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1 Department of Medical Biochemistry, Goteborg University, Gothenburg, Sweden
2 Proteome Systems Ltd, Sydney, NSW, Australia
3 Cystic Fibrosis/Pulmonary Research and Treatment Center, University of North Carolina, Chapel Hill, NC, USA
4 Cystic Fibrosis/Pulmonary Research and Treatment Center, University of North Carolina, Chapel Hill, NC, USA; Department of Cell and Molecular Physiology, University of North Carolina, Chapel Hill, NC, USA
5 Cystic Fibrosis/Pulmonary Research and Treatment Center, University of North Carolina, Chapel Hill, NC, USA; Department of Biochemistry and Biophysics, University of North Carolina, Chapel Hill, NC, USA
* To whom correspondence should be addressed. E-mail: cwdavis{at}med.unc.edu.
A longstanding question in obstructive airways disease is whether observed changes in mucin composition and/or post-translational glycosylation are due to genetic or to environmental factors. We tested whether the mucins secreted by second passage primary human bronchial epithelial (HBE) cell cultures derived from non-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 (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 non-inflammatory conditions of cell culture. We conclude that the differences observed in the mucins sampled directly from patients is most likely due to environmental factors relating to infection and/or inflammation.
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