Heterogeneity of mucus glycoproteins from cystic fibrotic sputum. Are there different families of mucins?

Thornton, David J.; Sheehan, John K.; Carlstedt, Ingemar

doi:10.1042/bj2760677

Cited by 25 publications

(23 citation statements)

References 17 publications

(16 reference statements)

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“…However, the presence of two chronic bronchitic samples that did not contain the ' shoulder, ' and one ' normal ' sample that did, suggests that there is some overlap between the groups. The elution position on ion-exchange HPLC showed the glycopeptides from the major chronic bronchitic mucin to be less charged than those from the ' dense ' pool, consistent with the earlier findings from CF sputum [35].…”

Section: Figure 7 Ion-exchange Hplc Of High-molecular-mass Glycopeptisupporting

confidence: 88%

Mucins in airway secretions from healthy and chronic bronchitic subjects

Davies

Hovenberg

Lindén

et al. 1996

Biochemical Journal

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Little is known about whether the properties of respiratory mucins are altered as a result of airway irritation, but histochemical studies of respiratory tract secretory cells show a more 'acidic' staining pattern after exposure to tobacco smoke. Furthermore it has been suggested that proteoglycans are the major glycoconjugates in 'normal' respiratory secretions, whereas mucins predominate in sputum. To investigate these observations further, mucins from secretions collected from the tracheal surface of healthy non-smoking 'normal' subjects and sputum from patients with chronic bronchitis were compared. All samples contained one major mucin population after density-gradient centrifugation, and a small amount of 'denser' mucin was present in some chronic bronchitic and one of the 'normal' samples. Proteoglycans were not a major component of 'normal' secretions. The major mucin population from chronic bronchitic samples had molecular masses between 10 and 30 MDa and behaved as random coils in solution. Whole mucins from 'normal' individuals and chronic bronchitic patients were excluded from Sepharose CL-2B, whereas reduced subunits were included. Proteolysis of subunits yielded two populations of high-molecular-mass glycopeptides differing in size, suggesting the presence of two different tandem repeat regions in the mucins. Finally, mucins from patients with chronic bronchitis are less, rather than more, acidic than those from 'normal' individuals. Mucins from bronchitic sputum and 'normal' secretions are thus similar in their macromolecular properties, but differ slightly in charge density.

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Section: Figure 7 Ion-exchange Hplc Of High-molecular-mass Glycopeptisupporting

confidence: 88%

Mucins in airway secretions from healthy and chronic bronchitic subjects

Davies

Hovenberg

Lindén

et al. 1996

Biochemical Journal

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“…The respiratory syndromes commonly referred to as IAD (5,48) and RAO (formerly known as chronic obstructive pulmonary disease or COPD; Refs. 19,25,29) are both characterized by excess airway mucus and associated neutrophilic inflammation.…”

Section: Discussionmentioning

confidence: 99%

Muc5b and Muc5ac are the major oligomeric mucins in equine airway mucus

Rousseau

Kirkham²,

McKANE³

et al. 2007

American Journal of Physiology-Lung Cellular and Molecular Phys

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Horses frequently suffer from respiratory diseases, which, irrespective of etiology, are often associated with airway mucus accumulation. Studies on human airways have shown that the key structural components of the mucus layer are oligomeric mucins, which can undergo changes of expression and properties in disease. However, there is little information on these gel-forming glycoproteins in horse airways mucus. Therefore, the aims of this study were to isolate equine airways oligomeric mucins, characterize their macromolecular properties, and identify their gene products. To this end, pooled tracheal washes, collected from healthy horses and horses suffering from respiratory diseases, were solubilized with 6 M guanidinium chloride (GdmCl). The oligomeric mucins were purified by density gradient centrifugation followed by size exclusion chromatography. Biochemical and biophysical analyses showed the mucins were stiffened random coils in solution that were polydisperse in size (M(r) = 6-20 MDa, average M(r) = 14 MDa) and comprised of disulfide-linked subunits (average M(r) = 7 MDa). Agarose gel electrophoresis showed that the pooled mucus sample contained at least two populations of oligomeric mucins. Electrospray ionization tandem mass spectrometry of tryptic digests of the unfractionated mucin preparation showed that the oligomeric mucins Muc5b and Muc5ac were present. In summary, we have shown that equine airways mucus is a mixture of Muc5b and Muc5ac mucins that have a similar macromolecular organization to their human counterparts. This study will form the basis for future studies to analyze the contribution of these two mucins to equine airways pathology associated with mucus accumulation.

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“…The gel-forming mucins from the airways are large macromolecules [molecular masses of (10-30)i10' Da] composed of subunits linked end-to-end by disulphide bonds [1][2][3], and recent biochemical studies have indicated the presence of at least two different airway mucins [4]. Regions rich in serine, threonine and proline residues (STP-rich regions) alternate with stretches with a more ' conventional ' amino acid composition.…”

Section: Introductionmentioning

confidence: 99%

Different mucins are produced by the surface epithelium and the submucosa in human trachea: identification of MUC5AC as a major mucin from the goblet cells

Hovenberg

Davies

Carlstedt

1996

Biochemical Journal

260

206

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Mucins were extracted from the epithelial surface and the submucosal tissue of human trachea in order to enrich glycoproteins from the goblet cells and the submucosal glands respectively. The macromolecules were purified using density-gradient centrifugation, and the presence of the MUC5AC mucin was investigated using an antiserum raised against a synthetic peptide based on the sequence of the MUC5AC apoprotein. Mucins from the surface epithelium showed a higher reactivity with the antiserum relative to carbohydrate than those from the submucosa, and ion-exchange HPLC of reduced subunits revealed the presence of two distinct mucin populations in the samples. The predominant species from the surface epithelium was more acidic than the major population from the submucosa and showed a strong reactivity with the anti-MUC5AC anti-serum. In contrast, the major portion of the submucosal mucins were less acidic and showed no MUC5AC reactivity, although a more acidic population did react with the antibody. Rate-zonal centrifugation showed that the MUC5AC mucin from the surface epithelium is smaller than the major submucosal mucin, and that both are composed of subunits. Immunolocalization confirmed that the MUC5AC mucin from human trachea originates from the goblet cells and that this glycoprotein is not a major product of the submucosal glands.

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Heterogeneity of mucus glycoproteins from cystic fibrotic sputum. Are there different families of mucins?

Cited by 25 publications

References 17 publications

Mucins in airway secretions from healthy and chronic bronchitic subjects

Mucins in airway secretions from healthy and chronic bronchitic subjects

Muc5b and Muc5ac are the major oligomeric mucins in equine airway mucus

Different mucins are produced by the surface epithelium and the submucosa in human trachea: identification of MUC5AC as a major mucin from the goblet cells

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