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Glycobiology Advance Access published online on June 22, 2005
Glycobiology, doi:10.1093/glycob/cwi099
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© The Author 2005. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oupjournals.org
Received May 3, 2005
Revised June 19, 2005
Accepted June 19, 2005

Article

Transmembrane and secreted MUC1 probes show trafficking-dependent changes in O-glycan core profiles

Katja Engelmann 1, Carol L. Kinlough 2, Stefan Müller 1, Hani Razawi 1, Stephan E. Baldus 3, Rebecca P. Hughey 2, and Franz-Georg Hanisch 1*

1 Center of Biochemistry, Medical Faculty, and Center of Molecular Medicine (CMMC), University of Cologne, Joseph-Stelzmann-Str. 52, 50931 Köln, Germany
2 Department of Medicine, Renal-Electrolyte Division, University of Pittsburgh School of Medicine, Pittsburgh, PA 15213, USA
3 Institute of Pathology, Medical Faculty, University of Cologne, Joseph-Stelzmann-Str. 9, 50931 Köln, Germany

* To whom correspondence should be addressed.
Franz-Georg Hanisch, E-mail: franz.hanisch{at}uni-koeln.de


  Abstract

The human mucin MUC1 is expressed both as a transmembrane heterodimeric protein complex that recycles via the trans-Golgi network, and as a secreted isoform. To determine whether differences in cellular trafficking might influence the O-glycosylation profiles on these isoforms we developed a model system consisting of membrane-bound and secretory recombinant glycosylation probes. Secretory MUC1-S contains only a truncated repeat domain, while in MUC1-M constructs this domain is attached to the native transmembrane and cytoplasmic domains of MUC1 either directly (M0) or via an intermitting non-functional (M1) or functional sperm protein-enterokinase-agrin (SEA) module (M2); the SEA module contains a putative proteolytic cleavage site and is associated with proteins receiving extensive O-glycosylation. We showed that MUC1-M2 simulates endogenous MUC1 by recycling from the cell surface of CHO mutant ldlD14 cells through intracellular compartments where its glycosylation continues. The profiles of O-linked glycans on MUC1-S secreted by epithelial EBNA-293 and MCF-7 breast cancer cells revealed patterns dominated by core2-based oligosaccharides. In contrast, the respective membrane-shed probes expressed in the same cells showed a complete shift to patterns dominated by sialyl core1. In conclusion, glycan core profiles reflected the subcellular trafficking pathways of the secretory or membraneous probes and the modifying activities of the resident glycosyltransferases.

Keywords: MUC1/O-glycosylation/mass spectrometry/trafficking/transmembrane protein.
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