TY - JOUR
T1 - Comparison of the methods for profiling glycoprotein glycans - HUPO human disease glycomics/proteome initiative multi-institutional study
AU - Wada, Yoshinao
AU - Azadi, Parastoo
AU - Costello, Catherine E.
AU - Dell, Anne
AU - Dwek, Raymond A.
AU - Geyer, Hildegard
AU - Geyer, Rudolf
AU - Kakehi, Kazuaki
AU - Karlsson, Niclas G.
AU - Kato, Koichi
AU - Kawasaki, Nana
AU - Khoo, Kay Hooi
AU - Kim, Soohyun
AU - Kondo, Akihiro
AU - Lattova, Erika
AU - Mechref, Yehia
AU - Miyoshi, Eiji
AU - Nakamura, Kazuyuki
AU - Narimatsu, Hisashi
AU - Novotny, Milos V.
AU - Packer, Nicolle H.
AU - Perreault, Hélène
AU - Peter-Katalinić, Jasna
AU - Pohlentz, Gottfried
AU - Reinhold, Vernon N.
AU - Rudd, Pauline M.
AU - Suzuki, Akemi
AU - Taniguchi, Naoyuki
N1 - An erratum for this article exists and can be found in Glycobiology, vol. 17, issue 5, p.10G. DOI: 10.1093/glycob/cwm041
PY - 2007/4
Y1 - 2007/4
N2 - Mass spectrometry (MS) of glycoproteins is an emerging field in proteomics, poised to meet the technical demand for elucidation of the structural complexity and functions of the oligosaccharide components of molecules. Considering the divergence of the mass spectrometric methods employed for oligosaccharide analysis in recent publications, it is necessary to establish technical standards and demonstrate capabilities. In the present study of the Human Proteome Organisation (HUPO) Human Disease Glycomics/Proteome Initiative (HGPI), the same samples of transferrin and immunoglobulin-G were analyzed for N -linked oligosaccharides and their relative abundances in 20 laboratories, and the chromatographic and mass spectrometric analysis results were evaluated. In general, matrix-assisted laser desorption/ionization (MALDI) time-of-flight MS of permethylated oligosaccharide mixtures carried out in six laboratories yielded good quantitation, and the results can be correlated to those of chromatography of reductive amination derivatives. For underivatized oligosaccharide alditols, graphitized carbon-liquid chromatography (LC)/electrospray ionization (ESI) MS detecting deprotonated molecules in the negative ion mode provided acceptable quantitation. The variance of the results among these three methods was small. Detailed analyses of tryptic glycopeptides employing either nano LC/ESI MS/MS or MALDI MS demonstrated excellent capability to determine site-specific or subclass-specific glycan profiles in these samples. Taking into account the variety of MS technologies and options for distinct protocols used in this study, the results of this multi-institutional study indicate that MS-based analysis appears as the efficient method for identification and quantitation of oligosaccharides in glycomic studies and endorse the power of MS for glycopeptide characterization with high sensitivity in proteomic programs.
AB - Mass spectrometry (MS) of glycoproteins is an emerging field in proteomics, poised to meet the technical demand for elucidation of the structural complexity and functions of the oligosaccharide components of molecules. Considering the divergence of the mass spectrometric methods employed for oligosaccharide analysis in recent publications, it is necessary to establish technical standards and demonstrate capabilities. In the present study of the Human Proteome Organisation (HUPO) Human Disease Glycomics/Proteome Initiative (HGPI), the same samples of transferrin and immunoglobulin-G were analyzed for N -linked oligosaccharides and their relative abundances in 20 laboratories, and the chromatographic and mass spectrometric analysis results were evaluated. In general, matrix-assisted laser desorption/ionization (MALDI) time-of-flight MS of permethylated oligosaccharide mixtures carried out in six laboratories yielded good quantitation, and the results can be correlated to those of chromatography of reductive amination derivatives. For underivatized oligosaccharide alditols, graphitized carbon-liquid chromatography (LC)/electrospray ionization (ESI) MS detecting deprotonated molecules in the negative ion mode provided acceptable quantitation. The variance of the results among these three methods was small. Detailed analyses of tryptic glycopeptides employing either nano LC/ESI MS/MS or MALDI MS demonstrated excellent capability to determine site-specific or subclass-specific glycan profiles in these samples. Taking into account the variety of MS technologies and options for distinct protocols used in this study, the results of this multi-institutional study indicate that MS-based analysis appears as the efficient method for identification and quantitation of oligosaccharides in glycomic studies and endorse the power of MS for glycopeptide characterization with high sensitivity in proteomic programs.
UR - http://www.scopus.com/inward/record.url?scp=33947192955&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/record.url?scp=34447316424&partnerID=8YFLogxK
UR - https://doi.org/10.1093/glycob/cwm041
U2 - 10.1093/glycob/cwl086
DO - 10.1093/glycob/cwl086
M3 - Article
C2 - 17223647
AN - SCOPUS:33947192955
SN - 0959-6658
VL - 17
SP - 411
EP - 422
JO - Glycobiology
JF - Glycobiology
IS - 4
ER -