Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0032285 (pneumonia)
 54,520 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The mucosubstances of the bronchial epithelial goblet cells in non-pneumonic calves were almost exclusively sulphomucin; neutral mucin, sialomucin and sulphomucin were produced by the submucosal glands. Calves with lesions of cuffing pneumonia from which M. dispar was frequently cultured had increased numbers of epithelial goblet cells extending into the peripheral airways as far as the bronchioles. These pneumonic animals had epithelial goblet cells, some of which contained sialomucin, while in the gland a switch from neutral to acid mucosubstance in the form of increased sulphomucins and sialomucins was detected.
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PMID:A histochemical study of mucosubstances in the bovine respiratory tract with special reference to cuffing pneumonia. 59 Aug 84

Mycoplasma hyopneumoniae causes pneumonia in pigs. The effect of infection by this organism on histochemical characteristics of airway mucin within epithelial cells was studied. Seven- to 10-week-old pigs were inoculated intratracheally with M hyopneumoniae or culture broth, and lung tissues were collected from inoculated and control pigs at 2, 4, and 6 weeks after inoculation. Tissue sections were stained with periodic acid-Schiff/Alcian blue, pH 2.5 or high iron diamine/Alcian blue. Histologic features of randomly selected bronchi, bronchioles, and submucosal glands were compared in sections stained with periodic acid-Schiff/Alcian blue. Bronchial goblet cell sulfomucin and sialomucin were quantitated by image analysis of sections stained with high iron diamine/Alcian blue. Bronchi and bronchioles of infected pigs contained proportionately fewer goblet cells with mucin at all stages of infection than age-matched control pigs. Goblet cells in bronchi of infected pigs contained significantly less total mucin and sialomucin, and significantly more sulfomucin than goblet cells of control pigs. Increased sulfated mucin in bronchial goblet cells may reflect altered glycoprotein production or secretion in response to infection with M hyopneumoniae.
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PMID:Histochemical and morphologic changes of porcine airway epithelial cells in response to infection with Mycoplasma hyopneumoniae. 141 80

The sensitivity of Pneumocystis carinii detection using silver stain (Grocott method) was compared to that using the avidin-biotin-complex immunoperoxidase (IP) staining method with anti-P. carinii monoclonal antibody. Silver stain detected only cyst wall, whereas IP stained both cyst wall and trophozoites. Serial sections of formalin-fixed, paraffin-embedded autopsy lung specimens from 41 acquired immune deficiency syndrome patients in three disease categories were stained: I--premortem or autopsy diagnosis of P. carinii pneumonia (13 cases); II--history of treated P. carinii pneumonia but no P. carinii detected in autopsy tissue specimens (15 cases); and III--no clinical or autopsy evidence of P. carinii pneumonia (13 cases). Smears from 7 bronchoalveolar lavages (3 positive) and 11 induced sputa (1 positive) also were stained. All cases of P. carinii in category I were detected with equal sensitivity. P. carinii undetected by silver stain in category II and III cases and in bronchoalveolar lavages and induced sputa were not revealed by IP. Detection of trophozoites by IP did not improve sensitivity because the staining pattern was amorphous or focally granular, and thus easily confused with nonspecific staining of mucin or intracellular or free particulate material. Reliable identification of trophozoites could be made only with coexisting cyst structures. Silver staining was more advantageous because it also identified fungal infections and was faster and more cost effective than IP.
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PMID:Detection of Pneumocystis carinii. Comparative study of monoclonal antibody and silver staining. 161 17

We describe the pathologic features in surgically excised lung tissue specimens from 18 cases of allergic bronchopulmonary aspergillosis (ABPA). The main abnormalities involved bronchi and bronchioles. All cases showed bronchocentric granulomatosis (BCG), mucoid impaction of bronchi (MIB), or both. The impacted mucin of MIB contained large numbers of eosinophils and Charcot-Leyden crystals. A distinctive exudative bronchiolitis was present distal to areas of BCG in 13 cases. This lesion was characterized by filling of bronchiolar lumens with necrotic neutrophils and eosinophils in a basophilic mucinous exudate. A peribronchiolar chronic inflammatory infiltrate was seen in 15 cases; eosinophils were prominent in 10 of these cases. Foci of eosinophilic pneumonia were seen in 13 cases, and noninvasive fungal hyphae were identified in 14. We conclude that the finding of BCG or MIB, or a combination of both, especially in conjunction with tissue eosinophilia, should suggest the diagnosis of ABPA. When noninvasive fungal hyphae are also present, the changes are diagnostic of ABPA or a related allergic fungal reaction.
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PMID:Pathologic features of allergic bronchopulmonary aspergillosis. 334 88

A rare case of primary papillary adenocarcinoma of the renal pelvis is reported. A 75-year-old man was introduced to our institute because of chance hematuria. He had no history of urolithiasis or urinary tract infection. Excretory urography showed a space taking lesion at the lower position of left renal pelvis with low function. Because of advanced stage with paraaortic lymphnode invasion, simple nephrectomy followed by irradiation and systemic chemotherapy with 5-FU was done. He died of pneumonia and acute heart failure after subtotal gastrectomy for peptic ulcer four months after the nephrectomy. Excised specimen revealed papillary adenocarcinoma of the renal pelvis without mucin production. This case was the 51st case reported in the literature. A short review of the disease is also reported.
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PMID:[Primary papillary adenocarcinoma of renal pelvis: a case report and review of the literature]. 356 86

Pneumocystis carinii, an extracellular parasite thriving in the lungs of immunosuppressed mammals, is a major cause of death in AIDS patients in the USA. As a prelude to growth, the parasite adheres mostly to type I pneumocytes lining the alveolar spaces. The mechanism of adherence remains unknown, largely because of difficulties in isolating type I pneumocytes and maintaining them in vitro. As a first step to understand P. carinii adherence to its natural substrate, we developed an in situ method to directly study parasite binding to lung alveolar cells. We used formaldehyde-fixed paraffin-embedded sections of normal rat lung as substrate for adhesion. As in its binding to the lungs in vivo, P. carinii adhered preferentially to type I pneumocytes. Adherence was saturable, time and dose dependent, and selectively blocked by glycoconjugates, in particular bovine submaxillary mucin, fetuin, and asialofetuin, suggesting that it may be mediated by a lectin type of interaction. Further, IgG of rats with P. carinii pneumonia inhibited adherence, suggesting that it may react with parasite ligands involved in the recognition of type I cell receptors. Our results demonstrate the usefulness of the in situ model for studying the mechanisms of P. carinii adherence to alveolar cells. In addition, this method may be valuable for identifying neutralizing antibodies and drugs potentially useful for controlling the infection in vivo.
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PMID:A novel in situ model to study Pneumocystis carinii adhesion to lung alveolar epithelial cells. 750 75

The properties of an extracellular neuraminidase produced by a Pasteurella multocida A:3 strain that was isolated in a case of bovine pneumonia were examined during growth in a defined medium. This enzyme (isolated from concentrated culture supernatants of P. multocida A:3) was active against N-acetylneuramin lactose, human alpha-1-acid glycoprotein, fetuin, colominic acid, and bovine submaxillary mucin. Enzyme elaboration was correlated with the growth of the organism in a defined medium, with maximum quantities produced in the stationary phase. The enzyme was purified by a combination of ammonium sulfate fractionation, ion exchange on DEAE-Sephacel, and gel filtration on Sephadex G-200. The purified neuraminidase possessed a specific activity of 9.36 mumol of sialic acid released per min per mg of protein against fetuin. The enzyme possessed a pH optimum of 6.0 and a Km of 0.03 mg/ml. The P. multocida A:3 neuraminidase had a molecular weight of approximately 500,000 as estimated by gel filtration. The enzyme was stable at 4 and 37 degrees C for 3 h. Approximately 75% of the neuraminidase activity was lost within 30 min at 50 degrees C. Greater than 90% of the enzyme activity was destroyed within 10 min at temperatures of > or = 65 degrees C. The P. multocida neuraminidase does not appear to be serologically related to the Pasteurella haemolytica A1 neuraminidase since antiserum prepared against the purified P. haemolytica enzyme did not neutralize the P. multocida enzyme.
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PMID:Extracellular neuraminidase production by a Pasteurella multocida A:3 strain associated with bovine pneumonia. 772 75

In this study we have assessed the action of a novel glycoprotease, secreted by the bovine pneumonia pathogen Pasteurella haemolytica, on epitectin expressed on the surface of human laryngeal carcinoma (H.Ep.2) cells. Epitectin has been previously characterized as a high buoyant density glycoprotein of mass of over 350 kDa extensively glycosylated on serine and threonine by small oligosaccharides. Purified metabolically labeled epitectin was very effectively hydrolyzed by the glycoprotease. However, short- and long-term treatments yielded a complex mixture of products which could not be resolved by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) or column chromatography, probably because of the heterogeneity of the structure and the distribution of the saccharides. Treatment of H.Ep.2 cells with glycoprotease followed by flow cytometric analysis revealed a significant loss in the cell surface epitopes detected by the anti-epitectin Ca2 monoclonal antibody. The action of the glycoprotease on cell surface epitectin was blocked by anti-glycoprotease antisera and was absent in an extract of a glycoprotease-negative strain of P. haemolytica. When extracts of cells treated with glycoprotease for 4 h were subjected to SDS-PAGE followed by 125I-wheat germ agglutinin overlay and autoradiography, the intensity of the characteristic epitectin bands was found to be drastically reduced compared to controls. H.Ep.2 cells metabolically labeled with [3H]glucosamine were also incubated with or without the glycoprotease and the released products were fractionated and analyzed. The enzyme-released products were found to be enriched in mucin-type glycopeptides. Thus the P. haemolytica glycoprotease could be used to selectively degrade mucin glycoproteins on cancer cell surface.
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PMID:Cleavage of epitectin, a mucin-type sialoglycoprotein, from the surface of human laryngeal carcinoma cells by a glycoprotease from Pasteurella haemolytica. 817 12

KL-6, a mucin-like high-molecular-weight glycoprotein, is a serum marker indicating the disease activity of pneumonitis, such as idiopathic pulmonary fibrosis (IPF), hypersensitivity pneumonitis, and sarcoidosis. Immunohistochemical studies have shown that KL-6 is strongly expressed on Type 2 pneumocytes and also exists on epithelial cells in other organs. It has not been clarified whether the increased levels of KL-6 in sera from patients with pneumonitis are derived from the lower respiratory tract. In this study, KL-6 levels were evaluated in bronchoalveolar lavage fluid (BALF) samples from 9 healthy control subjects and 32 patients with interstitial pneumonitis. An abnormally high level of KL-6 in BALF was observed in 70% (7 of 10) of patients with IPF, 64% (9 of 14) of patients with sarcoidosis, and 100% (8 of 8) of patients with hypersensitivity pneumonitis but in none of the healthy control subjects. KL-6 levels in BALF were significantly correlated with numbers of total cells (p < 0.001), lymphocytes (p < 0.001), and neutrophils (p < 0.05) and with concentrations of albumin (p < 0.001) and total protein (p < 0.001) in BALF and, further, with serum KL-6 levels (p < 0.01). These results indicate that increased levels of serum KL-6 in patients with pneumonitis reflect the production levels of KL-6 derived from damaged or regenerating Type 2 pneumocytes in the lower respiratory tract.
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PMID:KL-6, a mucin-like glycoprotein, in bronchoalveolar lavage fluid from patients with interstitial lung disease. 836 34

The properties of an extracellular neuroaminidase produced by a Pasteurella haemolytica A1 strain (isolated from a case of bovine pneumonia) during growth in a defined medium were examined in this investigation. This enzyme, isolated from concentrated culture supernatants of P. haemolytica A1, was active against N-acetylneuramin lactose, human alpha 1-acid glycoprotein, fetuin, and bovine submaxillary mucin. Neuraminidase production paralleled bacterial growth in a defined medium and was maximal in the stationary phase of growth. The enzyme was purified to homogeneity by a combination of salt fractionation, ion-exchange chromatography on DEAE-Sephacel, and gel filtration on Sephadex G-200. These procedures yielded an enzyme preparation that possessed a specific activity of 100.62 mumol of sialic acid released per min per mg of protein against human alpha 1-acid glycoprotein. The Km value for this enzyme with human alpha 1-acid glycoprotein as the substrate was 1.1 mg/ml, and the enzyme possessed a pH optimum of 6.5. The P. haemolytica A1 neuraminidase had a molecular weight of approximately 150,000 as estimated by gel filtration and approximately 170,000 when analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The enzyme was stable at 4 degrees C for 3 h. At 37 degrees C for 3 h, 25% of enzymatic activity was lost. Approximately 55% of the enzyme activity was lost within 30 min at 50 degrees C, with greater than 70% of the enzyme activity being destroyed within 10 min at temperatures of > or = 65 degrees C.
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PMID:Neuraminidase production by a Pasteurella haemolytica A1 strain associated with bovine pneumonia. 841 46


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