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

Journal article
Authors H. Ito
H. Kaji
A. Togayachi
P. Azadi
M. Ishihara
R. Geyer
C. Galuska
H. Geyer
K. Kakehi
M. Kinoshita
Niclas G. Karlsson
Chunsheng S. Jin
K. Kato
H. Yagi
S. Kondo
N. Kawasaki
N. Hashii
D. Kolarich
K. Stavenhagen
N. H. Packer
M. Thaysen-Andersen
M. Nakano
N. Taniguchi
A. Kurimoto
Y. Wada
M. Tajiri
P. Y. Yang
W. Q. Cao
H. Li
P. M. Rudd
H. Narimatsu
Published in Glycoconjugate Journal
Volume 33
Issue 3
Pages 405-415
ISSN 0282-0080
Publication year 2016
Published at Institute of Biomedicine, Department of Medical Biochemistry and Cell Biology
Pages 405-415
Language en
Links dx.doi.org/10.1007/s10719-015-9625-...
Keywords Human proteome organization (HUPO), Human disease glycomics/proteome initiative (HGPI), Glycoproteomics, lc-esi-ms, human-disease, glycosylation analysis, protein glycosylation, glycomics experiment, mass-spectrometry, breast-carcinoma, immunoglobulin-g, ovarian-cancer, golgi ph
Subject categories Biochemistry and Molecular Biology, Cell Biology

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.

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