muramidase and Bronchitis

Oral immunotherapy with inactivated non-typeable Haemophilus influenzae (NTHi) prevents exacerbations of chronic obstructive pulmonary disease, but the mechanism is unclear. The aim of this study was to determine the mechanism of protection. This was a placebo versus active prospective study over 3 months in 64 smokers. The active treatment was three courses of oral NTHi given at monthly intervals, followed by measurement of bacteriological and immunological parameters. The results can be summarized: (i) NTHi-specific T cells increased in the placebo treatment group over time (P<0.05); (ii) the T cell response in the oral NTHi group started earlier than that in the placebo group (P<0.05); and (iii) serum NTHi-specific immunoglobulin (Ig)G had significantly greater variation in the placebo group (P<0.0001). The increase in antibody in placebos over time correlated with exposure to live H. influenzae (P<0.05) determined from culture of gargles; (iv) reduction in saliva lysozyme over time (P<0.05) was detected only in the oral NTHi treatment group. These data are consistent with T cell priming of gut lymphoid tissue by aspiration of bronchus content into the gut, with oral immunotherapy augmenting this process leading to enhanced bronchus protection. The evidence for protection was a stable IgG antibody level through the study in the oral NTHi treatment group, contrasting with an increase in antibody correlating with exposure of the airways to H. influenzae in the placebo group. Saliva lysozyme was a useful biomarker of mucosal inflammation, falling after oral NTHi consistent with a reduction in the level of intralumenal inflammation.

Topics: Administration, Oral; Adolescent; Adult; Antibodies, Bacterial; Bronchitis; Carrier Proteins; Disease Progression; Female; Haemophilus influenzae; Haemophilus Vaccines; Humans; Immunity, Mucosal; Immunoglobulin G; Interferon-gamma; Lactoferrin; Male; Middle Aged; Muramidase; Nitric Oxide; Prospective Studies; Pulmonary Disease, Chronic Obstructive; Saliva; Smoking; Sputum; T-Lymphocytes; Vaccines, Inactivated; Young Adult

Chronic bronchitis is associated with airways obstruction and inflammation. In order to determine whether aerosolized beclomethasone can modulate airway inflammation and diminish airway obstruction, subjects with chronic bronchitis performed spirometry and underwent bronchoalveolar lavage (BAL) before and after receiving 6 wk of therapy (five puffs four times a day) with either aerosolized beclomethasone (n = 20) or placebo (n = 10) in a double-blinded, randomized fashion. All subjects received aerosolized albuterol before each use of the study medications. Before BAL, the airways were visually assessed for the appearance of inflammation and assigned a score, the bronchitis index. BAL was performed by instilling five 20-ml aliquots of saline into each of three sites and pooling and separately analyzing the returns from the first aliquots to yield a "bronchial sample." The bronchial lavages were repeated in an additional three sites to increase the volume of fluid available for analysis. The fluid was prepared for cytologic examination by cytocentrifugation. Albumin (as a measure of epithelium permeability) and lactoferrin and lysozyme (as measures of serous cell activity) were measured in unconcentrated BAL fluid by enzyme-linked immunosorbent assay, and concentrations in epithelial lining fluid were estimated using urea as an internal marker for dilution. After treatment, the beclomethasone group, but not the placebo group, showed improvement in FVC (p = 0.02), FEV1 (p = 0.002), and 25 to 75% forced expiratory flow (p = 0.006). Associated with the improvement in spirometry, the bronchitis index fell (13.5 +/- 1.0 versus 10.75 +/- 1.1, p = 0.02) in the beclomethasone-treated group, but not the placebo-treated group.(ABSTRACT TRUNCATED AT 250 WORDS)

Topics: Administration, Inhalation; Adult; Aerosols; Airway Obstruction; Albumins; Beclomethasone; Blood Gas Analysis; Bronchitis; Bronchoalveolar Lavage Fluid; Bronchoscopy; Chronic Disease; Double-Blind Method; Female; Forced Expiratory Volume; Humans; Inflammation; Lactoferrin; Male; Middle Aged; Muramidase; Smoking; Transferrin; Vital Capacity

Topics: Albumins; Asthma; Bromhexine; Bronchitis; Chronic Disease; Clinical Trials as Topic; Female; Gels; Glycoproteins; Humans; Male; Middle Aged; Muramidase; Placebos; Proteins; Sputum; Ultracentrifugation

Antimicrobial proteins are important in lung defense and are potential therapeutic agents in chronic airways infection such as seen in cystic fibrosis (CF). In preparation for future clinical studies, we sought (1) to determine levels of three antimicrobial proteins [lactoferrin, lysozyme, and secretory leukoprotease inhibitor (SLPI)] in the CF airway and (2) to examine the relationships between these antimicrobial proteins and airway inflammation and infection. We examined bronchoalveolar lavage fluid (BALF) from 45 individuals with CF and 23 disease control individuals. Airway inflammation was measured through BALF neutrophil counts and neutrophil elastase activity. Infection was assessed through quantitative counts of CF-related bacterial pathogens. BALF lysozyme activity and lactoferrin levels were elevated in individuals with CF compared to controls whereas SLPI levels were not different between the groups. Among the CF subjects, lysozyme activity and lactoferrin increased with age while SLPI decreased with age. Lysozyme activity and lactoferrin concentrations correlated positively with neutrophil counts but not with bacterial colony counts. SLPI levels were inversely related to both neutrophil counts and bacterial colony counts. This study provides information concerning the levels of antimicrobial proteins present in the CF airway that are relevant to future clinical trials of these compounds and demonstrates clear relationships between antimicrobial protein-specific levels and airway inflammation and infection.

Topics: Adolescent; Adult; Biomarkers; Bronchitis; Bronchoalveolar Lavage Fluid; Case-Control Studies; Child; Child, Preschool; Cross-Sectional Studies; Cystic Fibrosis; Female; Humans; Immunity, Innate; Infant; Lactoferrin; Leukocyte Count; Leukocyte Elastase; Male; Muramidase; Respiratory Tract Infections; Secretory Leukocyte Peptidase Inhibitor; Young Adult

Active smoking increases asthma severity and is related to diminished treatment efficacy. Animal models in which inhalation of both allergen and mainstream cigarette smoke are combined can help us to understand the complex interaction between both agents. We have recently shown that, in allergic mice, the airway inflammation can be cleared by repeated allergen challenge, resulting in the establishment of a state of inhalational tolerance.. In this study, we assessed in vivo the impact of cigarette smoke on the efficacy and time course of this form of tolerance induction. We exposed sensitized mice to concurrent mainstream cigarette smoke and allergen (Ovalbumin- OVA) and measured the airway inflammation at different time points.. We first confirmed that aerosolized OVA administered for a prolonged time period (4-8 weeks) resulted in the establishment of tolerance. Concurrent OVA and smoke exposure for 2 weeks showed that tobacco smoke enhanced the Th-2 driven airway inflammation in the acute phase. In addition, the induction of the tolerance by repeated inhalational OVA challenge was delayed significantly by the tobacco smoke, since 4 weeks of concurrent exposure resulted in a more persistent eosinophilic airway inflammation, paralleled by a more mature dendritic cell phenotype. However, smoke exposure could not prevent the establishment of tolerance after 8 weeks of antigen exposure as shown by both histopathology (disappearance of the Th-2 driven inflammation) and by in vivo functional experiments. In these tolerized mice, some of the inflammatory responses to the smoke were even attenuated.. Cigarette smoke enhances acute allergic inflammation and delays, but does not abrogate the development of tolerance due to prolonged challenge with inhaled antigen in experimental asthma.

Topics: Animals; Bronchitis; Bronchoalveolar Lavage Fluid; Chemokines; Cytokines; Flow Cytometry; Humans; Immune Tolerance; Immunoglobulin E; Lung; Male; Mice; Mice, Inbred C57BL; Muramidase; Nicotiana; Ovalbumin; Smoke; Th2 Cells; Time Factors

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

Clinical, laboratory and immunological methods used to study 68 patients with chronic bronchitis revealed a normalizing effect of intratracheal administration of lyzozyme and its combinations with carbenicillin on the indices of cellular and humoral links of immunity. Treatment tactics is discussed.

Topics: Adult; Bronchitis; Carbenicillin; Chronic Disease; Drug Evaluation; Drug Therapy, Combination; Female; Humans; Male; Middle Aged; Muramidase; Remission Induction

Topics: Bronchitis; Bronchoalveolar Lavage Fluid; Chronic Disease; Humans; Lactoferrin; Muramidase

Lactoferrin and lysozyme are proteins found in high concentrations on mucosal surfaces, and they have activities potentially important for the modulation of inflammation. To investigate whether these proteins might contribute to the modulation of the intraluminal airway inflammation associated with chronic bronchitis, lactoferrin and lysozyme were measured in bronchoalveolar lavage (BAL) fluid from 22 subjects with chronic bronchitis and, for comparison, with 10 symptom-free smokers and 16 normal subjects. As a further control, transferrin, a protein structurally homologous to lactoferrin but not known to arise in airway epithelial cells, was also measured. BAL was performed by sequentially instilling and retrieving five 20 ml aliquots of normal saline solution into each of three sites. Analyzing the first aliquots separately from the later four provided fluid that was enriched for airway contents. The concentration of lactoferrin (11.83 +/- 2.86 micrograms/ml vs 0.68 +/- 0.18 micrograms/ml, p less than 0.00001), and lysozyme (6.75 +/- 1.51 micrograms/ml vs 0.52 +/- 0.09 microgram/ml, p less than 0.00001), but not transferrin (3.22 +/- 0.38 microgram/ml vs 2.68 +/- 0.24 micrograms/ml, p = 0.55) was higher in the bronchial sample lavage fluid, suggesting an airway origin for lactoferrin and lysozyme. In subjects with chronic bronchitis, bronchial sample lactoferrin (23.1 +/- 0.5 micrograms/ml) and lysozyme (12.6 +/- 3.5 micrograms/ml) were elevated compared with the normal subjects' lactoferrin (1.9 +/- 0.5 micrograms/ml, p less than 0.0001) and lysozyme (0.77 +/- 0.22 microgram/ml, p less than 0.0001) and the symptom-free smokers' lactoferrin (4.1 +/- 0.8 micrograms/ml, p = 0.005) and lysozyme (4.9 +/- 1.3 micrograms/ml, p = 0.02). Transferrin concentrations did not demonstrate the same relationships. Finally, when the content of bronchial sample lactoferrin and lysozyme were compared with the content of bronchial sample neutrophils, poor correlations were found, which may imply an airway epithelial origin for the two proteins. Thus lactoferrin and lysozyme appear to arise in the lower respiratory tract within the airways and their levels are elevated in association with chronic bronchitis. This suggests that lactoferrin and lysozyme may contribute to the modulation of airway inflammation in chronic bronchitis.

Topics: Bronchi; Bronchitis; Bronchoalveolar Lavage Fluid; Chronic Disease; Epithelium; Humans; Lactoferrin; Lactoglobulins; Muramidase; Neutrophils; Pulmonary Alveoli; Respiratory Function Tests; Respiratory System; Smoking; Transferrin

Children with allergic bronchitis and bronchial asthma underwent exercise therapy and training carried out on a regular basis for 9 to 15 months, which resulted in the disease relief, raised exercise tolerance, and promoted normalization of the local defence factors of the respiratory mucosa.

Topics: Adolescent; Asthma; Bronchitis; Child; Child, Preschool; Exercise Therapy; Humans; Immunoglobulin A, Secretory; Muramidase; Nasal Mucosa; Respiration

Local protection in patients with complicated tuberculosis was investigated. The bronchoalveolar lavage fluid (BALF) was tested for the levels of IgA, sIgA, IgM, IgG, lysozyme, activity of granulocyte proteinases (elastase and trypsin-like proteinases) and their acid-fast inhibitors, ability to produce interferons by the BALF cells, the BALF cell composition and functional activity of alveolar macrophages. The local protection was shown to be decreased in the patients with nonspecific inflammatory processes in the bronchi. The decrease was especially pronounced in the patients with purulent endobronchitis. The data indicated the necessity of using immunocorrectors in combined therapy of such patients.

Topics: Adjuvants, Immunologic; Bronchitis; Bronchoalveolar Lavage Fluid; Humans; Immunoglobulins; Interferons; Muramidase; Tuberculosis, Pulmonary

Topics: Bronchitis; Chronic Disease; Humans; Lactoferrin; Lactoglobulins; Muramidase; Sputum

The effects of purified human airway lysozyme and hen egg-white lysozyme on growth rate and viability of growing type I Streptococcus pneumoniae were studied. Exposure of bacteria to human and hen lysozyme at the same final concentration (100 micrograms/ml) for 1.5-4.5 h resulted in a marked reduction of the number of colony-forming units per ml compared to control cultures. After a 1.5-h exposure to human or hen lysozyme, the remaining percentage of colony forming units per ml was 54% and 69%, respectively. The onset of growth only appeared after a 3.5-h exposure period for human lysozyme whereas it began at 2.5 h for hen lysozyme. After 3.5 h and 4.5 h of exposure, the number of colony-forming units was significantly lower (p less than 0.05) in human lysozyme-treated bacteria cultures compared to control cultures. Parallel electron microscopic observations of Streptococcus pneumoniae cultures confirmed that the density of pneumococci was less in the presence of either human lysozyme or hen lysozyme in comparison to control cultures, and showed the presence of numerous long, ribbon-like material and cytoplasmic condensations liberated in the culture medium.

Topics: Bronchi; Bronchitis; Bronchoalveolar Lavage Fluid; Humans; Microscopy, Electron; Muramidase; Streptococcus pneumoniae

The authors presented some data on the lysozyme content and adhesion features of the sputum in 31 patients: 19 patients with chronic obstructive bronchitis and 12 patients with chronic bronchitis against a background of bronchial asthma. Marked reverse correlation between the lysozyme content and sputum adhesion values (r = -0.79) was found. With the subsiding of exacerbation and remission occurrence the lysozyme content increased and a sputum adhesion value reduced. In the exacerbation phase the mean lysozyme content in the sputum was 3.6 +/- 0.1 mg/mg of protein, and in remission occurrence 6.9 +/- 0.2 mg/mg of protein. The adhesion value was 0.6 X 10(4) +/- 0.22 X 10(4) N/m2 and 0.32 X 10(4) +/- 0.01 X 10(4) N/m2, respectively. The time course of the lisozyme content in the sputum of patients with chronic bronchitis can be used as a prognostic factor to assess remission occurrence rates and the nature of change of rheological features of the sputum.

Topics: Adhesiveness; Bronchitis; Chronic Disease; Ciliary Motility Disorders; Humans; Male; Middle Aged; Muramidase; Prognosis; Sputum; Viscosity

A study was made of the humoral (IgA, G, M, lysozyme and lactoferrin) and cellular links (phagocytic activity of alveolar macrophages) of pulmonary local defence as well as sputum adhesion in 177 patients with chronic nonspecific pulmonary diseases (80 patients with chronic obstructive bronchitis, 54 patients with pyo-obstructive bronchitis, 23 patients with chronic purulent bronchitis and 20 patients with chronic nonobstructive bronchitis). A rise of the level of lysozyme and lactoferrin in the bronchial content and sputum as compared to the initial level was accompanied by a decrease in the sputum adhesion and promoted the elimination of exacerbation. In the absence of a rise or reduction of the concentration of lysozyme and lactoferrin over time more prolonged exacerbations and a tendency to purulent complications were noted. A stable drop or absence of IgA in bronchial wash off were observed in patients with IgA selective deficiency, and lung lesions were characterized by inclination to frequent recurrences, lingering exacerbations, concomitant diseases of the accessory sinuses and GI tract disorders. Indices of the phagocytic activity of alveolar macrophages in patients with chronic purulent bronchitis, particularly against a background of chronic alcoholic intoxication, were significantly lower as compared to patients with catarrhal bronchitis.

Topics: Bronchiectasis; Bronchitis; Chronic Disease; Dysgammaglobulinemia; Humans; IgA Deficiency; Immunoglobulins; Lactoferrin; Lung; Macrophages; Muramidase; Phagocytosis; Pneumonia; Pulmonary Alveoli; Recurrence; Sputum

Topics: Bronchitis; Complement System Proteins; Humans; Muramidase; Pneumonia

Topics: Animals; Bronchitis; Chronic Disease; Humans; Male; Medicine, Chinese Traditional; Medicine, East Asian Traditional; Mice; Muramidase; Plant Extracts; Plants, Medicinal; Rats; Sputum

Topics: Bronchi; Bronchitis; Chronic Disease; Humans; Immunodiffusion; Muramidase; Prognosis; Saliva

Bronchial secretions obtained during bronchoscopic examination of 60 children suffering from respiratory tract infections were studied for the concentration of immunoglobulins, anti-proteolytic factors, lactoferrin, and lysozyme. Eleven children having bronchial asthma without a history of chronic or recurrent infections of the respiratory tract were designated as a control. The results were analysed in relation to clinical diagnosis (chronic bronchitis, bronchitis, bronchiectasis) or to the local status of bronchial mucosa at the time of bronchoscopy (no inflammation, inflammation, inflammation with documented bacterial infection). The statistical analysis of the results revealed a decrease of lactoferrin and locally produced IgA in the group of children suffering from bronchitis and chronic bronchitis. Samples infected with Haemophilus species had significantly higher concentration of lactoferrin than any other group. Similarly, albumin in this group was higher than in the other group except that other bacteria were present. Samples infected with Haemophilus also had increased concentrations of S-IgA, IgG, and anti-proteolytic factors when compared with the group without local inflammation.

Topics: Bacterial Infections; Bronchi; Bronchitis; Child; Child, Preschool; Humans; Immunoglobulin A; Immunoglobulin A, Secretory; Lactoferrin; Mucus; Muramidase; Respiratory Tract Infections; Serum Albumin

Topics: Adult; Bronchitis; Chronic Disease; Female; Humans; Immunity, Innate; Male; Muramidase; Phagocytosis

We prepared in rabbits an antiserum against low molecular weight protease inhibitor (LMI) purified from the sputum of patients with purulent bronchitis. Using this antiserum in an immunoperoxidase staining method we found that this inhibitor was located exclusively in the serous cells of the submucosal glands of human upper and lower airways. The inhibitor was localized also in serous cells of the sublingual and submandibular glands. In contrast, LMI could not be demonstrated in the serous cells of the parotid gland. In the tissues investigated a strong association between the localization of the protease inhibitor and lysozyme was observed. Our observations indicate that the inhibitor may be present together with lysozyme as a secretory product in the serous cell granules. The possible consequences of the coexistence of these two proteins in the defense mechanism of the respiratory tract is discussed.

Topics: Amino Acids; Bronchi; Bronchitis; Histocytochemistry; Humans; Immunodiffusion; Immunoenzyme Techniques; Muramidase; Nasal Mucosa; Protease Inhibitors; Salivary Glands; Serous Membrane; Sputum; Trachea

The effects of vasoactive intestinal peptide (VIP) were analyzed on the in vitro release of radioactively labeled mucus glycoconjugates and lysozyme by explants of human bronchial mucosa from normal subjects and from patients with chronic bronchitis. These effects were compared with the effects of VIP on the discharge of labeled macromolecules (analyzed by quantitative autoradiography) from mucous and serous cells of the airway submucosal glands. In explants of 9 mucosal specimens of normal airways, VIP (10 ng to 1 micrograms/ml) caused a dose-dependent inhibition of baseline and methacholine-stimulated release of both glycoconjugates and lysozyme. At a concentration (1 micrograms/ml) that caused maximal inhibition of glycoconjugate and lysozyme release, VIP also caused a small inhibition of baseline but not methacholine-induced discharge of labeled macromolecules from mucous and serous cells of the submucosal glands. In explants from 5 patients with chronic bronchitis, VIP did not inhibit baseline or methacholine-stimulated glycoconjugate release and mucous or serous cell discharge, even at doses greater than 1 micrograms/ml. By contrast, VIP did inhibit baseline and methacholine-stimulated release of lysozyme, but this was less marked than in explants of normal airways. In view of the proximity of neurons containing VIP to submucosal gland cells, this study supported the hypothesis that VIP may contribute to the neurohumoral regulation of mucus secretion by the human airway. It was evident, however, that the effects of VIP could not be accounted for in terms of inhibiting cell discharge alone. In chronic bronchitis, the reduction or absence of sensitivity to VIP inhibition suggests a functional difference in the regulation of mucus secretion, which may contribute to mucus hypersecretion.

Topics: Bronchi; Bronchitis; Culture Techniques; Exocrine Glands; Female; Gastrointestinal Hormones; Humans; Macromolecular Substances; Male; Methacholine Compounds; Middle Aged; Mucus; Muramidase; Vasoactive Intestinal Peptide

Topics: Acute Disease; Bronchi; Bronchiectasis; Bronchitis; Child; Child, Preschool; Chronic Disease; Humans; Immunoglobulin A; Immunoglobulin A, Secretory; Immunoglobulin G; Immunoglobulin M; Immunoglobulins; Infant; Lactoferrin; Muramidase; Pneumonia, Staphylococcal

Serum angiotensin-converting enzyme (ACE) activity was studied in healthy controls, in 57 untreated sarcoidosis patients, and in 164 patients with other chest or lymph node diseases. The serum ACE activity of healthy persons was independent of sex, intake of meals, and smoking habits. There were no diurnal variations. Healthy children had a significantly higher ACE mean value than adults, whose ACE activity was not affected by age. The sarcoidosis patients had the highest ACE mean values, but those of patients with silicosis and asbestosis were also significantly elevated. Pulmonary cancer patients had decreased serum ACE activity, which was probably due to antimitotic treatment. Serum lysozyme (LZM) concentrations did not correlate with normal ACE activity, but the correlation between elevated ACE and LZM was significant in sarcoidosis and silicosis, and the trend was clearly the same for asbestosis. This indicates separate sources for these enzymes when ACE activity is normal, and a common source, i.e. macrophages, when ACE activity is increased. ACE production in certain diseases involving macrophages may be due to the bradykinin inhibiting effect of this enzyme.

Topics: Adolescent; Adult; Alveolitis, Extrinsic Allergic; Asbestosis; Bronchitis; Female; Hodgkin Disease; Humans; Lung Diseases; Lung Neoplasms; Lymphatic Diseases; Lymphoma; Male; Middle Aged; Muramidase; Peptidyl-Dipeptidase A; Pneumonia; Pulmonary Fibrosis; Sarcoidosis; Silicosis; Thoracic Neoplasms; Tuberculosis, Lymph Node; Tuberculosis, Pulmonary

Bronchial secretions from 207 children suffering from various pulmonary diseases and from 15 healthy controls were tested concentration of IgA, IgG, lactoferrin and lysozyme. The results obtained suggest that in many cases of chronic lung diseases in children the levels of lactoferrin and immunoglobulins, especially secretory IgA, are very low. In severe infections (cystic fibrosis, bronchiectases) significant increase of IgG concentration was observed.

Topics: Adolescent; Bronchi; Bronchiectasis; Bronchitis; Child; Child, Preschool; Chronic Disease; Cystic Fibrosis; Humans; Immunoglobulin A; Immunoglobulin A, Secretory; Immunoglobulin G; Lactoferrin; Lactoglobulins; Muramidase; Recurrence; Respiratory Tract Diseases; Respiratory Tract Infections

The concentration of immunoglobulins, lactoferrin and lysozyme we compared in bronchial secretions obtained from children with various chronic lung diseases. The IgG, lactoferrin and lysozyme, but not secretory IgA, concentrations were shown to be increased during chronic inflammatory response.

Topics: Adolescent; Bronchi; Bronchiectasis; Bronchitis; Bronchography; Bronchoscopy; Child; Child, Preschool; Chronic Disease; Cystic Fibrosis; Humans; Immunoglobulin A; Immunoglobulin A, Secretory; Immunoglobulin G; Lactoferrin; Lactoglobulins; Muramidase; Respiratory Tract Diseases

Topics: Bronchitis; Child; Chronic Disease; Humans; Immunity; Immunity, Innate; Immunoglobulin A; Immunoglobulin G; Muramidase; Respiratory System

Topics: Bronchitis; Humans; Immunoglobulin A; Immunoglobulin G; Muramidase; Sputum

Topics: Adult; Aged; Bronchi; Bronchitis; Chronic Disease; Complement System Proteins; Humans; Male; Middle Aged; Muramidase; Properdin

The concentrations of nine plasma proteins were determined by quantitative immunoelectrophoresis in sputum specimens from 29 patients with cystic fibrosis (CF) and from 24 patients with severe asthma and chronic bronchitis. The results suggested that the population of CF patients could be divided into two groups in spite of an absence of difference in clinical status between the groups. Average concentrations of seven plasma proteins in sputum of group I CF patients were identical with those in sputum of patients with bronchitis, but the average concentrations of six of these proteins in sputum from group II CF patients were higher than those in specimens from the bronchitic patients and were similar to corresponding concentrations in sputum from patients with asthma, all of whom were examined while in status asthmaticus. The average concentrations of 14 secretory proteins were the same in all sputum specimens whether or not they were produced by patients with cystic fibrosis, asthma or bronchitis. It was concluded that the concentrations in the bronchopulmonary secretions of proteins associated with host defence were not diminished in patients with cystic fibrosis, and failure to produce adequate concentrations of proteins with antimicrobial activity was unlikely to be responsible for the above average susceptibility to chest infection in cystic fibrosis. It is suggested that there exists a group of CF patients in whom a pulmonary allergic reaction generates an inflammatory response as severe as that characterizing status asthmaticus and that this response could be detrimental.

Topics: Adult; Aged; Albumins; Asthma; Beta-Globulins; Blood Proteins; Bronchitis; Child; Child, Preschool; Cystic Fibrosis; Female; Glycoproteins; Haptoglobins; Humans; Immunoelectrophoresis; Immunoglobulin A; Immunoglobulin G; Lactoferrin; Male; Middle Aged; Muramidase; Sputum; Transferrin

Topics: Air Sacs; Animals; Arginine; Bacteriophages; Blood; Bronchitis; Chick Embryo; Culture Media; Embryo, Mammalian; Embryo, Nonmammalian; Female; Horses; Hydrogen-Ion Concentration; Methods; Muramidase; Mycoplasma; Mycoplasma Infections; Poultry Diseases; Turkeys; Virulence; Vitelline Membrane

Topics: Agammaglobulinemia; Age Factors; Bacterial Infections; Bronchitis; Child, Preschool; Chronic Disease; Complement System Proteins; Humans; Immunoglobulin A; Immunoglobulin G; Infant; Muramidase; Virus Diseases

Topics: Amylases; Animals; Bronchitis; Calcium; Chemical Precipitation; Chromatography, Gel; Chronic Disease; Colostrum; Glycoproteins; Glycosaminoglycans; Goats; Humans; Immunoelectrophoresis; Immunoglobulin A; Iron; Milk, Human; Muramidase; Peroxidases; Proteins; Rabbits; Saliva; Sputum; Ultracentrifugation

Topics: Bradykinin; Bronchi; Bronchial Spasm; Bronchitis; Chromatography; Cystic Fibrosis; Expectorants; Globulins; Glycoproteins; Humans; Immunoelectrophoresis; Immunoglobulin A; Immunoglobulin G; Infections; Mucins; Muramidase; Saliva; Sputum

Topics: Adolescent; Adult; Aerosols; Aged; Airway Obstruction; Ampicillin; Bronchial Spasm; Bronchitis; Chloramphenicol; Chronic Disease; Cough; DNA; Expectorants; Glycosaminoglycans; Humans; Immunoglobulin G; L-Lactate Dehydrogenase; Middle Aged; Muramidase; Potassium Iodide; Respiratory Function Tests; Sputum

Topics: Bronchi; Bronchitis; Chronic Disease; Humans; Immunity; Immunoglobulins; Interferons; Mucous Membrane; Muramidase; Opsonin Proteins; Phagocytosis; Properdin; Sputum

Topics: Adult; Aged; Asthma; Blood Proteins; Bronchitis; Carbohydrates; Chronic Disease; Diagnosis, Differential; Electrophoresis; Female; Globulins; Glycoproteins; Haptoglobins; Heart Failure; Humans; Hydrogen-Ion Concentration; Immunoglobulin A; Immunoglobulin G; Lung Diseases; Macroglobulins; Male; Middle Aged; Muramidase; Sputum; Transferrin; Trypsin Inhibitors; Ultracentrifugation

Topics: Anti-Bacterial Agents; Bronchitis; Chronic Disease; DNA; gamma-Globulins; Glycoproteins; Humans; Immunoglobulins; L-Lactate Dehydrogenase; Muramidase; Pseudomonas; Sputum

Topics: Adolescent; Anti-Bacterial Agents; Anti-Inflammatory Agents; Blood Sedimentation; Bronchitis; Child; Child, Preschool; Female; Humans; Male; Muramidase; Paranasal Sinuses; Radiography; Sinusitis

Topics: Antitussive Agents; Bronchitis; Chronic Disease; Humans; Male; Middle Aged; Muramidase; Tetracycline

Topics: Adult; Antineoplastic Agents; Antitoxins; Bacillus; Bronchitis; Chronic Disease; Complement System Proteins; Humans; Leukocytes; Male; Middle Aged; Mining; Muramidase; Phagocytosis; Polysaccharides, Bacterial; Respiratory Function Tests; Serratia marcescens; Sputum; Staphylococcus; Stimulation, Chemical; Streptococcus; Streptococcus pneumoniae; Yeasts

Topics: Agammaglobulinemia; Asthma; Bronchitis; Chronic Disease; Cystic Fibrosis; Humans; Marfan Syndrome; Muramidase

Topics: Asthma; Bronchitis; Chlorides; Chronic Disease; Electrophoresis; Glycoproteins; Humans; Hydrogen-Ion Concentration; Immunoelectrophoresis; Molecular Weight; Muramidase; Phosphates; Potassium; Sodium; Sputum

Topics: Bronchitis; Chromatography, Gel; Cysteine; Electrophoresis; gamma-Globulins; Glycoproteins; Humans; Immunoelectrophoresis; Kallikreins; Mucins; Muramidase; Neuraminidase; Nucleic Acids; Proteins; Sputum; Transferrin; Trypsin; Viscosity

Topics: Bronchitis; Chronic Disease; Glycosaminoglycans; Humans; Muramidase; Sputum; Viscosity

Topics: Alpha-Globulins; Beta-Globulins; Bronchitis; Chemistry Techniques, Analytical; Chromatography, Ion Exchange; Electrophoresis; Humans; Immunoelectrophoresis; In Vitro Techniques; Mucus; Muramidase; Proteins; Sputum

Topics: Bronchitis; Chloramphenicol; Humans; Infant; Influenza, Human; Muramidase; Orthomyxoviridae; Orthomyxoviridae Infections; Rhinitis; Streptomycin; Tracheitis