Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0149514 (bronchitis)
 6,902 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Eosinophilic bronchitis and desquamation of the bronchial mucosa are the salient features of the pathology of both allergic (extrinsic) and nonallergic (intrinsic) asthma. Because of this association, the possibility of the eosinophil being the cause of the injury to the bronchial mucosa has been investigated during the last decade. In vitro, eosinophil granule major basic protein (MBP) concentrations as low as 10 micrograms.ml-1 cause desquamation and destruction of the epithelium of the airways which mimic the morphology of damage to the mucosa of the bronchi in asthma. Concentrations of MBP in the cytotoxic range for the bronchial mucosa in vitro have been measured in sputum of asthmatics (up to 92 micrograms.ml-1) and decline with treatment. Deposits of MBP have been detected by immunofluorescence within ulcerated areas of bronchial mucosa and necrotic portions of the bronchial wall in patients who had died of asthma. Most recently, the eosinophil peroxidase (EPO) and the eosinophil cationic protein (ECP) have also been found to be toxic for the epithelium of the airways in vitro, thus increasing the cytotoxic capability of the eosinophil against the bronchial mucosa in asthma. These latest research data continue to support the "eosinophil hypothesis" in the pathogenesis of this disease. According to this hypothesis, in the formidably complex network of cells and mediators responsible for the bronchial obstruction, the destruction of the mucociliary apparatus and the characteristic hyperresponsiveness of the airways in asthma; the eosinophil is the principal effector cell. In bronchial asthma a T cell modulated eosinophilic bronchitis is the primary abnormality while bronchospasm and hyperreactivity of the airways are secondary phenomena.
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PMID:The eosinophilic injury to the mucosa of the airways in the pathogenesis of bronchial asthma. 195 9

Common Whatman filter paper grade 1 and nitrocellulose membrane were compared for their sensitivity in a dot-immunobinding assay for detection of serum antibody titers to Arkansas avian infectious bronchitis virus (AIBV). For a blue to purple color detection, serum antibodies were bound to AIBV antigen adsorbed on the filter-paper discs or nitrocellulose membrane. Rabbit anti-chicken IgG horseradish-peroxidase (HRP) conjugate and hydrogen peroxide with 4-chloro-1-naphthol (HRP-color development reagent) were applied. The study indicates that very small amounts of antigen/antisera are needed for the dot-immunobinding assay. The test is sensitive, economical, and easy to run and can be completed within 6-8 hours.
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PMID:A dot-immunobinding assay for infectious bronchitis virus. 283 14

High levels of nonspecific background absorbance and increased variability were found in a previously optimized enzyme-linked immunosorbent assay (ELISA) for infectious bronchitis virus (IBV) antibody after changing to commercially available non-pathogen-free eggs for viral antigen production. An increase in bound viral antigen in the assay caused a proportionate increase in the nonspecific binding of the conjugate, independent of other variables, in the absence of serum. Virus was propagated in non-pathogen-free eggs, and individual viral proteins were separated by polyacrylamide gel electrophoresis and transferred to nitrocellulose. Localization of chicken IgG-virus complexes were identified by immunoprecipitation with peroxidase-conjugated anti-chicken IgG. Specific staining at molecular weights corresponding to major proteins of IBV was demonstrated in these viral preparations. Virus grown in specific-pathogen-free eggs and treated in the same manner showed only slight amounts of staining. This evidence suggests that viral antigens grown in eggs from a non-pathogen-free flock bind with maternal chicken immunoglobulins present in the allantoic cavity of eggs. This IgG caused nonspecific reactions in our chicken ELISA system and gives cause for concern in any diagnostic system requiring the propagation of agents in fertile eggs.
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PMID:Nonspecific reactions in an enzyme-linked immunosorbent assay caused by binding of immunoglobulins in situ to egg-propagated infectious bronchitis virus. 301 1

We studied correlation between airway hyper-responsiveness induced by local exposure to a macrophage inductor Broncho-Vaxom and the development of airway inflammation in dogs. To detect airway inflammation, bronchoalveolar lavage and biopsy of airway mucosa were performed. The airway responsiveness was registered by capnograph measuring gas-exchange disturbances during obstructive reactions provocated by inhalation of various concentrations of acetylcholine aerosol. Broncho-Vaxom generated a protracted airway inflammation characterized by a slight and reversible increase in the number of neutrophils at 24 h after induction, and by a long-lasting influx of macrophages peaked about at the second week. The number of macrophages turned to initial levels 3 weeks later. Macrophages migrating to the bronchoalveolar surface were activated because peroxidase positivity and bearing C3b receptors of these cells increased gradually during the inflammatory process. Airway responsiveness measured at 3, 6 and 24 h after induction did not differ significantly from baseline values, but hyper-responsiveness was developed at 96 h using 0.5 and 1.0% acetylcholine aerosol (p less than 0.01 and p less than 0.001) during the non-purulent, macrophage-mediated inflammation. This situation modelled by Broncho-Vaxom induction is very similar to those observed in children with recurrent obstructive bronchitis. The results suggest that a macrophage-mediated inflammation caused by antigens, infections or pollutants may generate a long-lasting airway hyper-responsiveness.
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PMID:Effect of experimental airway inflammation on bronchial hyper-responsiveness induced by Broncho-Vaxom in dogs. 326 65

Horseradish peroxidase-conjugated goat anti-ostrich IgG was raised and used in commercial enzyme-linked immunosorbent assay kits to detect antibodies reactive with 11 poultry pathogens in sera from 149 ostriches from nine farms around Zimbabwe. Antibodies were detected to turkey rhinotracheitis virus (99%), Newcastle disease virus (23%), avian reovirus (19%), infectious bursal disease virus (15%), avian encephalomyelitis virus (15%), Mycoplasma gallisepticum and/or M. synoviae (11%), reticuloendotheliosis virus (10%), Salmonella enteritidis (8%), avian leukosis virus (3%), infectious bronchitis virus (2%), and Pasteurella multocida (< 1%). Although evidence of prior infection with turkey rhinotracheitis and newcastle disease virus was present on all farms tested, there was marked variation between farms in the prevalence of exposure to other poultry pathogens.
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PMID:A serosurvey using enzyme-linked immunosorbent assay for antibodies against poultry pathogens in ostriches (Struthio camelus) from Zimbabwe. 783 18

Monoclonal antibodies (MAb) F5 to human IgG were used for creating immunoperoxidase conjugate. MAb dissociation constant was 10(-9)M-1 and the number of binding sites 1. Enzyme immunoassay (EIA) and immunoblotting showed that MAb F5 specifically recognize conformation epitope on intact human IgG molecule but not on other human immunoglobulins or denatured IgG. The resultant peroxidase conjugate with MAb F5 was used for EIA titration of antibacterial antibodies in sera from 30 patients with pulmonary tuberculosis, 28 patients with nonspecific pulmonary diseases (bronchitis and/or asthma, pneumonia), and 12 donors. For comparison similar studies were carried out with reference commercial immunoperoxidase conjugate to human IgG(H + L) manufactured at N. F. Gamaleya Institute of Epidemiology and Microbiology. Mycobacterium tuberculosis monoantigen (mol. weight 15-18 kD), affinity isolated by antibacterial MAb S4C1G4 (alpha S4C1G4), and PPD (Batch RT 45, Stattens Seruminstitut, Denmark) were used. Sensitivity and specificity of serum antibacterial antibodies were compared. The specificity of conjugate based on MAb F5 with monoantigen alpha S4C1G4 was 78.21%, sensitivity 94.50%, while those of conjugate to human IgG(H + L) were 53.30 and 76.89%, respectively (p < 0.001). For PPD the specificity and sensitivity were 56.75 and 72.33%, respectively (conjugate with MAb F5) versus 47.67 and 62.38% for conjugate against IgG(H + L), p < 0.001. Similar values were obtained in assessment of the concentrations of antibodies to alpha S4C1G4 for MAb F5 conjugate: specificity and sensitivity 47.16 and 71.56%, respectively, versus 23.67 and 95.16% for PPD (p < 0.05). No statistically significant differences between the experimental groups were detected with IgG(H + L) conjugate. We believe that specific MAb-based conjugate to human IgG will improve the efficacy of EIA as a method for the diagnosis of pulmonary tuberculosis.
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PMID:[Improving the efficacy of tuberculosis immunodiagnosis using anti-human IgG monoclonal antibodies]. 1045 1

A wasting disease was found in 32 athymic nude rats. The rats had parotid sialoadenitis with intranuclear inclusion bodies in ductal and acinar epithelial cells. Other common lesions included bronchitis, bronchiolitis and secondary bacterial pneumonia. Less commonly, rhinitis and Harderian adenitis were seen. Intranuclear inclusions were also seen in bronchial epithelium of 1 rat, Harderian gland acini of 1 rat and laryngeal glands of 2 rats. Viral particles, averaging 45 nm in diameter, sometimes in crystalline arrays, were found in the nucleus of parotid epithelial cells. By the use of the avidin-biotin-peroxidase complex (ABC) immunoperoxidase technique, antibodies to disrupted SV40 virus (the group specific antigen of the polyomavirus (miopapovavirus) genus of the papovavirus family) reacted with intranuclear inclusions and cytoplasm of parotid epithelium and inclusions in lung and Harderian gland. The viral antigen did not cross react with antibodies to mouse polyoma, mouse K or disrupted bovine papilloma viruses.
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PMID:Papovaviral sialoadenitis in athymic nude rats. 1062 95

Airways inflammation in chronic bronchitis is thought predominantly to be a direct consequence of neutrophil recruitment and release of elastase in response to factors such as cigarette smoke. The aims of this study were to assess the role of smoking and determine whether the serum elastase inhibitor alpha1-antitrypsin (alpha1AT) influenced the process. Airways inflammation was compared between patients with chronic obstructive bronchitis with (n=39) and without (n=42) severe alpha1AT deficiency. The authors assessed the sputum concentration of the neutrophil chemoattractants interleukin-8 (IL-8) and leukotriene (LT)B4, myeloperoxidase (MPO) as a marker of neutrophil influx, neutrophil elastase activity and its natural inhibitors, alpha1AT and secretory leukoprotease inhibitor (SLPI). Finally serum alpha1AT was measured to determine the degree of protein leakage (sputum sol serum alpha1AT ratio). Compared to current smokers, the exsmokers had a lower concentration of the chemoattractant IL-8 (p<0.05) and a lower MPO concentration, although this failed to reach conventional statistical significance (p=0.06). Patients with alpha1AT deficiency had greater inflammation in the larger airways with increased LTB4 (p<0.005), MPO (p<0.001), neutrophil elastase activity (p<0.01), protein leak (p<0.001), and were found to have a lower anti-proteinase screen with both reduced sputum alpha1AT (p<0.001) and SLPI concentrations (p<0.05). The reduction in sputum interleukin-8 levels in exsmokers may decrease neutrophil influx and thus explain the slower rate of neutrophil mediated progression of lung disease compared to subjects who continue to smoke. Patients with alpha1-antitrypsin deficiency had greater inflammation suggesting that alpha1-antitrypsin plays an important role in protecting the larger airways from the inflammatory effects of elastase activity and may explain their more rapid progression of disease.
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PMID:Airways inflammation in chronic bronchitis: the effects of smoking and alpha1-antitrypsin deficiency. 1085 53

An antibody-capture enzyme-linked immunosorbent assay (ELISA) for detection of antibody to turkey coronavirus (TCV) utilizing infectious bronchitis virus (IBV) antigen was developed. Anti-TCV hyperimmune turkey serum and normal turkey serum were used as positive or negative control serum for optimization of the ELISA system. Goat anti-turkey immunoglobulin G (light plus heavy chains) conjugated with horseradish peroxidase was used as detector antibody. The performance of the ELISA system was evaluated with 45 normal turkey sera and 325 turkey sera from the field and the cutoff point was determined. Serum samples of turkeys experimentally infected with TCV collected sequentially from 1 to 63 days postinfection were applied to the established antibody-capture ELISA using IBV antigens. The optimum conditions for differentiation between anti-TCV hyperimmune serum and normal turkey serum were serum dilution at 1:40 and conjugate dilution at 1:1600. Of the 325 sera from the field, 175 were positive for TCV by immunofluorescent antibody (IFA) assay. The sensitivity and specificity of the ELISA relative to IFA test were 93.1% and 96.7%, respectively, based on the results of serum samples from the field turkey flocks using the optimum cutoff point of 0.18 as determined by the logistic regression method. The ELISA values of all 45 normal turkey sera were completely separated from that of IFA-positive sera. The ELISA results of serum samples collected from turkeys experimentally infected with TCV were comparable to that of the IFA assay. Reactivity of anti-rotavirus, anti-reovirus, anti-adenovirus, or anti-enterovirus antibodies with the IBV antigens coated in the commercially available ELISA plates coated with IBV antigens could be utilized for detection of antibodies to TCV in antibody-capture ELISA.
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PMID:Detection of antibody to turkey coronavirus by antibody-capture enzyme-linked immunosorbent assay utilizing infectious bronchitis virus antigen. 1100 96

A competitive enzyme immunoassay was developed to measure the changes in serum levels of ovotransferrin (OTF) during inflammation and infectious diseases in chickens. The assay is based on the competition of serum OTF with a fixed concentration of biotin-labeled OTF to bind to a rabbit anti-chicken transferrin antibody immobilized on microtiter wells. After several washing steps, the antibody-bound biotinylated OTF is probed with streptavidin-horseradish peroxidase conjugate (HRP) followed by a colorimetric detection of the HRP activity. The relative changes in the optical density of color are plotted against the competing concentrations of OTF with logarithmic regression to generate a standard curve that is used to determine the concentrations of OTF in unknown samples. Serum had no effect on the measurement of OTE By this method, the time course changes of serum OTF levels in 4-wk-old male broiler chickens that were subjected to inflammation by croton oil injection were measured. The results showed croton oil-induced inflammation elevated serum OTF levels at 16 hr postinjection. OTF levels reached a peak by 72 hr, remained high through 120 hr, and returned to a basal level of olive oil-injected controls by 240 hr. There were no changes in serum OTF levels at any of the above time points in olive oil-injected control chickens. For studies with poultry diseases, specific-pathogen-free (SPF) male chickens were challenged with known bacterial and viral pathogens, and serum was collected at the height of the infection, i.e., 7 days after the challenge. Compared with uninjected controls, the SPF chickens challenged with Escherichia coli, fowl poxvirus, respiratory enteric orphan virus, infectious bursal disease virus, infectious bronchitis virus, or infectious laryngotracheitis virus had higher levels of OTF in serum. Inflammation-induced changes in serum OTF levels were also evident in the changes in the density of a 65-kD band protein corresponding to OTF. These results demonstrate that serum OTF may be a nonspecific clinical marker of inflammation associated with traumatic or infectious avian diseases.
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PMID:Changes in serum ovotransferrin levels in chickens with experimentally induced inflammation and diseases. 1192 23


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