IgA and lysozyme proteins in sputum from patients with chronic obstructive pulmonary disease. I. Relation of the proteins to sputum viscosity].
    Revista clinica espanola, 1984, Feb-15, Volume: 172, Issue:3

    Topics: Humans; Immunoglobulin A; Lung Diseases, Obstructive; Male; Muramidase; Sputum; Viscosity

1984
The release of elastase, myeloperoxidase, and lysozyme from human alveolar macrophages.
    The American review of respiratory disease, 1982, Volume: 126, Issue:2

    Human alveolar macrophages from lungs of cigarette smokers were retrieved by lavage of surgical specimens. The macrophage secretions were harvested after 18 h of incubation. The medium contained at least 2 acid-stable factors that could release enzymes from cytochalasin-B-treated human neutrophils. Our study focused on the largest of these factors, which had an apparent mass ratio of 5,400 by gel filtration chromatography in 10% acetic acid. The high molecular weight (HMW) factor was partially degraded by trypsin. Chymotrypsin completely destroyed the factor, but human neutrophil elastase did not affect it. The factor is partially extractable into chloroform indicating that it is very hydrophobic and may contain a lipid. High concentrations of the HMW factor inhibited the release of lysozyme and myeloperoxidase. Because elastases can cause emphysema when introduced into alveoli of animals, the most important observation may be that the HMW factor was able to release elastase from human neutrophils attached to Millipore membranes in the absence of cytochalasin B. The enzyme-releasing factors may be identical to neutrophil chemotactic factors recently described by others. The contribution of the released elastase to the protease load in the lung may be augmented by the simultaneous release from neutrophils of myeloperoxidase, which can inactivate alpha 1-antitrypsin. This interaction between alveolar macrophages and neutrophils may have importance in the pathogenesis of emphysema.

    Topics: Chemotaxis, Leukocyte; Chromatography, Gel; Female; Humans; In Vitro Techniques; Lung Diseases, Obstructive; Male; Muramidase; Neutrophils; Pancreatic Elastase; Peroxidase; Peroxidases; Pulmonary Alveoli; Pulmonary Emphysema; Solubility

1982
The importance of lysozyme for the viscosity of sputum from patients with chronic obstructive lung disease.
    Scandinavian journal of clinical and laboratory investigation, 1980, Volume: 40, Issue:8

    Addition of lysozyme (1 g/l) to sputum from patients with chronic obstructive lung disease increased the viscosity of the material significantly. The effect was prevented by addition of salt (LiCl) in the high concentration (0.25 mol/l). The sole addition of salt decreased the viscosity of native sputum. These results together with our earlier [5] studies of the interaction between the positively charged lysozyme and the negatively charged mucin molecules in model systems, indicate that lysozyme acts as a cross-linking agent in mucus by an electrostatic mechanism. Lysozyme is thus, at least partly, responsible for building up a macromolecular network giving mucus its characteristic gel-like properties.

    Topics: Chlorides; Humans; Lithium; Lung Diseases, Obstructive; Mucus; Muramidase; Sputum; Viscosity

1980