Comparison of the methods for profiling glycoprotein glycans—HUPO Human Disease Glycomics/Proteome Initiative multi-institutional study

Yoshinao Wada(Osaka International Cancer Institute), Parastoo Azadi(University of Georgia), Catherine E. Costello(Boston University), Anne Dell(Imperial College London), Raymond A. Dwek(University of Oxford), Hildegard Geyer(Justus-Liebig-Universität Gießen), Rudolf Geyer(Justus-Liebig-Universität Gießen), Kazuaki Kakehi(Kindai University), Niclas G. Karlsson(Ollscoil na Gaillimhe – University of Galway), Koichi Kato(Nagoya City University), Nana Kawasaki(National Institute of Health Sciences), Kay‐Hooi Khoo(Institute of Biological Chemistry, Academia Sinica), Soohyun Kim(Korea Basic Science Institute), Akihiro Kondo, Erika Lattová(The University of Osaka), Yehia Mechref(Indiana University Bloomington), Eiji Miyoshi(The University of Osaka), Kazuyuki Nakamura(Yamaguchi University), Hisashi Narimatsu(National Institute of Advanced Industrial Science and Technology), Miloš V. Novotný(University of Münster), Nicolle H. Packer, Hélène Perreault(University of Manitoba), Jasna Peter‐Katalinić(University of Münster), Gottfried Pohlentz(University of Münster), Vernon N. Reinhold(University of New Hampshire), Pauline M. Rudd(University College Dublin), Akemi Suzuki(RIKEN), Naoyuki Taniguchi(The University of Osaka)
Glycobiology
January 12, 2007
10.1093/glycob/cwl086
Cited by 396Open Access
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Abstract

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 Human Proteome Organisation (HUPO) Human Disease Glycomics/Proteome Initiative (HGPI), 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 nano LC/ESI MS/MS or MALDI MS demonstrated 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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