Heterogeneity of the carbohydrate chains of sulfated bronchial glycoproteins isolated from a patient suffering from cystic fibrosis.

Roussel, P; Lamblin, Geneviève; Degand, Pierre

doi:10.1016/s0021-9258(19)41690-6

Cited by 135 publications

(27 citation statements)

References 29 publications

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“…In addition to genetic background, pathological conditions also alter the composition of glycoconjugates of mucins. A remarkable diversity of carbohydrate chains has been observed in mucins from patients with cystic fibrosis (Roussel et al 1975;Ramphal et al 1989), chronic bronchitis (Feldhoff et al 1979Lhermitte et al 1991), or bronchiectasis (Van Halbeek et al 1988. Although the association of chronic obstructive pulmonary disease with the ␣ 1 -anti-trypsin gene has been established, the associations of pulmonary diseases and lung function with other genetic risk factors, including glycosyltransferases for synthesis of histo-blood group antigens, were also suggested (Springer 1970;Raza et al 1991;Ramphal et al 1991;Kauffmann et al 1996;Scharfman et al 1996;Sandford et al 1997;Weimann et al 1998).…”

Section: Discussionmentioning

confidence: 99%

Distribution of H Type 1–4 Chains of the ABO(H) System in Different Cell Types of Human Respiratory Epithelium

Fujitani

Liu

Okamura

et al. 2000

J Histochem Cytochem.

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We used three anti-H monoclonal antibodies (MAbs) specific for H Type 1, H Type 2, and H Type 3/4 antigens to investigate the distribution of H Type 1-H Type 4 chains of the ABO(H) histo-blood group in the human respiratory system. Strong staining of H Type 1 chain and weak staining of H Type 2 chain were observed in mucous cells of submucosal glands of bronchial epithelium, which were dependent on the secretor status. No H Type 3/4 chains were detected in mucous cells. Serous cells of submucosal glands of respiratory system showed no staining by three anti-H antibodies. H Type 1 and H Type 3/4 antigens were detected heterogeneously in apical surfaces of bronchial epithelium from secretors but not from nonsecretors. In contrast, basal cells of bronchial epithelium expressed H Type 2 irrespective of the secretor status, probably regulated by the H gene. Some alveolar Type II cells contained only H Types 3/4, which were dependent on the secretor status, whereas alveolar Type I cells had no H antigens. Our results indicated that different cell types in respiratory epithelium expressed different types of carbohydrate chains of histo-blood group antigens under the control of the H or the Se gene.

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Section: Discussionmentioning

confidence: 99%

Distribution of H Type 1–4 Chains of the ABO(H) System in Different Cell Types of Human Respiratory Epithelium

Fujitani

Liu

Okamura

et al. 2000

J Histochem Cytochem.

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“…To obtain mucin preparations in as nearly native form as possible, solubilization with 0.22 M potassium thiocyanate was used, as it is known to provide mucin preparations which are Theologically active (Khan et al, 1976, Brown et al, 1981. In several previous studies, however, reduction of the disulfide bonds and subseuqnt alkyltion of the free thiol groups have been used to solubilize the bronchial mucus secretions (Boat et al, 1976;Roussel et al, 1975;Roberts, 1974Roberts, , 1976Havez et al, 1970;Sachdev et al, 1978). However, it has not been shown whether the reduction of the disulfide bonds of the respiratory mucins affects their molecular weights and/or other physical characteristics.…”

Section: Discussionmentioning

confidence: 99%

Comparison of physicochemical properties of purified mucus glycoproteins isolated from respiratory secretions of cystic fibrosis and asthmatic patients

Chace¹,

Flux²,

Sachdev³

1985

Biochemistry

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The major nonreduced mucus glycoproteins (mucins) from sputa of cystic fibrosis (CF) and asthmatic patients have been purified to electrophoretic homogeneity and subjected to physical and chemical characterization. The sputum specimens were solubilized in buffer containing 0.22 M KSCN and fractionated on Bio-Gel A-5m, followed by digestion with DNase, rechromatography on the same column, and chromatography on hydroxylapatite. Sodium dodecyl sulfate gel electrophoresis of purified mucins gave a single band. Carbohydrate analyses of the purified mucins showed no significant differences in the sugar components from the two mucins. However, the CF mucin contained substantially higher (11%) sulfate content than that observed for the asthmatic mucin (5.9%). Amino acid analyses indicated that the CF mucin had higher levels of serine plus threonine (35%) as compared to the asthmatic mucin (29%). In contrast, CF mucin contained a lower content of aspartate, glutamate, and glycine than that observed for the asthmatic mucin. Molecular weights of 3.8 X 10(6) and 3.5 X 10(6) were obtained for CF and asthmatic mucins, respectively, from light-scattering studies of mucins in the presence of 6 M guanidine hydrochloride. Reduction of the disulfide bonds of the two mucins did not alter their molecular weights. Liquid chromatographic studies on Sepharose CL2B showed that CF mucin forms aggregates sufficiently large to be excluded from the gel. As compared to the CF mucin, the asthmatic mucin formed fewer of these large aggregates under identical experimental conditions. Reduction and alkylation of the mucins resulted in their inability to form aggregates. The higher state of aggregation of CF mucin may influence the viscoelastic properties of the CF lung's mucus secretions.

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“…This macromolecule has binding domains for passive clearance of both protein and lipid and may also function as a ligand (via its saccharides) for cell surface receptors of microorganisms. Many previous studies have focused on the mucin isolated from the bronchial secretions of patients with cystic fibrosis or asthma (Chernick & Barbero, 1959;Feldhoff et al, 1979;Lamblin et al, 1977;Rose et al, 1979;Roussel et al, 1975) or normal individuals tThis work was supported in part by U.S. Public Health Service Grant HL28650.…”

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confidence: 99%

Structure of canine tracheobronchial mucin glycoprotein

Ringler¹,

Selvakumar²,

Woodward³

et al. 1987

Biochemistry

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Canine tracheal mucin glycoprotein was isolated from beagle dogs fitted with tracheal pouches. Following exclusion chromatography on Sepharose CL-4B, noncovalently associated proteins were further resolved by dissociative density gradient centrifugation in CsBr-guanidinium chloride, and the mucin was then extracted with chloroform-methanol. The delipidated high-density product obtained had a nominal molecular weight of about 10(6) and an overall composition characteristic for a mucin glycoprotein, viz., a high content of serine and threonine, about 80% carbohydrate by weight, the absence of mannose or uronic acid, measurable ester sulfate, and a Pronase-resistant domain of molecular weight (1.75-3.0) X 10(5) which contains essentially all of the saccharide residues. Noncovalently bound lipid amounted to 6-10% by weight and was primarily cholesterol and cholesteryl esters. Cleavage of disulfide bonds by performic acid oxidation resulted in the release of a protein (Mr 65,000) not otherwise resolved by sodium dodecyl sulfate gel electrophoresis or the purification scheme.

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Heterogeneity of the carbohydrate chains of sulfated bronchial glycoproteins isolated from a patient suffering from cystic fibrosis.

Cited by 135 publications

References 29 publications

Distribution of H Type 1–4 Chains of the ABO(H) System in Different Cell Types of Human Respiratory Epithelium

Distribution of H Type 1–4 Chains of the ABO(H) System in Different Cell Types of Human Respiratory Epithelium

Comparison of physicochemical properties of purified mucus glycoproteins isolated from respiratory secretions of cystic fibrosis and asthmatic patients

Structure of canine tracheobronchial mucin glycoprotein

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