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Glycobiology Advance Access originally published online on February 6, 2008
Glycobiology 2008 18(5):353-366; doi:10.1093/glycob/cwn010
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© The Author 2008. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org

Differentiating N-linked glycan structural isomers in metastatic and nonmetastatic tumor cells using sequential mass spectrometry

Justin M. Prien2, Leanne C. Huysentruyt4, David J. Ashline2, Anthony J. Lapadula2,3, Thomas N. Seyfried4 and Vernon N. Reinhold1,2

2 Division of Molecular, Cellular, and Biomedical Sciences, The Glycomics Center
3 Department of Computer Science, University of New Hampshire, Durham, NH 03824
4 Department of Biology, Boston College, Chestnut Hill, MA 02467, USA

1 To whom correspondence should be addressed: e-mail: vnr{at}unh.edu

Received on January 13, 2008; accepted on February 1, 2008

In an effort to understand the role of molecular glycosylation in cancer a murine model has been used to characterize and fingerprint malignancies in established cell lines that manifest all the hallmarks of metastatic disease: spontaneous development, local invasion, intravasation, immune system survival, extravasation, and secondary tumor formation involving liver, kidney, spleen, lung, and brain. Using astrocyte cell controls, we compared N-linked glycosylation from a nonmetastatic brain tumor cell line and two different metastatic brain tumor cells. Selected ions in each profile were disassembled by ion trap mass spectrometry (MSn) which exhibited multiple structural differences between each tissue. These unique structures were identified within isomeric compositions as pendant nonreducing termini of di- and trisaccharide fragments, probably transparent to a tandem MS approach but distinctively not to sequential ion trap MSn detection.

Key words: Biomarker / carbohydrate / isomer / malignancy / oligosaccharide


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