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

Rose, Mary C.; Lynn, William S.; Kaufman, Bernard

doi:10.1021/bi00585a029

Cited by 63 publications

(39 citation statements)

References 26 publications

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“…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: Discussionsupporting

confidence: 54%

“…The procedures used for the solubilization and chromatographic resolution of the components of LM-gel and for the purification of tracheobronchial mucins have been described (5). Briefly, the samples were thawed, diluted with saline, homogenized, heated in a boiling 546 ROSE ET AL.…”

Section: Methodsmentioning

confidence: 99%

“…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)(4)(5), alterations in mucin structure could effect the physiological behavior of mucus.…”

mentioning

confidence: 99%

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

et al. 1987

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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...

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Section: Discussionsupporting

confidence: 54%

Section: Methodsmentioning

confidence: 99%

mentioning

confidence: 99%

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

et al. 1987

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“…These glycoproteins are normally found as a dissolved, entangled network in mucus. When dissolved in purified form, mucins have been shown to form a gel (12) and recreate the rheologic properties of mucus (1). It is for these reasons that mucins and the factors that affect their structure and expression in health and disease have been extensively studied.…”

Section: Mucus Rheologymentioning

confidence: 99%

The role of airway mucus in pulmonary toxicology.

Samet

Cheng

1994

Environ Health Perspect

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Airway mucus is a complex airway secretion whose primary function as part of the mucociliary transport mechanism is to to serve as renewable and transportable barrier against inhaled particulates and toxic agents. The rheologic properties necessary for this function are imparted by glycoproteins, or mucins. Some respiratory disease states, e.g., asthma, cystic fibrosis, and bronchitis, are characterized by quantitative and qualitative changes in mucus biosynthesis that contribute to pulmonary pathology. Similar alterations in various aspects of mucin biochemistry and biophysics, leading to mucus hypersecretion and altered mucus rheology, result from inhalation of certain air pollutants, such as ozone, sulfur dioxide, nitrogen dioxide, and cigarette smoke. The consequences of these pollutant-induced alterations in mucus biology are discussed in the context of pulmonary pathophysiology and toxicology. -Environ Health Perspect 1 02(Suppl 2): 89-103 (1994).

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“…Over the past decade, a number of laboratories have initiated characterization of the airway mucin from normal, asthmatic, chronic bronchitic, and cystic fibrosis sputa, as well as mucins from the submaxillary gland, intestine, and reproductive tract (2)(3)(4)(5)(6)(7). Much debate arises from a lack of consensus about methods of purification and criteria for purity of mucins.…”

Section: Introductionmentioning

confidence: 99%

The core polypeptide of cystic fibrosis tracheal mucin contains a tandem repeat structure. Evidence for a common mucin in airway and gastrointestinal tissue.

Gérard¹,

Eddy²,

Shows³

1990

J. Clin. Invest.

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A cystic fibrosis trachea cDNA library was constructed and probed with a synthetic oligonucleotide containing a consensus sequence recently identified in human intestinal mucin. One of the isolated clones, AMN-22, has been characterized extensively. The cDNA sequence of this 884-bp fragment was determined, and revealed a tandem repeat structure rich in threonine and proline residues. The repeating sequence of AMN-22 was similar but not identical to that determined for gut mucin.

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

Cited by 63 publications

References 26 publications

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

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

The role of airway mucus in pulmonary toxicology.

The core polypeptide of cystic fibrosis tracheal mucin contains a tandem repeat structure. Evidence for a common mucin in airway and gastrointestinal tissue.

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