Comparison of Methods for Profiling O-Glycosylation HUMAN PROTEOME ORGANISATION HUMAN DISEASE GLYCOMICS/PROTEOME INITIATIVE MULTI-INSTITUTIONAL STUDY OF IgA1

被引:119
作者
Wada, Yoshinao [1 ,2 ]
Dell, Anne [3 ]
Haslam, Stuart M. [3 ]
Tissot, Berangere [3 ]
Canis, Kevin [3 ]
Azadi, Parastoo [4 ]
Backstrom, Malin [5 ]
Costello, Catherine E. [6 ]
Hansson, Gunnar C. [5 ]
Hiki, Yoshiyuki [7 ]
Ishihara, Mayumi [4 ]
Ito, Hiromi [8 ]
Kakehi, Kazuaki [9 ]
Karlsson, Niclas [10 ]
Hayes, Catherine E. [10 ]
Kato, Koichi [11 ,12 ,13 ]
Kawasaki, Nana [14 ]
Khoo, Kay-Hooi [15 ]
Kobayashi, Kunihiko [16 ]
Kolarich, Daniel [17 ]
Kondo, Akihiro [18 ]
Lebrilla, Carlito [20 ]
Nakano, Miyako [17 ]
Narimatsu, Hisashi [8 ]
Novak, Jan [21 ]
Novotny, Milos V. [22 ]
Ohno, Erina [13 ]
Packer, Nicolle H. [17 ]
Palaima, Elizabeth [6 ]
Renfrow, Matthew B. [21 ]
Tajiri, Michiko [1 ,2 ,23 ]
Thomsson, Kristina A. [5 ]
Yagi, Hirokazu [13 ]
Yu, Shin-Yi [15 ]
Taniguchi, Naoyuki [19 ,24 ,25 ]
机构
[1] Osaka Med Ctr, Izumi Ku, Osaka 5941101, Japan
[2] Res Inst Maternal & Child Hlth, Izumi Ku, Osaka 5941101, Japan
[3] Univ London Imperial Coll Sci Technol & Med, Dept Life Sci, Div Mol Biosci, London SW7 2AZ, England
[4] Univ Georgia, Complex Carbohydrate Res Ctr, Analyt Serv, Athens, GA 30602 USA
[5] Univ Gothenburg, Dept Med Biochem, S-40530 Gothenburg, Sweden
[6] Boston Univ, Sch Med, Dept Biochem, Boston, MA 02118 USA
[7] Fujita Hlth Univ, Sch Med, Dept Internal Med, Aichi 4701192, Japan
[8] Natl Inst Adv Ind Sci & Technol, Res Ctr Med Glycosci, Tsukuba, Ibaraki 3058568, Japan
[9] Kinki Univ, Fac Pharmaceut Sci, Osaka 5778502, Japan
[10] Natl Univ Ireland, Dept Chem, Galway 091756650, Ireland
[11] Natl Inst Nat Sci, Inst Mol Sci, Okazaki, Aichi 4448585, Japan
[12] Natl Inst Nat Sci, Okazaki Inst Integrat Biosci, Okazaki, Aichi 4448585, Japan
[13] Nagoya City Univ, Grad Sch Pharmaceut Sci, Nagoya, Aichi 4678603, Japan
[14] Natl Inst Hlth Sci, Div Biol Chem & Biol, Tokyo 1588501, Japan
[15] Acad Sinica, Natl Res Program Genom Med Core Facil Prote & Gly, Inst Biol Chem, Taipei 115, Taiwan
[16] Hokkaido Univ, Grad Sch Med, Dept Pediat, Sapporo, Hokkaido 0608638, Japan
[17] Macquarie Univ, Dept Chem & Biomol Sci, Sydney, NSW 2109, Australia
[18] Osaka Univ, Grad Sch Med, Div Hlth Sci, Lab Mol Diagnost & Informat, Suita, Osaka 5650871, Japan
[19] Osaka Univ, Grad Sch Med, Dept Biochem, Suita, Osaka 5650871, Japan
[20] Univ Calif Davis, Dept Chem, Davis, CA 95616 USA
[21] Univ Alabama, Dept Microbiol & Biochem & Mol Genet, Birmingham, AL 35294 USA
[22] Indiana Univ, Dept Chem, Bloomington, IN 47405 USA
[23] Japan Sci & Technol Agcy, Kawaguchi, Saitama 3320012, Japan
[24] Osaka Univ, Inst Sci & Ind Res, Osaka 5670047, Japan
[25] RIKEN, Adv Sci Inst, Dis Glyc Team, Syst Glycobiol Grp, Wako, Saitama 3510198, Japan
基金
英国生物技术与生命科学研究理事会; 日本学术振兴会; 瑞典研究理事会; 美国国家卫生研究院;
关键词
ELECTRON-CAPTURE DISSOCIATION; RESONANCE MASS-SPECTROMETRY; HUMAN SERUM IGA1; HINGE REGION; NEPHROPATHY; HETEROGENEITY; GLYCANS; IMMUNOGLOBULIN; ANTIBODIES; PEPTIDES;
D O I
10.1074/mcp.M900450-MCP200
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
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. Molecular & Cellular Proteomics 9: 719-727, 2010.
引用
收藏
页码:719 / 727
页数:9
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