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)

The concentrations of tissue-polypeptide antigen (TPA), ferritin, alpha 1-acid glycoprotein (alpha 1-aGP), transthyretin (TBPA), alpha 1-antitrypsin (alpha 1-Pi), alpha 2-macroglobulin (alpha 2-MG), C-reactive protein and IgA were determined in broncho-alveolar lavage fluid of 13 patients with chronic bronchitis and 11 with bronchial carcinoma and accompanying bronchitis. Measurement of TPA, alpha 1-Pi, ferritin and transthyretin provides useful additional information in the diagnosis of bronchial carcinoma. The ratios of TPA/TBPA, alpha 1-Pi/TBPA and alpha 1-aGP/TBPA differentiate highly sensitively between bronchial carcinoma and chronic bronchitis.
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PMID:[Bronchoalveolar lavage. The humoral parameter spectrum in bronchial carcinoma and chronic bronchitis]. 300 82

Oligonucleotide-directed mutagenesis was used to construct chimeric cDNAs that encode the extracellular and transmembrane domains of the vesicular stomatitis virus glycoprotein (G) linked to the cytoplasmic domain of either the immunoglobulin mu membrane heavy chain, the hemagglutinin glycoprotein of influenza virus, or the small glycoprotein (p23) of infectious bronchitis virus. Biochemical analyses and immunofluorescence microscopy demonstrated that these hybrid genes were correctly expressed in eukaryotic cells and that the hybrid proteins were transported to the plasma membrane. The rate of transport to the Golgi complex of G protein with an immunoglobulin mu membrane cytoplasmic domain was approximately sixfold slower than G protein with its normal cytoplasmic domain. However, this rate was virtually identical to the rate of transport of micron heavy chain molecules measured in the B cell line WEHI 231. The rate of transport of G protein with a hemagglutinin cytoplasmic domain was threefold slower than wild type G protein and G protein with a p23 cytoplasmic domain, which were transported at similar rates. The combined results underscore the importance of the amino acid sequence in the cytoplasmic domain for efficient transport of G protein to the cell surface. Also, normal cytoplasmic domains from other transmembrane glycoproteins can substitute for the G protein cytoplasmic domain in transport of G protein to the plasma membrane. The method of constructing precise hybrid proteins described here will be useful in defining functions of specific domains of viral and cellular integral membrane proteins.
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PMID:Cytoplasmic domains of cellular and viral integral membrane proteins substitute for the cytoplasmic domain of the vesicular stomatitis virus glycoprotein in transport to the plasma membrane. 301 9

The complete nucleotide sequence of cloned cDNAs containing the E2 glycoprotein-encoding region of the genome of transmissible gastroenteritis virus (TGEV) has been determined. A single large translatable frame of 4.3 kb starting at 8.2 kb from the 3' end of the genome was identified. Its deduced amino acid sequence contains the characteristic features of a coronavirus peplomer protein: the precursor polypeptide of TGEV E2 is 1447 residues long (i.e. 285 longer than the avian infectious bronchitis coronavirus spike protein); partial N-terminal sequencing demonstrated that a putative secretory signal sequence of 16 amino acids is absent in the virion-associated protein; the predicted mol. wt. of the apoprotein is 158K; most of the 32 potential N-glycosylation sites available in the sequence are presumed to be functional to account for the difference between this and the experimentally determined value (200K to 220K); a typical hydrophobic sequence near the C terminus is likely to be responsible for anchoring the peplomer to the virion envelope.
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PMID:The predicted primary structure of the peplomer protein E2 of the porcine coronavirus transmissible gastroenteritis virus. 303 11

The lateral mobility of the vesicular stomatitis virus spike glycoprotein (G protein) and various mutant G proteins produced by site-directed mutagenesis of the G cDNA has been measured. Fluorescence recovery after photobleaching results for the wild type G protein in transfected COS-1 cells yielded a mean diffusion coefficient (D) of 8.5 (+/- 1.3) X 10(-11) cm2/s and a mean mobile fraction of 75% (+/- 3%). Eight mutant proteins were also examined: dTM14, lacking six amino acids from the transmembrane domain; TA2, lacking an oligosaccharide in the extracellular domain; QN2, possessing an extra N-linked oligosaccharide in the extracellular domain; CS2, possessing a serine instead of a cysteine at residue 489 in the cytoplasmic domain, preventing palmitate addition to the glycoprotein; TMR-stop, lacking the entire cytoplasmic domain except an arginine at residue 483; and three chimeric proteins, G mu, G23, and GHA, containing in place of the 29 amino acid wild type cytoplasmic domain the cytoplasmic domains from the surface IgM from the spike protein of the infectious bronchitis virus or from the hemagglutinin protein of the influenza virus, respectively. The mean D for the mutant proteins varied over a relatively small range, with the slowest mutant, G23, exhibiting a value of 11.3 (+/- 1.4) X 10(-11) cm2/s and the fastest mutant, GHA, having a D of 28.6 (+/- 4.5) X 10(-11) cm2/s. The mean mobile fraction similarly varied over a small range, extending from 55 to 68%. None of the mutations resulted in the more rapid diffusion characteristic of membrane proteins embedded in artificial bilayers. Therefore, it appears that the cytoplasmic and transmembrane domains themselves contribute little to restraining the lateral mobility of this integral membrane protein when expressed in transfected cells.
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PMID:Effects of mutations in three domains of the vesicular stomatitis viral glycoprotein on its lateral diffusion in the plasma membrane. 303 31

Density-gradient analysis was used to follow the transition from normal to hypersecretory bronchial mucus in a model of bronchitis induced in dogs by chronic exposure to SO2 gas. Aspirates of saline bronchial lavage were obtained by fiberoptic bronchoscopy from dogs before, during a 6- to 9-month exposure period to SO2 gas, and during a recovery period of similar duration. Prior to SO2 exposure, aspirates from all animals had a low yield of nondialyzable macromolecules (15 +/- 6 mg/aspirate) and similar composition. Specifically, epithelial glycoprotein of typical buoyant density was not detected; rather a glycoconjugate of higher buoyant density with features of both proteoglycan and glycoprotein was identified. Neutral lipids were predominant with lesser amounts of phospholipids; no glycolipids were detected. During the SO2 exposure period, aspirates from five of the eight dogs contained components similar in buoyant density to human bronchitic glycoprotein. Glycoprotein isolated from the canine aspirates was similar to glycoprotein isolated from human chronic bronchitic sputum, having the same carbohydrate composition and range of oligosaccharide size. Further, during and after SO2 exposure some aspirates contained appreciable amounts of glycolipids. These data demonstrate substantial similarities in composition between normal human and canine mucus and in mucus isolated from dogs with chronic airway inflammation induced by repeated irritant exposure and from human patients with chronic bronchitis.
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PMID:Transition from normal to hypersecretory bronchial mucus in a canine model of bronchitis: changes in yield and composition. 334 78

The diseases included are those commonly called chronic bronchitis, bronchiolitis, bronchiectasis and asthma. The definitions most commonly used are those called for and applied in epidemiological studies. In this symposium, it is the role of inflammation in these various diseases that will be explored. The term bronchiectasis describes bronchial or bronchiolar distortion and scarring. It is well described by the terms bronchitis obliterans and bronchiolitis obliterans. In the 'wet' form of the disease, chronic sputum production is a feature. The factors that cause mucus hypersecretion in chronic bronchitis probably operate. Chronic bronchitis is characterized by mucus hypersecretion. Recent studies reveal that change in the nature of secretion is an early sign: new constituents appear before the amount is appreciably increased. Bronchial aspirate from normal non-smoking human volunteers, as judged by density gradient ultracentrifugation, contained no typical epithelial glycoprotein but did contain a glycoconjugate of higher buoyant density that included sugars characteristic of proteoglycans. In normal volunteers who had smoked, albeit mildly, macromolecular yield was not increased; however, a glycoconjugate of buoyant density typical of epithelial glycoprotein but with sugars characteristic of both proteoglycans and glycoprotein was identified. In simple, chronic bronchitis a typical epithelial glycoprotein can be identified. Study of the canine model of chronic bronchitis supports these findings. In organ culture, human and canine airways do not secrete the typical epithelial glycoprotein under baseline conditions but they do when stimulated, as by cholinergic agents. Analysis of lipids also yields a similar picture in human disease and in the canine model. Cholesterol is typical of normal mucus. When secretion is obviously increased, glycolipid is also present.
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PMID:The pathology of obstructive and inflammatory airway diseases. 353 90

Analysis of differentially radiolabelled avian infectious bronchitis virus (IBV) indicated that the matrix (M) polypeptides of mol. wt. 23 X 10(3) (23K), 26K, 28K, 30K and 34K (M23 to M34) which have been shown to give the same peptide maps, differed in their degree of glycosylation; M23 was not glycosylated while glycosylation increased with increasing mol. wt. from M26 to M34. Both glucosamine and mannose were components of M26 to M34 but [3H]fucose appeared to be associated mainly with M34. Endo-beta-N-acetylglucosaminidase H removed oligosaccharides from M28 and M30 but not M26 and M34, to give a polypeptide of 23K. The surface projection glycopolypeptides S1 (90K) and S2 (84K) incorporated 3H-labelled glucosamine and mannose but not fucose and had oligosaccharides removed by endoglycosidase H. The mol. wt. of the resultant polypeptides varied among experiments; the lowest mol. wt. observed were 64K and 61K. These results indicate (i) that the polypeptide moieties of the S polypeptides are approximately 64K and 61K, and 23K for the M polypeptide, (ii) that the oligosaccharides of the S and M polypeptides are of the high-mannose type and are linked to the polypeptides by N-glycosidic linkages, and (iii) that the M glycoprotein of IBV differs from that of murine coronaviruses and bovine coronavirus L9 which have O-linked oligosaccharides.
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PMID:Coronavirus IBV glycopolypeptides: size of their polypeptide moieties and nature of their oligosaccharides. 630 14

The nucleotide sequences of S1 glycoprotein genes of the Gray and JMK strains of avian infectious bronchitis virus (IBV) were determined and compared with published sequences for IBV. The IBV Gray and JMK strains had 99% nucleotide sequence similarity. The overall nucleotide sequence similarity of the Gray and JMK strains compared with other IBV strains was between 82.0% and 87.4%. The similarity of the predicted amino acid sequence for the S1 glycoproteins of the Gray and JMK strains was 98.8%. Six of the 10 differences in the amino acid sequence were found between residues 99 and 127, suggesting a possible role for that region in the tissue trophisms of the viruses. The S1 glycoprotein of the Gray and JMK strains had 79.5%-84.6% amino acid similarity with the published sequence of other IBV strains. Serine instead of phenylalanine was observed in the protease cleavage site between the S1 and S2 glycoprotein subunits for the Gray and JMK strains, which was similar to the published sequence for the Ark99 and SE17 strains. The significance of that amino acid change is not known. Based on the nucleotide sequence of the Gray and JMK strains, the BsmAI restriction enzyme was selected by computer analysis and was used in restriction fragment length polymorphism analysis to differentiate the two strains.
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PMID:Molecular cloning and sequence comparison of the S1 glycoprotein of the Gray and JMK strains of avian infectious bronchitis virus. 759 1

An antigenic variant of avian infectious bronchitis virus (IBV), a coronavirus, was isolated and characterized. This strain, CU-T2, possesses a number of unusual features, which have not been previously observed in IBV. The S1 glycoprotein of CU-T2 carries virus-neutralizing and serotype-specific epitopes of two IBV serotypes, Arkansas (Ark) and Massachusetts (Mass). Sequence analysis revealed that the virus, originally an Ark serotype, has acquired the Mass-specific epitope by mutation(s). This provides evidence that point mutations may lead to generation of IBV antigenic variants in the field. It was further observed that two independent recombination events involving three different IBV strains had occurred in the S2 glycoprotein gene and N protein gene of CU-T2, indicating that genomic RNA recombination in IBV may occur in multiple genes in nature. It was especially significant that a sequence of Holland 52 (a vaccine strain) had replaced half of the N gene of CU-T2. This proves that recombination among vaccine strains is contributing to the generation of IBV variants in the field. Based on these observations it is predicted that every IBV field isolate could have unique genetic nature. Therefore, several recently reported diagnostic and serotyping methods of IBV which are based on dot-blot hybridization, restriction fragment length polymorphism (RFLP), and polymerase chain reaction (PCR), may not reveal the true antigenic and/or genetic nature of IBV isolates, and may in fact yield misleading information.
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PMID:A novel variant of avian infectious bronchitis virus resulting from recombination among three different strains. 771 Mar 54

The S1, N and M proteins, obtained from the nephropathogenic N1/62 strain of infectious bronchitis virus (IBV) by immunoaffinity purification with monoclonal antibodies, were used for immunization of chickens. For all three antigens multiple immunizations were necessary for induction of an antibody response. Protection of chickens vaccinated with the S1 glycoprotein against virulent challenge was demonstrated by the complete absence of virus in tracheas and kidneys of vaccinated chickens. Following four immunizations with the S1 glycoprotein 71% and 86% of chickens were protected at the level of tracheas and kidneys, respectively. Three immunizations with the S1 glycoprotein protected 70% and 10% of chickens at the level of kidney and trachea, respectively. Neither the N nor the M antigen induced protection to a virulent challenge with the nephropathogenic N1/62 strain of IBV after four immunizations. Virus neutralizing, haemagglutination inhibiting and ELISA antibodies were detected in chickens immunized with the S1 glycoprotein and inactivated N1/62 virus, however there was no correlation between the presence of any of these antibodies and protection.
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PMID:The S1 glycoprotein but not the N or M proteins of avian infectious bronchitis virus induces protection in vaccinated chickens. 798 2


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