Comparison of methods for profiling O-glycosylation: Human proteome organisation human disease glycomics/proteome initiative multi-institutional study of IgA1

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 Karlsson, Catherine E. Hayes, Koichi Kato, Nana Kawasaki, Kay Hooi Khoo, Kunihiko Kobayashi, Daniel KolarichAkihiro Kondo, Carlito B 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

Research output: Contribution to journalArticle

111 Scopus citations

Abstract

The Human Proteome Organisation Human Disease Glycomics/Proteome Initiative recently coordinated a multiinstitutional 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.

Original languageEnglish (US)
Pages (from-to)719-727
Number of pages9
JournalMolecular and Cellular Proteomics
Volume9
Issue number4
DOIs
StatePublished - Apr 2010

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Analytical Chemistry

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    Wada, Y., Dell, A., Haslam, S. M., Tissot, B., Canis, K., Azadi, P., Bäckström, M., Costello, C. E., Hansson, G. C., Hiki, Y., Ishihara, M., Ito, H., Kakehi, K., Karlsson, N., Hayes, C. E., Kato, K., Kawasaki, N., Khoo, K. H., Kobayashi, K., ... Taniguchi, N. (2010). Comparison of methods for profiling O-glycosylation: Human proteome organisation human disease glycomics/proteome initiative multi-institutional study of IgA1. Molecular and Cellular Proteomics, 9(4), 719-727. https://doi.org/10.1074/mcp.M900450-MCP200