In vivo glycosylation of MUC1 in airway epithelial cells

Howard S. Silverman; Mark Sutton-Smith; Paul Heal; Simon Parry; Timea Palmai-Pallag; Shih Hsing Leir; Howard R. Morris; Anne Dell; Ann Harris

doi:10.1023/B:GLYC.0000004009.24191.d3

In vivo glycosylation of MUC1 in airway epithelial cells

Howard S. Silverman, Mark Sutton-Smith, Paul Heal, Simon Parry, Timea Palmai-Pallag, Shih Hsing Leir, Howard R. Morris, Anne Dell, Ann Harris^*

^*Corresponding author for this work

Pediatrics

Research output: Contribution to journal › Article › peer-review

6 Scopus citations

Abstract

The O-glycans that decorate mucin glycoproteins contribute to the biophysical and biochemical properties of these molecules and hence their function as a barrier and lubricant on epithelial surfaces. Alterations in mucln O-glycosylation in certain diseases may contribute to pathology. It is known that both the host cell type and the amino acid sequence of the mucin tandem repeat contribute to the O-glycosylation of a mucin molecule. We expressed an epitope-tagged MUC1 mucin cDNA construct in the airway cell line 16HBE14o- and the colon carcinoma cell line Caco2 and used Fast Atom Bombardment Mass Spectrometry to evaluate the contribution of the host cell to differences in O-glycosylation of a single mucin. Many of the glycans detected on the MUC1 mucin were common to both cell types, as would be predicted from biosynthetic constraints. However, MUC1 synthesized in the airway cell line showed comparatively low levels of sialylation but carried a range of oligo-N-acetyllactosamine structures that were not seen in the colon carcinoma cell line.

Original language	English (US)
Pages (from-to)	379-384
Number of pages	6
Journal	Glycoconjugate Journal
Volume	19
Issue number	6
DOIs	https://doi.org/10.1023/B:GLYC.0000004009.24191.d3
State	Published - Jul 2002

Funding

We thank Dr. D. Greunert for the 16HBE14o-cell line and M.A. Hollingsworth for helpful discussions. This work was funded by the Cystic Fibrosis Trust, the Wellcome Trust and the Biotechnology and Biological Sciences Research Council.

Keywords

Airway epithelium
MUC1
Mucin O-glycosylation

ASJC Scopus subject areas

Molecular Biology
Biochemistry
Cell Biology

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1023/B:GLYC.0000004009.24191.d3

Cite this

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title = "In vivo glycosylation of MUC1 in airway epithelial cells",

abstract = "The O-glycans that decorate mucin glycoproteins contribute to the biophysical and biochemical properties of these molecules and hence their function as a barrier and lubricant on epithelial surfaces. Alterations in mucln O-glycosylation in certain diseases may contribute to pathology. It is known that both the host cell type and the amino acid sequence of the mucin tandem repeat contribute to the O-glycosylation of a mucin molecule. We expressed an epitope-tagged MUC1 mucin cDNA construct in the airway cell line 16HBE14o- and the colon carcinoma cell line Caco2 and used Fast Atom Bombardment Mass Spectrometry to evaluate the contribution of the host cell to differences in O-glycosylation of a single mucin. Many of the glycans detected on the MUC1 mucin were common to both cell types, as would be predicted from biosynthetic constraints. However, MUC1 synthesized in the airway cell line showed comparatively low levels of sialylation but carried a range of oligo-N-acetyllactosamine structures that were not seen in the colon carcinoma cell line.",

keywords = "Airway epithelium, MUC1, Mucin O-glycosylation",

author = "Silverman, {Howard S.} and Mark Sutton-Smith and Paul Heal and Simon Parry and Timea Palmai-Pallag and Leir, {Shih Hsing} and Morris, {Howard R.} and Anne Dell and Ann Harris",

note = "Funding Information: We thank Dr. D. Greunert for the 16HBE14o-cell line and M.A. Hollingsworth for helpful discussions. This work was funded by the Cystic Fibrosis Trust, the Wellcome Trust and the Biotechnology and Biological Sciences Research Council. Copyright: Copyright 2008 Elsevier B.V., All rights reserved.",

year = "2002",

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doi = "10.1023/B:GLYC.0000004009.24191.d3",

language = "English (US)",

volume = "19",

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AU - Silverman, Howard S.

AU - Sutton-Smith, Mark

AU - Heal, Paul

AU - Parry, Simon

AU - Palmai-Pallag, Timea

AU - Leir, Shih Hsing

AU - Morris, Howard R.

AU - Dell, Anne

AU - Harris, Ann

N1 - Funding Information: We thank Dr. D. Greunert for the 16HBE14o-cell line and M.A. Hollingsworth for helpful discussions. This work was funded by the Cystic Fibrosis Trust, the Wellcome Trust and the Biotechnology and Biological Sciences Research Council. Copyright: Copyright 2008 Elsevier B.V., All rights reserved.

PY - 2002/7

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N2 - The O-glycans that decorate mucin glycoproteins contribute to the biophysical and biochemical properties of these molecules and hence their function as a barrier and lubricant on epithelial surfaces. Alterations in mucln O-glycosylation in certain diseases may contribute to pathology. It is known that both the host cell type and the amino acid sequence of the mucin tandem repeat contribute to the O-glycosylation of a mucin molecule. We expressed an epitope-tagged MUC1 mucin cDNA construct in the airway cell line 16HBE14o- and the colon carcinoma cell line Caco2 and used Fast Atom Bombardment Mass Spectrometry to evaluate the contribution of the host cell to differences in O-glycosylation of a single mucin. Many of the glycans detected on the MUC1 mucin were common to both cell types, as would be predicted from biosynthetic constraints. However, MUC1 synthesized in the airway cell line showed comparatively low levels of sialylation but carried a range of oligo-N-acetyllactosamine structures that were not seen in the colon carcinoma cell line.

AB - The O-glycans that decorate mucin glycoproteins contribute to the biophysical and biochemical properties of these molecules and hence their function as a barrier and lubricant on epithelial surfaces. Alterations in mucln O-glycosylation in certain diseases may contribute to pathology. It is known that both the host cell type and the amino acid sequence of the mucin tandem repeat contribute to the O-glycosylation of a mucin molecule. We expressed an epitope-tagged MUC1 mucin cDNA construct in the airway cell line 16HBE14o- and the colon carcinoma cell line Caco2 and used Fast Atom Bombardment Mass Spectrometry to evaluate the contribution of the host cell to differences in O-glycosylation of a single mucin. Many of the glycans detected on the MUC1 mucin were common to both cell types, as would be predicted from biosynthetic constraints. However, MUC1 synthesized in the airway cell line showed comparatively low levels of sialylation but carried a range of oligo-N-acetyllactosamine structures that were not seen in the colon carcinoma cell line.

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In vivo glycosylation of MUC1 in airway epithelial cells

Abstract

Funding

Keywords

ASJC Scopus subject areas

UN SDGs

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