Comparison of the methods for profiling glycoprotein glycans--HUPO Human Disease Glycomics/Proteome Initiative multi-institutional study.
Yoshinao Wada,Parastoo Azadi,Catherine E. Costello,Anne Dell,Raymond A. Dwek,Hildegard Geyer,Rudolf Geyer,Kazuaki Kakehi,Niclas G. Karlsson,Koichi Kato,Nana Kawasaki,Kay-Hooi Khoo,Soo Hyun Kim,Akihiro Kondo,Erika Lattova,Yehia Mechref,Eiji Miyoshi,Kazuyuki Nakamura,Hisashi Narimatsu,Milos V. Novotny,Nicolle H. Packer,Hélène Perreault,Jasna Peter-Katalinić,Gottfried Pohlentz,Vernon N. Reinhold,Pauline M. Rudd,Pauline M. Rudd,Akemi Suzuki,Naoyuki Taniguchi +28 more
TLDR
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.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.read more
Citations
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Journal ArticleDOI
A systematic approach to protein glycosylation analysis: a path through the maze
TL;DR: Some of the major technologies routinely used for structural N- and O-glycan analysis are introduced, describing the complementary information that each provides.
Journal ArticleDOI
HPLC-based analysis of serum N-glycans on a 96-well plate platform with dedicated database software.
Louise Royle,Matthew Campbell,Matthew Campbell,Catherine M. Radcliffe,Catherine M. Radcliffe,Dawn M. White,David Harvey,Jodie L. Abrahams,Yun-Gon Kim,George Henry,Nancy A. Shadick,Michael E. Weinblatt,David M. Lee,Pauline M. Rudd,Pauline M. Rudd,Raymond A. Dwek +15 more
TL;DR: A robust, fully automatable technology platform that includes computer software for the detailed analysis of low femtomoles of N-linked sugars released from glycoproteins is presented, allowing optimization of production conditions and its application to rheumatoid arthritis is demonstrated.
Journal ArticleDOI
Glycan labeling strategies and their use in identification and quantification
TL;DR: Many glycan labels serve as a linker for oligosaccharide attachment to surfaces or carrier proteins, thereby allowing interaction studies with carbohydrate-binding proteins and supporting detailed structural characterization by (tandem) mass spectrometry.
Journal ArticleDOI
High Throughput Isolation and Glycosylation Analysis of IgG–Variability and Heritability of the IgG Glycome in Three Isolated Human Populations
Maja Pučić,Ana Knezevic,Jana Vidič,Barbara Adamczyk,Mislav Novokmet,Ozren Polasek,Olga Gornik,Sandra Supraha-Goreta,Mark R. Wormald,Irma Redzic,Harry Campbell,Alan F. Wright,Nicholas D. Hastie,James F. Wilson,Igor Rudan,Manfred Wuhrer,Pauline M. Rudd,Djuro Josic,Djuro Josic,Gordan Lauc +19 more
TL;DR: The majority of the structural features of the IgG glycome were consistent with previous studies, but sialylation was somewhat higher than reported previously, indicating that the final glycan structures are not a simple result of competing enzymatic activities, but a carefully regulated outcome designed to meet the prevailing physiological needs.
Journal ArticleDOI
Structural analysis of N - and O -glycans released from glycoproteins
TL;DR: This method can be used in conjunction with the analysis of enriched glycopeptides by capillary/nanoLC-ESI-MS/MS, which together provide detailed information regarding the site heterogeneity of glycosylation.
References
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