Hiromi Ito1, Hiroyuki Kaji1, Akira Togayachi1, Parastoo Azadi2, Mayumi Ishihara2, Rudolf Geyer3, Christina Galuska3, Hildegard Geyer3, Kazuaki Kakehi4, Mitsuhiro Kinoshita4, Niclas G Karlsson5, Chunsheng Jin5, Koichi Kato6, Hirokazu Yagi6, Sachiko Kondo6, Nana Kawasaki7, Noritaka Hashii7, Daniel Kolarich8, Kathrin Stavenhagen8, Nicolle H Packer9, Morten Thaysen-Andersen9, Miyako Nakano9, Naoyuki Taniguchi10, Ayako Kurimoto10, Yoshinao Wada11, Michiko Tajiri11, Pengyuan Yang12, Weiqian Cao12, Hong Li12, Pauline M Rudd13, Hisashi Narimatsu1. 1. National Institute of Advanced Industrial Science and Technology (AIST), Tsukuba 305-8568, Japan. 2. Complex Carbohydrate Research Center, Department of Biochemistry and Molecular Biology, University of Georgia, Athens 30602, USA. 3. Institute of Biochemistry, Faculty of Medicine, University of Giessen, Giessen D-35392, Germany. 4. Department of Pharmaceutical Sciences, Faculty of Pharmacy, Kinki University, Osaka 577-8502, Japan. 5. Department of Medical Biochemistry and Cell Biology, Institute of Biomedicine, Sahlgrenska Academy, University of Gothenburg, Gothenburg 40530, Sweden. 6. Graduate School of Pharmaceutical Sciences, Nagoya City University, Nagoya 467-8603, Japan. 7. Division of Biological Chemistry and Biologicals, National Institute of Health Sciences, Tokyo 158-8501, Japan. 8. Department of Biomolecular Systems, Max Planck Institute of Colloids and Interfaces, Potsdam D-14424, Germany. 9. Department of Chemistry and Biomolecular Sciences, Macquarie University, Sydney 2109, Australia. 10. Disease Glycomics Team, RIKEN, Saitama 351-0198, Japan. 11. Osaka Medical Center and Research Institute for Maternal and Child Health, Osaka 594-1101, Japan. 12. Department of Chemistry and Institutes of Biomedical Sciences, Fudan University, Shanghai 200433, China. 13. National Institute for Bioprocessing Research and Training (NIBRT), Dublin, Ireland.
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.
The n class="Species">Human Disease Glycomics/Proteome Initiative (HGPI) is an activity in the n>n class="Species">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.
Entities:
Keywords:
Glycoproteomics; Human disease glycomics/proteome initiative (HGPI); Human proteome organization (HUPO)
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