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Mucins and their O-Glycans from human bronchial epithelial cell cultures

¹Department of Medical Biochemistry, Göteborgs universitet, 405 30 Gothenburg, Sweden; ²Proteome Systems, Locked Bag 2073, Sydney, New South Wales 1670, Australia; and ³Cystic Fibrosis/Pulmonary Research and Treatment Center, ⁴Department of Cell and Molecular Physiology, and ⁵Department of Biochemistry and Biophysics, University of North Carolina, Chapel Hill, North Carolina 27599

Submitted 24 March 2004 ; accepted in final form 9 June 2004

A longstanding question in obstructive airway disease is whether observed changes in mucin composition and/or posttranslational glycosylation are due to genetic or to environmental factors. We tested whether the mucins secreted by second-passage primary human bronchial epithelial cell cultures derived from noncystic fibrosis (CF) or CF patients have intrinsically different specific mucin compositions, and whether these mucins are glycosylated differently. Both CF and non-CF cultures produced MUC5B, predominantly, as judged by quantitative agarose gel Western blots with mucin-specific antibodies: MUC5B was present at 10-fold higher levels than MUC5AC, consistent with our previous mRNA studies (Bernacki SH, Nelson AL, Abdullah L, Sheehan JK, Harris A, William DC, and Randell SH. Am J Respir Cell Mol Biol 20: 595–604, 1999). O-linked oligosaccharides released from purified non-CF and CF mucins and studied by HPLC mass spectrometry had highly variable glycan structures, and there were no observable differences between the two groups. Hence, there were no differences in either the specific mucins or their O-glycans that correlated with the CF phenotype under the noninfected/noninflammatory conditions of cell culture. We conclude that the differences observed in the mucins sampled directly from patients are most likely due to environmental factors relating to infection and/or inflammation.

cystic fibrosis; obstructive airway disease; mucus overproduction

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