Comparison of analytical methods for profiling N- and O-linked glycans from cultured cell lines View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2015-10-28

AUTHORS

Hiromi Ito, Hiroyuki Kaji, Akira Togayachi, Parastoo Azadi, Mayumi Ishihara, Rudolf Geyer, Christina Galuska, Hildegard Geyer, Kazuaki Kakehi, Mitsuhiro Kinoshita, Niclas G. Karlsson, Chunsheng Jin, Koichi Kato, Hirokazu Yagi, Sachiko Kondo, Nana Kawasaki, Noritaka Hashii, Daniel Kolarich, Kathrin Stavenhagen, Nicolle H. Packer, Morten Thaysen-Andersen, Miyako Nakano, Naoyuki Taniguchi, Ayako Kurimoto, Yoshinao Wada, Michiko Tajiri, Pengyuan Yang, Weiqian Cao, Hong Li, Pauline M. Rudd, Hisashi Narimatsu

ABSTRACT

The Human Disease Glycomics/Proteome Initiative (HGPI) is an activity in the Human Proteome Organization (HUPO) supported by leading researchers from international institutes and aims at development of disease-related glycomics/glycoproteomics analysis techniques. Since 2004, the initiative has conducted three pilot studies. The first two were N- and O-glycan analyses of purified transferrin and immunoglobulin-G and assessed the most appropriate analytical approach employed at the time. This paper describes the third study, which was conducted to compare different approaches for quantitation of N- and O-linked glycans attached to proteins in crude biological samples. The preliminary analysis on cell pellets resulted in wildly varied glycan profiles, which was probably the consequence of variations in the pre-processing sample preparation methodologies. However, the reproducibility of the data was not improved dramatically in the subsequent analysis on cell lysate fractions prepared in a specified method by one lab. The study demonstrated the difficulty of carrying out a complete analysis of the glycome in crude samples by any single technology and the importance of rigorous optimization of the course of analysis from preprocessing to data interpretation. It suggests that another collaborative study employing the latest technologies in this rapidly evolving field will help to realize the requirements of carrying out the large-scale analysis of glycoproteins in complex cell samples. More... »

PAGES

405-415

References to SciGraph publications

Journal

TITLE

Glycoconjugate Journal

ISSUE

3

VOLUME

33

Author Affiliations

  • Department of Biochemistry, Fukushima Medical University, 960-1295, Fukushima, Japan
  • National Institute of Advanced Industrial Science and Technology (AIST), 305-8568, Tsukuba, Japan
  • Complex Carbohydrate Research Center, Department of Biochemistry and Molecular Biology, University of Georgia, 30602, Athens, USA
  • Institute of Biochemistry, Faculty of Medicine, University of Giessen, D-35392, Giessen, Germany
  • Department of Pharmaceutical Sciences, Faculty of Pharmacy, Kinki University, 577-8502, Osaka, Japan
  • Department of Medical Biochemistry and Cell Biology, Institute of Biomedicine, Sahlgrenska Academy, University of Gothenburg, 40530, Gothenburg, Sweden
  • Graduate School of Pharmaceutical Sciences, Nagoya City University, 467-8603, Nagoya, Japan
  • Graduate School of Medical Life Science, Yokohama City University, 230-0045, Yokohama, Japan
  • Division of Biological Chemistry and Biologicals, National Institute of Health Sciences, 158-8501, Tokyo, Japan
  • Department of Biomolecular Systems, Max Planck Institute of Colloids and Interfaces, D-14424, Potsdam, Germany
  • Department of Molecular Biotechnology, Hiroshima University, 739-8530, Higashi-Hiroshima, Japan
  • Department of Chemistry and Biomolecular Sciences, Macquarie University, 2109, Sydney, Australia
  • Division of BioAnalytical Chemistry, VU University Amsterdam, 1081, Amsterdam, The Netherlands
  • Disease Glycomics Team, RIKEN, 351-0198, Saitama, Japan
  • Osaka Medical Center and Research Institute for Maternal and Child Health, 594-1101, Osaka, Japan
  • Department of Chemistry and Institutes of Biomedical Sciences, Fudan University, 200433, Shanghai, China
  • National Institute for Bioprocessing Research and Training (NIBRT), Dublin, Ireland
  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1007/s10719-015-9625-3

    DOI

    http://dx.doi.org/10.1007/s10719-015-9625-3

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1003995008

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/26511985


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