Glycobiology Advance Access published online on January 12, 2007
Glycobiology, doi:10.1093/glycob/cwl086
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Comparison of the Methods for Profiling Glycoprotein Glycans: HUPO HGPI (Human Proteome Organisation Human Disease Glycomics/Proteome Initiative) Multi-institutional Study
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1 Osaka Medical Center and Research Institute for Maternal and Child Health, 840 Murodo-cho, Izumi, Osaka 594-1101, Japan
2 Complex Carbohydrate Research Center, University of Georgia, 315 Riverbend Road, Athens, GA 30602-4712 USA
3 Mass Spectrometry Resource, Department of Biochemistry, Boston University School of Medicine, 670 Albany Street, Boston, MA 02118-2646, USA
4 Division of Molecular Biosciences, Imperial College, London SW7 2AZ, UK
5 Oxford Glycobiology Institute, Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK
6 Institute of Biochemistry, University of Giessen, Friedrichstrasse 24, D-35392 Giessen, Germany
7 Faculty of Pharmaceutical Sciences, Kinki University, Kowakae 3-4-1, Higashiosaka-shi, Osaka 577-8502, Japan
8 Proteome Systems Limited, Unit 1, 35-41 Waterloo Road, North Ryde, Sydney, NSW 2113, Australia
9 Chemistry Department, National University Ireland-Galway, Galway, Ireland
10 Graduate School of Pharmaceutical Sciences, Nagoya City University, 3-1 Tanabe-dori, Mizuho-ku, Nagoya 467-8603, Japan
11 Division of Biological Chemistry and Biologicals, National Institute of Health Sciences, 1-18-1 Kami-yoga, Setagaya-Ku, Tokyo 158-8501, Japan
12 Institute of Biological Chemistry, Academia Sinica, Taipei 115, Taiwan
13 Glycomics Team, Korea Basic Science Institute, 52 Eoun-dong, Daejeon 305-333, Korea
14 Department of Glycotherapeutics, Osaka University Graduate School of Medicine, Osaka 565-0871, Japan
15 Department of Chemistry, University of Manitoba, Winnipeg, Manitoba R3T 2N2, Canada
16 Department of Chemistry, Indiana University, Bloomington, IN 47405, USA
17 Department of Biochemistry, Osaka University Graduate School of Medicine, Osaka 565-0871, Japan
18 Department of Biochemistry and Biomolecular Recognition, Yamaguchi University School of Medicine, Minami-Kogushi, Ube, Yamaguchi 755-8505, Japan
19 Research Center for Glycoscience (RCG), National Institute of Advanced Industrial Science and Technology (AIST), Open Space Laboratory Central-2, 1-1-1 Umezono, Tsukuba, Ibaraki 305-8568, Japan
20 Institute for Medical Physics and Biophysics University of Münster, Robert-Koch-Str. 31 D-48149, Münster, Germany
21 Department of Chemistry, University of New Hampshire, Durham, New Hampshire 03824, USA
22 NIBRT, Conway Institute, University College Dublin, Belfield, Dublin 4, Ireland
23 RIKEN Frontier Research System, 2-1 Hirosawa, Wako-shi, Saitama, 351-0198, Japan
24 Department of Disease Glycomics, Research Institute for Microbial Diseases, Osaka University, Osaka 565-0871, Japan
Received on October 27, 2006; revised on December 25, 2006; accepted on January 2, 2007
Mass spectrometry (MS) of glycoproteins is an emerging field in proteomics, poised to meet the technical demand for elucidation of the structural complexity and functions of the oligosaccharide components of molecules. Considering the divergence of the mass spectrometric methods employed for oligosaccharide analysis in recent publications, it is necessary to establish technical standards and demonstrate capabilities. In the present study of the HUPO HGPI (Human Proteome Organisation Human Disease Glycomics/Proteome Initiative), the same samples of transferrin and immunoglobulin-G were analyzed for N-linked oligosaccharides and their relative abundances in 20 laboratories, and the chromatographic and mass spectrometric analysis results were evaluated. In general, matrix-assisted laser desorption/ionization (MALDI) time-of-flight MS of permethylated oligosaccharide mixtures carried out in six laboratories yielded good quantitation, and the results can be correlated to those of chromatography of reductive amination derivatives. For underivatized oligosaccharide alditols, graphitized carbon-liquid chromatography (LC)/electrospray ionization (ESI) MS detecting deprotonated molecules in the negative ion mode provided acceptable quantitation. The variance of the results among these three methods was small. Detailed analyses of tryptic glycopeptides employing either nanoLC/ESI MS/MS or MALDI MS demonstrated the excellent capability to determine site-specific or subclass-specific glycan profiles in these samples. Taking into account the variety of MS technologies and options for distinct protocols used in this study, the results of this multi-institutional study indicate that MS-based analysis appears as the efficient method for identification and quantitation of oligosaccharides in glycomic studies and endorse the power of MS for glycopeptide characterization with high sensitivity in proteomic programs.
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