Biochemical Exploration of Bronchial Hypersecretions

Havez, R; Roussel, P; Degand, Pierre; Randoux, A; Biserte, G

doi:10.1016/b978-0-08-013348-5.50048-x

Cited by 6 publications

(9 citation statements)

References 22 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…3) and analysis of different sections of this peak indicates that the glycoprotein components show a continuous variation with respect to their sugar and sulphate content rather than a discrete population of different glycoproteins. This result differs from the observations of Havez and co-workers [42,44] that three separate groups of glycoproteins are present in sputum, namely neutral glycoproteins, sialoglycoproteins and sulphoglycoproteins. Whereas the present investigation does indicate that small amounts of neutral glycoprotein may be present it is difficult to eliminate the possibility that this did not arise as a result of the action of neuraminidase on a sialoglycoprotein since it is known that saliva, which is a contaminant of sputum, does contain an active neuraminidase [51].…”

Section: Discussioncontrasting

confidence: 56%

“…Havez and co-workers [53] have also shown that this type of linkage is present in glycoproteins with blood group activity isolated from the sputum of patients with chronic bronchitis and bronchial carcinoma. They showed that 5 -6 serine residues and 10-12 threonine residues were destroyed per 100 amino acid residues which is in agreement with the results reported here using more extensive alkaline degradative procedures and under reductive alkaline cleavage.…”

Section: Discussionmentioning

confidence: 98%

See 1 more Smart Citation

Isolation and Characterisation of Glycoproteins from Sputum

Roberts

1974

European Journal of Biochemistry

View full text Add to dashboard Cite

Sputum has been separated into a sol and a gel phase by ultracentrifugation and the components of these phases examined. A glycoprotein of high molecular weight as well as serum albumin, immunoglobulin A, sll acid glycoprotein and lactoferrin were detected in the sol phase by gel filtration and immunodiffusion studies. A glycoprotein of similar chemical composition was isolated from the gel phase by solubilisation in 6 M urea/O. 1 M NaCl followed by fractional precipitation with ethanol.The carbohydrate content of this glycoprotein, termed the bronchial glycoprotein, varied from 58 (w/w) to 69% (w/w) with sputum from different patients and was composed of fucose, galactose, galactosamine, glucosamine and N-acetylneuraminic acid. Serine, threonine and proline constituted 44% (w/w) of the amino acid residues of the bronchial glycoprotein and an alkaline borohydride cleavage study indicated that 0-glycosidic linkages exist between N-acetylgalactosamine and the hydroxyamino acids in the peptide core. Fractionation of the bronchial glycoprotein on DEAESephadex A-25 yielded fractions enriched in sulphate and sialic acid but separate fuco, sialo and sulpho glycoproteins were not obtained. Similarly fractionation of the oligosaccharides released by the action of alkaline borohydride yielded a complex mixture of oligosaccharides but sulphated oligosaccharides free of sialic acid were not obtained. Separation of the oligosaccharides into two fractions of different sizes showed that sulphate content was greatest in the larger oligosaccharides whereas sialic acid content was highest in the smaller oligosaccharides. A methylation study of the bronchial glycoprotein, neuraminidase-digested bronchial glycoprotein and mild acid-hydrolysed bronchial glycoprotein revealed that the N-acetylneuraminic acid was linked to C-3 of penultimate galactose units. Fucose occurs in three different linkages, approximately 50 % is linked to C-2 of penultimate galactose units, approximately 25 % is linked to C-4 of glucosamine residues already substituted at

show abstract

Section: Discussioncontrasting

confidence: 56%

Section: Discussionmentioning

confidence: 98%

Isolation and Characterisation of Glycoproteins from Sputum

Roberts

1974

European Journal of Biochemistry

View full text Add to dashboard Cite

show abstract

“…LM-gel contains several components-mainly mucin glycoproteins (MGPs) and a series of lower molecular weight proteins (Havez et al, 1968;Roberts, 1974;Roussel et al, 1975;Boat et al, 1976;Feldhoff et al, 1976;Creeth et al, 1977;Rose et al, 1979). Whether these components are capable of forming a gel when separated from one another has not previously been clarified (Roberts, 1976).…”

mentioning

confidence: 99%

Resolution of the major components of human lung mucosal gel and their capabilities for reaggregation and gel formation

Rose¹,

Lynn²,

Kaufman³

1979

Biochemistry

View full text Add to dashboard Cite

“…Since proteinases in the C F LM-gel samples fragmented radiolabeled tracheobronchial mucin In vitro (Fig. 4), proteinases in LM-gel samples from pathological airways may account for the variations in molecular weight, solubility, and chromatographic behavior reported for tracheobronchial mucins (6,(37)(38)(39)(40)(41)(42)(43)46). This study has also demonstrated that TBM from healthy individuals exhibited physical and chemical properties similar to those of TBM from a patient with bronchial asthma (5).…”

Section: Discussionmentioning

confidence: 59%

“…4 B and C) were similar to K., values on Sepharose 4B of TBM glycopeptide generated by proteolytic enzymes (37)(38)(39). 4) The cysteine contents of the CF lung mucins analyzed were considerably lower than those of normal and asthmatic mucins, and similar to values obtained on analysis of the proteolytically-digested glycopeptide fragments of asthmatic mucin (39,40). However, considerable variability in the cysteine concentrations of tracheobronchial mucins has been reported (5,6,33,(38)(39)(40)(41)(42)(43) and cysteine is often not measured quantitively as it requires almost a mg of purified mucin for accurate measurements in duplicate.…”

Section: Discussionmentioning

confidence: 97%

Biochemical Properties of Tracheobronchial Mucins from Cystic Fibrosis and Non-Cystic Fibrosis Individuals

et al. 1987

View full text Add to dashboard Cite

ABSTRACT. Tracheobronchial mucins from healthy individuals and from patients with bronchial asthma or cystic fibrosis (CF) were isolated from lung mucus, purified, and their chemical and physical properties compared. Normal and asthmatic mucins required both a dissociating and a reducing agent for solubilization and exhibited identical chromatographic behavior on Sepharose 4B, Sepharose 2B, and hydroxylapatite and similar amino acid and carbohydrate compositions. In contrast, 1) C F lung mucins were solubilized in the absence of dissociating and/or reducing agents and 2) the majority of the C F mucins analyzed was eluted in the included volume of Sepharose 4B with K. , values of 0.3 + 0.1 rather than in the void volume and thus appeared smaller than normal and asthmatic mucins. The lower molecular weight mucins in C F sputum apparently are produced by bacterial or inflammatory cell proteinases since radiolabelled asthmatic mucin was digested to smaller fragments when incubated with crude C F lung mucosal samples. Furthermore, mucins secreted by tracheal explants from C F and from non-CF individuals eluted in the void volume on Sepharose 4B, suggesting that CF tracheobronchial mucins were not inherently smaller than non-CF mucins. (Pediatr Res 22: 545-551, 1987 mucus of exocrine glands or epithelial tubular systems of the respiratory, gastrointestinal, and reproductive tracts (2) which is the basis for the generally held assumption that C F mucus is "abnormal." Since mucus glycoproteins (mucins) are the macromolecules responsible for the viscoelastic properties of mucus (3-5), alterations in mucin structure could effect the physiological behavior of mucus.To date, the most comprehensive studies on C F mucins (6-8) have utilized TBM isolated from C F sputum as copious amounts of such material are readily available. There is limited information available on TBM from healthy airways primarily because of the difficulties in obtaining sufficient amounts of adequate material for analysis. Thus, insufficient information currently exists to determine whether C F and non-CF mucins are different (see Ref. 9 for review) although available studies suggest differences in sulfation of C F respiratory tract mucins (10). However, recent studies have suggested that TBM from healthy airways exhibit physical properties (size, chromatographic behavior on molecular sieving, solubility) different than those of mucins from pathological airways (I I-13). While isolating and purifying human mucins from normal and pathological mucus, we obtained results that indicated that C F TBM were considerably more heterogeneous and smaller in size than non-CF TBM. The smaller size of C F mucins in the samples analyzed could result from in vivo proteolysis, as C F airways are chronically infected with pathogens that produce proteinases (14, 15) and both C F sputum and bronchial washings contain high levels of extracellular proteinase activity (1 6-18). Alternatively, the smaller mucins could reflect inherent differences in C F mucins. These possibili...

show abstract

Biochemical Exploration of Bronchial Hypersecretions

Cited by 6 publications

References 22 publications

Isolation and Characterisation of Glycoproteins from Sputum

Isolation and Characterisation of Glycoproteins from Sputum

Resolution of the major components of human lung mucosal gel and their capabilities for reaggregation and gel formation

Biochemical Properties of Tracheobronchial Mucins from Cystic Fibrosis and Non-Cystic Fibrosis Individuals

Contact Info

Product

Resources

About