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Comparison of methods for profiling O-glycosylation: Human Proteome Organisation Human Disease Glycomics/Proteome Initiative multi-institutional study of IgA1.

Journal article
Authors Yoshinao Wada
Anne Dell
Stuart M Haslam
Bérangère Tissot
Kévin Canis
Parastoo Azadi
Malin Bäckström
Catherine E Costello
Gunnar C. Hansson
Yoshiyuki Hiki
Mayumi Ishihara
Hiromi Ito
Kazuaki Kakehi
Niclas G. Karlsson
C E Hayes
Koichi Kato
Nana Kawasaki
Kay-Hooi Khoo
Kunihiko Kobayashi
Daniel Kolarich
Akihiro Kondo
Carlito Lebrilla
Miyako Nakano
Hisashi Narimatsu
Jan Novak
Milos V Novotny
Erina Ohno
Nicolle H Packer
Elizabeth Palaima
Matthew B Renfrow
Michiko Tajiri
Kristina A Thomsson
Hirokazu Yagi
Shin-Yi Yu
Naoyuki Taniguchi
Published in Molecular & cellular proteomics
Volume 9
Issue 4
Pages 719-727
ISSN 1535-9484
Publication year 2010
Published at Institute of Biomedicine, Department of Medical Biochemistry and Cell Biology
Pages 719-727
Language en
Keywords Algorithms, Carbohydrate Sequence, Disease, etiology, Glycomics, methods, organization & administration, standards, Glycoproteins, chemistry, Glycosylation, Humans, Immunoglobulin A, analysis, chemistry, metabolism, Metabolome, Models, Biological, Polysaccharides, chemistry, Proteome, analysis, metabolism, Proteomics, methods, organization & administration, standards, Societies, Scientific, organization & administration
Subject categories Medical Biotechnology (with a focus on Cell Biology (including Stem Cell Biology), Molecular Biology, Microbiology, Biochemistry or Biopharmacy)


The Human Proteome Organisation Human Disease Glycomics/Proteome Initiative recently coordinated a multi-institutional study that evaluated methodologies that are widely used for defining the N-glycan content in glycoproteins. The study convincingly endorsed mass spectrometry as the technique of choice for glycomic profiling in the discovery phase of diagnostic research. The present study reports the extension of the Human Disease Glycomics/Proteome Initiative's activities to an assessment of the methodologies currently used for O-glycan analysis. Three samples of IgA1 isolated from the serum of patients with multiple myeloma were distributed to 15 laboratories worldwide for O-glycomics analysis. A variety of mass spectrometric and chromatographic procedures representative of current methodologies were used. Similar to the previous N-glycan study, the results convincingly confirmed the pre-eminent performance of MS for O-glycan profiling. Two general strategies were found to give the most reliable data, namely direct MS analysis of mixtures of permethylated reduced glycans in the positive ion mode and analysis of native reduced glycans in the negative ion mode using LC-MS approaches. In addition, mass spectrometric methodologies to analyze O-glycopeptides were also successful.

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